NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1915223084|dbj|BBV81745|]
View 

dehydrogenase [Enterobacter kobei]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK06128 super family cl32118
SDR family oxidoreductase;
25-293 1.62e-163

SDR family oxidoreductase;


The actual alignment was detected with superfamily member PRK06128:

Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 456.24  E-value: 1.62e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  25 GLASEMQPVPDHGEKSYKGHGRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALIKAEGRKAIA 104
Cdd:PRK06128   31 GTIHEMQPKPDHGEQSYKGFGRLQGRKALITGADSGIGRATAIAFAREGADIALNYLPEEEQDAAEVVQLIQAEGRKAVA 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 105 LPGDIRDETFCQNLVEEAVSKLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINT 184
Cdd:PRK06128  111 LPGDLKDEAFCRQLVERAVKELGGLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPGASIINT 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 185 SSVQAVKPSPVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVE 264
Cdd:PRK06128  191 GSIQSYQPSPTLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSGGQPPEKIPDFGSETPMKRPGQPVE 270
                         250       260
                  ....*....|....*....|....*....
gi 1915223084 265 IAPLYVTLASDACSYTSGQVWCSDGGDGV 293
Cdd:PRK06128  271 MAPLYVLLASQESSYVTGEVFGVTGGLLL 299
 
Name Accession Description Interval E-value
PRK06128 PRK06128
SDR family oxidoreductase;
25-293 1.62e-163

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 456.24  E-value: 1.62e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  25 GLASEMQPVPDHGEKSYKGHGRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALIKAEGRKAIA 104
Cdd:PRK06128   31 GTIHEMQPKPDHGEQSYKGFGRLQGRKALITGADSGIGRATAIAFAREGADIALNYLPEEEQDAAEVVQLIQAEGRKAVA 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 105 LPGDIRDETFCQNLVEEAVSKLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINT 184
Cdd:PRK06128  111 LPGDLKDEAFCRQLVERAVKELGGLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPGASIINT 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 185 SSVQAVKPSPVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVE 264
Cdd:PRK06128  191 GSIQSYQPSPTLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSGGQPPEKIPDFGSETPMKRPGQPVE 270
                         250       260
                  ....*....|....*....|....*....
gi 1915223084 265 IAPLYVTLASDACSYTSGQVWCSDGGDGV 293
Cdd:PRK06128  271 MAPLYVLLASQESSYVTGEVFGVTGGLLL 299
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
25-291 8.10e-153

classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 427.86  E-value: 8.10e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  25 GLASEMQPVPDHGEKSYKGHGRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALIKAEGRKAIA 104
Cdd:cd05355     2 GIEAKMDPLPDFGEKSYKGSGKLKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDAEETKKLIEEEGRKCLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 105 LPGDIRDETFCQNLVEEAVSKLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINT 184
Cdd:cd05355    82 IPGDLGDESFCRDLVKEVVKEFGKLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKGSSIINT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 185 SSVQAVKPSPVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPmEKVKEFGGDTPLGRPGQPVE 264
Cdd:cd05355   162 TSVTAYKGSPHLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIPSSFPE-EKVSEFGSQVPMGRAGQPAE 240
                         250       260
                  ....*....|....*....|....*..
gi 1915223084 265 IAPLYVTLASDACSYTSGQVWCSDGGD 291
Cdd:cd05355   241 VAPAYVFLASQDSSYVTGQVLHVNGGE 267
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
46-290 4.90e-98

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 288.22  E-value: 4.90e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:COG1028     3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEA--LEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:COG1028    81 FGRLDILVNNAGITP-PGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERggGRIVNISSIAGLRGSPGQAAYAASK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQ 283
Cdd:COG1028   160 AAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQ 239

                  ....*..
gi 1915223084 284 VWCSDGG 290
Cdd:COG1028   240 VLAVDGG 246
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
58-290 5.20e-68

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 211.52  E-value: 5.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  58 DSGIGRAVAIAYAREGADVAINYLPEEEKDAAEviALIKAEGRKAIalPGDIRDETFCQNLVEEAVSKLGGLDILINNAG 137
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVVLTDLNEALAKRVE--ELAEELGAAVL--PCDVTDEEQVEALVAAAVEKFGRLDILVNNAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 138 R-QQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLLDYAQTKACLAVFTKSLAKQ 216
Cdd:pfam13561  81 FaPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915223084 217 LGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQVWCSDGG 290
Cdd:pfam13561 161 LGPRGIRVNAISPGPIKTLAASGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGG 234
SDR_subfam_1 TIGR03971
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
47-290 2.35e-51

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274889 [Multi-domain]  Cd Length: 270  Bit Score: 169.57  E-value: 2.35e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVA----------INYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQ 116
Cdd:TIGR03971   1 LEGKVAFITGAARGQGRSHAVRLAEEGADIIavdicadidtVPYPLATPDDLAETVRLVEALGRRIVARQADVRDRAALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 117 NLVEEAVSKLGGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSP 194
Cdd:TIGR03971  81 AAVDAGVAEFGRLDIVVANAGICSI-GPLWELTEEQWDDMIDVNLTGVWNTVKAAAPHMIERggGSIVLTSSTAGLKGGP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 195 VLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPG----------PYWTVLQSSGGQPMEKVKEFGGDTPLGRPG-QPV 263
Cdd:TIGR03971 160 GGAHYVAAKHGVVGLMRSLALELAPHGIRVNAVHPTgvntpmidneAMYRLFRPDLDTPTDAAEAFRSMNALPVPWvEPE 239
                         250       260
                  ....*....|....*....|....*..
gi 1915223084 264 EIAPLYVTLASDACSYTSGQVWCSDGG 290
Cdd:TIGR03971 240 DISNAVLFLASDEARYVTGVTLPVDAG 266
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
53-200 2.24e-09

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 55.57  E-value: 2.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084   53 LITGGDSGIGRAVAIAYAREGADvainYL------PEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGAR----RLvllsrsGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVE 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915223084  127 GGLDILINNAGRQQYReSLEELTTEDFDATFKTNVYApFWITKAALRHLKASSVIInTSSVQAVKPSPVLLDYA 200
Cdd:smart00822  80 GPLTGVIHAAGVLDDG-VLASLTPERFAAVLAPKAAG-AWNLHELTADLPLDFFVL-FSSIAGVLGSPGQANYA 150
 
Name Accession Description Interval E-value
PRK06128 PRK06128
SDR family oxidoreductase;
25-293 1.62e-163

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 456.24  E-value: 1.62e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  25 GLASEMQPVPDHGEKSYKGHGRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALIKAEGRKAIA 104
Cdd:PRK06128   31 GTIHEMQPKPDHGEQSYKGFGRLQGRKALITGADSGIGRATAIAFAREGADIALNYLPEEEQDAAEVVQLIQAEGRKAVA 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 105 LPGDIRDETFCQNLVEEAVSKLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINT 184
Cdd:PRK06128  111 LPGDLKDEAFCRQLVERAVKELGGLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPGASIINT 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 185 SSVQAVKPSPVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVE 264
Cdd:PRK06128  191 GSIQSYQPSPTLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSGGQPPEKIPDFGSETPMKRPGQPVE 270
                         250       260
                  ....*....|....*....|....*....
gi 1915223084 265 IAPLYVTLASDACSYTSGQVWCSDGGDGV 293
Cdd:PRK06128  271 MAPLYVLLASQESSYVTGEVFGVTGGLLL 299
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
25-291 8.10e-153

classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 427.86  E-value: 8.10e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  25 GLASEMQPVPDHGEKSYKGHGRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALIKAEGRKAIA 104
Cdd:cd05355     2 GIEAKMDPLPDFGEKSYKGSGKLKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDAEETKKLIEEEGRKCLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 105 LPGDIRDETFCQNLVEEAVSKLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINT 184
Cdd:cd05355    82 IPGDLGDESFCRDLVKEVVKEFGKLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKGSSIINT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 185 SSVQAVKPSPVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPmEKVKEFGGDTPLGRPGQPVE 264
Cdd:cd05355   162 TSVTAYKGSPHLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIPSSFPE-EKVSEFGSQVPMGRAGQPAE 240
                         250       260
                  ....*....|....*....|....*..
gi 1915223084 265 IAPLYVTLASDACSYTSGQVWCSDGGD 291
Cdd:cd05355   241 VAPAYVFLASQDSSYVTGQVLHVNGGE 267
PRK06701 PRK06701
short chain dehydrogenase; Provisional
25-293 7.65e-132

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 375.53  E-value: 7.65e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  25 GLASEMQPVPDHGEKSYKGHGRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkDAAEVIALIKAEGRKAIA 104
Cdd:PRK06701   22 GIESLMNPLPQFEAPNYKGSGKLKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHE-DANETKQRVEKEGVKCLL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 105 LPGDIRDETFCQNLVEEAVSKLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINT 184
Cdd:PRK06701  101 IPGDVSDEAFCKDAVEETVRELGRLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQGSAIINT 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 185 SSVQAVKPSPVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSgGQPMEKVKEFGGDTPLGRPGQPVE 264
Cdd:PRK06701  181 GSITGYEGNETLIDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLIPS-DFDEEKVSQFGSNTPMQRPGQPEE 259
                         250       260
                  ....*....|....*....|....*....
gi 1915223084 265 IAPLYVTLASDACSYTSGQVWCSDGGDGV 293
Cdd:PRK06701  260 LAPAYVFLASPDSSYITGQMLHVNGGVIV 288
PRK07985 PRK07985
SDR family oxidoreductase;
25-291 7.47e-125

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 358.15  E-value: 7.47e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  25 GLASEMQPVPDHGEKSYKGHGRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALIKAEGRKAIA 104
Cdd:PRK07985   25 GIQAKMTPVPDCGEKTYVGSGRLKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLPVEEEDAQDVKKIIEECGRKAVL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 105 LPGDIRDETFCQNLVEEAVSKLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINT 184
Cdd:PRK07985  105 LPGDLSDEKFARSLVHEAHKALGGLDIMALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKGASIITT 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 185 SSVQAVKPSPVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVE 264
Cdd:PRK07985  185 SSIQAYQPSPHLLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALQISGGQTQDKIPQFGQQTPMKRAGQPAE 264
                         250       260
                  ....*....|....*....|....*..
gi 1915223084 265 IAPLYVTLASDACSYTSGQVWCSDGGD 291
Cdd:PRK07985  265 LAPVYVYLASQESSYVTAEVHGVCGGE 291
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
46-290 4.90e-98

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 288.22  E-value: 4.90e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:COG1028     3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEA--LEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:COG1028    81 FGRLDILVNNAGITP-PGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERggGRIVNISSIAGLRGSPGQAAYAASK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQ 283
Cdd:COG1028   160 AAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQ 239

                  ....*..
gi 1915223084 284 VWCSDGG 290
Cdd:COG1028   240 VLAVDGG 246
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
52-288 3.35e-77

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 234.87  E-value: 3.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAeviALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLDI 131
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAEL---AAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGRQqYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQTKACLAVF 209
Cdd:cd05233    78 LVNNAGIA-RPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKqgGGRIVNISSVAGLRPLPGQAAYAASKAALEGL 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915223084 210 TKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPmEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQVWCSD 288
Cdd:cd05233   157 TRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPE-EAEKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
47-290 4.85e-72

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 221.99  E-value: 4.85e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK05557    3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAG-AEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAG--RqqyRESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK05557   82 GGVDILVNNAGitR---DNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMmkQRSGRIINISSVVGLMGNPGQANYAAS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGqpmEKVKE-FGGDTPLGRPGQPVEIAPLYVTLASDACSYTS 281
Cdd:PRK05557  159 KAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDALP---EDVKEaILAQIPLGRLGQPEEIASAVAFLASDEAAYIT 235

                  ....*....
gi 1915223084 282 GQVWCSDGG 290
Cdd:PRK05557  236 GQTLHVNGG 244
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
58-290 5.20e-68

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 211.52  E-value: 5.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  58 DSGIGRAVAIAYAREGADVAINYLPEEEKDAAEviALIKAEGRKAIalPGDIRDETFCQNLVEEAVSKLGGLDILINNAG 137
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVVLTDLNEALAKRVE--ELAEELGAAVL--PCDVTDEEQVEALVAAAVEKFGRLDILVNNAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 138 R-QQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLLDYAQTKACLAVFTKSLAKQ 216
Cdd:pfam13561  81 FaPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915223084 217 LGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQVWCSDGG 290
Cdd:pfam13561 161 LGPRGIRVNAISPGPIKTLAASGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGG 234
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
47-290 3.18e-66

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 207.62  E-value: 3.18e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:cd05358     1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDA-AEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYRESLEeLTTEDFDATFKTNVYAPFWITKAALRHL---KASSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:cd05358    80 GTLDILVNNAGLQGDASSHE-MTLEDWNKVIDVNLTGQFLCAREAIKRFrksKIKGKIINMSSVHEKIPWPGHVNYAASK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQ 283
Cdd:cd05358   159 GGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQRADLLSLIPMGRIGEPEEIAAAAAWLASDEASYVTGT 238

                  ....*..
gi 1915223084 284 VWCSDGG 290
Cdd:cd05358   239 TLFVDGG 245
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
47-290 3.08e-65

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 204.43  E-value: 3.08e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:cd05362     1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNYASSKAA-AEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYREsLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLLDYAQTKACL 206
Cdd:cd05362    80 GGVDILVNNAGVMLKKP-IAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDGGRIINISSSLTAAYTPNYGAYAGSKAAV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 207 AVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPmEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQVWC 286
Cdd:cd05362   159 EAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGKTE-EAVEGYAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNGQVIR 237

                  ....
gi 1915223084 287 SDGG 290
Cdd:cd05362   238 ANGG 241
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
45-290 4.35e-64

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 201.61  E-value: 4.35e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK05565    1 MKLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEA-AQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK05565   80 KFGKIDILVNNAGISNF-GLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMikRKSGVIVNISSIWGLIGASCEVLYSAS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGpywtVLQSSGGQPMEKVKEFG--GDTPLGRPGQPVEIAPLYVTLASDACSYT 280
Cdd:PRK05565  159 KGAVNAFTKALAKELAPSGIRVNAVAPG----AIDTEMWSSFSEEDKEGlaEEIPLGRLGKPEEIAKVVLFLASDDASYI 234
                         250
                  ....*....|
gi 1915223084 281 SGQVWCSDGG 290
Cdd:PRK05565  235 TGQIITVDGG 244
FabG-like PRK07231
SDR family oxidoreductase;
46-290 7.33e-64

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 201.21  E-value: 7.33e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEekDAAEVIALIKAEGRkAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK07231    2 RLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEE--AAERVAAEILAGGR-AIAVAADVSDEADVEAAVAAALER 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK07231   79 FGSVDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEggGAIVNVASTAGLRPRPGLGWYNASK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSS--GGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTS 281
Cdd:PRK07231  159 GAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAfmGEPTPENRAKFLATIPLGRLGTPEDIANAALFLASDEASWIT 238

                  ....*....
gi 1915223084 282 GQVWCSDGG 290
Cdd:PRK07231  239 GVTLVVDGG 247
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
46-290 1.73e-63

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 200.00  E-value: 1.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK05653    2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEA--AEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK05653   80 FGALDILVNNAGITR-DALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYgrIVNISSVSGVTGNPGQTNYSAAK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGpywtVLQSSGGQPM--EKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTS 281
Cdd:PRK05653  159 AGVIGFTKALALELASRGITVNAVAPG----FIDTDMTEGLpeEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYIT 234

                  ....*....
gi 1915223084 282 GQVWCSDGG 290
Cdd:PRK05653  235 GQVIPVNGG 243
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
50-231 1.26e-62

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 196.30  E-value: 1.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINyLPEEEKdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGL 129
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLV-DRSEEK-LEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPSPVLLDYAQTKACLA 207
Cdd:pfam00106  79 DILVNNAGITG-LGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSggRIVNISSVAGLVPYPGGSAYSASKAAVI 157
                         170       180
                  ....*....|....*....|....
gi 1915223084 208 VFTKSLAKQLGPKGIRVNAVAPGP 231
Cdd:pfam00106 158 GFTRSLALELAPHGIRVNAVAPGG 181
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
50-290 3.52e-61

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 193.92  E-value: 3.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGL 129
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEA--AAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAG--RQQYresLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTKAC 205
Cdd:cd05333    79 DILVNNAGitRDNL---LMRMSEEDWDAVINVNLTGVFNVTQAVIRAMikRRSGRIINISSVVGLIGNPGQANYAASKAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 206 LAVFTKSLAKQLGPKGIRVNAVAPGPYWTvlqssggqPM-----EKVKE-FGGDTPLGRPGQPVEIAPLYVTLASDACSY 279
Cdd:cd05333   156 VIGFTKSLAKELASRGITVNAVAPGFIDT--------DMtdalpEKVKEkILKQIPLGRLGTPEEVANAVAFLASDDASY 227
                         250
                  ....*....|.
gi 1915223084 280 TSGQVWCSDGG 290
Cdd:cd05333   228 ITGQVLHVNGG 238
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
45-294 6.85e-61

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 193.55  E-value: 6.85e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK12825    2 GSLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEE-AAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK12825   81 RFGRIDILVNNAGIFE-DKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGgrIVNISSVAGLPGWPGRSNYAAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGpyWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSG 282
Cdd:PRK12825  160 KAGLVGLTKALARELAEYGITVNMVAPG--DIDTDMKEATIEEAREAKDAETPLGRSGTPEDIARAVAFLCSDASDYITG 237
                         250
                  ....*....|..
gi 1915223084 283 QVWCSDGGDGVI 294
Cdd:PRK12825  238 QVIEVTGGVDVI 249
PRK12939 PRK12939
short chain dehydrogenase; Provisional
47-290 9.62e-59

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 188.26  E-value: 9.62e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK12939    5 LAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAE--ARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:PRK12939   83 GGLDGLVNNAGITN-SKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGrgRIVNLASDTALWGAPKLGAYVASKG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPmEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQV 284
Cdd:PRK12939  162 AVIGMTRSLARELGGRGITVNAIAPGLTATEATAYVPAD-ERHAYYLKGRALERLQVPDDVAGAVLFLLSDAARFVTGQL 240

                  ....*.
gi 1915223084 285 WCSDGG 290
Cdd:PRK12939  241 LPVNGG 246
PRK12826 PRK12826
SDR family oxidoreductase;
45-290 1.55e-58

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 187.82  E-value: 1.55e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEekDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK12826    2 RDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGD--DAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQA-VKPSPVLLDYAQ 201
Cdd:PRK12826   80 DFGRLDILVANAGIFP-LTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGggRIVLTSSVAGpRVGYPGLAHYAA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 202 TKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTvlQSSGGQPMEKVKEFGG-DTPLGRPGQPVEIAPLYVTLASDACSYT 280
Cdd:PRK12826  159 SKAGLVGFTRALALELAARNITVNSVHPGGVDT--PMAGNLGDAQWAEAIAaAIPLGRLGEPEDIAAAVLFLASDEARYI 236
                         250
                  ....*....|
gi 1915223084 281 SGQVWCSDGG 290
Cdd:PRK12826  237 TGQTLPVDGG 246
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
47-290 1.68e-58

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 187.62  E-value: 1.68e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEE-KDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:cd05364     1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERlEETRQSCLQAGVSEKKILLVVADLTEEEGQDRIISTTLAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQqYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS-VIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:cd05364    81 FGRLDILVNNAGIL-AKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKgEIVNVSSVAGGRSFPGVLYYCISKA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDT----PLGRPGQPVEIAPLYVTLASDACSYT 280
Cdd:cd05364   160 ALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRMGMPEEQYIKFLSRAkethPLGRPGTVDEVAEAIAFLASDASSFI 239
                         250
                  ....*....|
gi 1915223084 281 SGQVWCSDGG 290
Cdd:cd05364   240 TGQLLPVDGG 249
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
47-290 3.37e-56

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 181.40  E-value: 3.37e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEviALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:cd05347     3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQ--QLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:cd05347    81 GKIDILVNNAGIIR-RHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMikQGHGKIINICSLLSELGGPPVPAYAASKG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQV 284
Cdd:cd05347   160 GVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVVADPEFNDDILKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQI 239

                  ....*.
gi 1915223084 285 WCSDGG 290
Cdd:cd05347   240 IFVDGG 245
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
49-290 5.82e-55

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 178.62  E-value: 5.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAINylPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGG 128
Cdd:cd05344     1 GKVALVTAASSGIGLAIARALAREGARVAIC--ARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 LDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPSPVLLDYAQTKACL 206
Cdd:cd05344    79 VDILVNNAG-GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwgRIVNISSLTVKEPEPNLVLSNVARAGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 207 AVFTKSLAKQLGPKGIRVNAVAPGPYWT---------VLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDAC 277
Cdd:cd05344   158 IGLVKTLSRELAPDGVTVNSVLPGYIDTervrrlleaRAEKEGISVEEAEKEVASQIPLGRVGKPEELAALIAFLASEKA 237
                         250
                  ....*....|...
gi 1915223084 278 SYTSGQVWCSDGG 290
Cdd:cd05344   238 SYITGQAILVDGG 250
PRK12829 PRK12829
short chain dehydrogenase; Provisional
47-290 1.16e-53

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 175.63  E-value: 1.16e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAeviaLIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK12829    9 LDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAAT----AARLPGAKVTATVADVADPAQVERVFDTAVERF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS---VIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK12829   85 GGLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGhggVIIALSSVAGRLGYPGRTPYAASK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWT-----VLQSSGGQPMEKVKEFGGD----TPLGRPGQPVEIAPLYVTLAS 274
Cdd:PRK12829  165 WAVVGLVKSLAIELGPLGIRVNAILPGIVRGprmrrVIEARAQQLGIGLDEMEQEylekISLGRMVEPEDIAATALFLAS 244
                         250
                  ....*....|....*.
gi 1915223084 275 DACSYTSGQVWCSDGG 290
Cdd:PRK12829  245 PAARYITGQAISVDGN 260
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
47-290 3.24e-53

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 173.93  E-value: 3.24e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAIN-YLPEEEKDAAEVIAliKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:cd05369     1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAgRKPEVLEAAAEEIS--SATGGRAHPIQCDVRDPEAVEAAVDETLKE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS---VIINTSSVQAVKPSPVLLDYAQT 202
Cdd:cd05369    79 FGKIDILINNAA-GNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKhggSILNISATYAYTGSPFQVHSAAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGPY-----WTVLqSSGGQPMEKVKEfggDTPLGRPGQPVEIAPLYVTLASDAC 277
Cdd:cd05369   158 KAGVDALTRSLAVEWGPYGIRVNAIAPGPIpttegMERL-APSGKSEKKMIE---RVPLGRLGTPEEIANLALFLLSDAA 233
                         250
                  ....*....|...
gi 1915223084 278 SYTSGQVWCSDGG 290
Cdd:cd05369   234 SYINGTTLVVDGG 246
PRK12937 PRK12937
short chain dehydrogenase; Provisional
47-290 5.81e-53

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 173.00  E-value: 5.81e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK12937    3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAA-ADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLLDYAQTKACL 206
Cdd:PRK12937   82 GRIDVLVNNAGVMPLG-TIADFDLEDFDRTIATNLRGAFVVLREAARHLGQGGRIINLSTSVIALPLPGYGPYAASKAAV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 207 AVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPmEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQVWC 286
Cdd:PRK12937  161 EGLVHVLANELRGRGITVNAVAPGPVATELFFNGKSA-EQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAWVNGQVLR 239

                  ....
gi 1915223084 287 SDGG 290
Cdd:PRK12937  240 VNGG 243
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
49-290 1.15e-52

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 172.95  E-value: 1.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGG 128
Cdd:cd05366     2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEA-AKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 LDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLK---ASSVIINTSSVQAVKPSPVLLDYAQTKAC 205
Cdd:cd05366    81 FDVMVNNAGIAPI-TPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKklgHGGKIINASSIAGVQGFPNLGAYSASKFA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 206 LAVFTKSLAKQLGPKGIRVNAVAPG----PYW-----TVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDA 276
Cdd:cd05366   160 VRGLTQTAAQELAPKGITVNAYAPGivktEMWdyideEVGEIAGKPEGEGFAEFSSSIPLGRLSEPEDVAGLVSFLASED 239
                         250
                  ....*....|....
gi 1915223084 277 CSYTSGQVWCSDGG 290
Cdd:cd05366   240 SDYITGQTILVDGG 253
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
46-234 1.46e-52

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 172.36  E-value: 1.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEekDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:COG0300     2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAE--RLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:COG0300    80 FGPIDVLVNNAGVGGGG-PFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRArgRGRIVNVSSVAGLRGLPGMAAYAASK 158
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWT 234
Cdd:COG0300   159 AALEGFSESLRAELAPTGVRVTAVCPGPVDT 189
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
47-290 8.94e-52

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 170.68  E-value: 8.94e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK08936    5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEE-EANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYRESlEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV---IINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK08936   84 GTLDVMINNAGIENAVPS-HEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDIkgnIINMSSVHEQIPWPLFVHYAASK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQ 283
Cdd:PRK08936  163 GGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKFADPKQRADVESMIPMGYIGKPEEIAAVAAWLASSEASYVTGI 242

                  ....*..
gi 1915223084 284 VWCSDGG 290
Cdd:PRK08936  243 TLFADGG 249
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
48-275 1.28e-51

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 169.59  E-value: 1.28e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  48 TGKKALITGGDSGIGRAVAIAYAREGADVAINylpeeEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLG 127
Cdd:COG4221     4 KGKVALITGASSGIGAATARALAAAGARVVLA-----ARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 128 GLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQTKAC 205
Cdd:COG4221    79 RLDVLVNNAGVAL-LGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRArgSGHIVNISSIAGLRPYPGGAVYAATKAA 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915223084 206 LAVFTKSLAKQLGPKGIRVNAVAPGPYWT--VLQSSGGQPMEKVKEFGGDTPLgrpgQPVEIAPLYVTLASD 275
Cdd:COG4221   158 VRGLSESLRAELRPTGIRVTVIEPGAVDTefLDSVFDGDAEAAAAVYEGLEPL----TPEDVAEAVLFALTQ 225
SDR_subfam_1 TIGR03971
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
47-290 2.35e-51

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274889 [Multi-domain]  Cd Length: 270  Bit Score: 169.57  E-value: 2.35e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVA----------INYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQ 116
Cdd:TIGR03971   1 LEGKVAFITGAARGQGRSHAVRLAEEGADIIavdicadidtVPYPLATPDDLAETVRLVEALGRRIVARQADVRDRAALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 117 NLVEEAVSKLGGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSP 194
Cdd:TIGR03971  81 AAVDAGVAEFGRLDIVVANAGICSI-GPLWELTEEQWDDMIDVNLTGVWNTVKAAAPHMIERggGSIVLTSSTAGLKGGP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 195 VLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPG----------PYWTVLQSSGGQPMEKVKEFGGDTPLGRPG-QPV 263
Cdd:TIGR03971 160 GGAHYVAAKHGVVGLMRSLALELAPHGIRVNAVHPTgvntpmidneAMYRLFRPDLDTPTDAAEAFRSMNALPVPWvEPE 239
                         250       260
                  ....*....|....*....|....*..
gi 1915223084 264 EIAPLYVTLASDACSYTSGQVWCSDGG 290
Cdd:TIGR03971 240 DISNAVLFLASDEARYVTGVTLPVDAG 266
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
52-293 2.39e-51

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 168.90  E-value: 2.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAINYLPEEekDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLDI 131
Cdd:cd05365     2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSE--GAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSPVLLDYAQTKACLAVF 209
Cdd:cd05365    80 LVNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAggGAILNISSMSSENKNVRIAAYGSSKAAVNHM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 210 TKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKvKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQVWCSDG 289
Cdd:cd05365   160 TRNLAFDLGPKGIRVNAVAPGAVKTDALASVLTPEIE-RAMLKHTPLGRLGEPEDIANAALFLCSPASAWVSGQVLTVSG 238

                  ....
gi 1915223084 290 GDGV 293
Cdd:cd05365   239 GGVQ 242
PRK06947 PRK06947
SDR family oxidoreductase;
50-290 2.26e-50

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 166.52  E-value: 2.26e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINYLpEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGL 129
Cdd:PRK06947    3 KVVLITGASRGIGRATAVLAAARGWSVGINYA-RDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGRL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS-----SVIINTSSVQAVKPSP-VLLDYAQTK 203
Cdd:PRK06947   82 DALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDrggrgGAIVNVSSIASRLGSPnEYVDYAGSK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPmEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQ 283
Cdd:PRK06947  162 GAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASGGQP-GRAARLGAQTPLGRAGEADEVAETIVWLLSDAASYVTGA 240

                  ....*..
gi 1915223084 284 VWCSDGG 290
Cdd:PRK06947  241 LLDVGGG 247
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
52-290 6.52e-50

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 165.22  E-value: 6.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAINYLpEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLDI 131
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAERGADVVINYR-KSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAgRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPSPVLLDYAQTKACLAVF 209
Cdd:cd05359    80 LVSNA-AAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGggRIVAISSLGSIRALPNYLAVGTAKAALEAL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 210 TKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQVWCSDG 289
Cdd:cd05359   159 VRYLAVELGPRGIRVNAVSPGVIDTDALAHFPNREDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTLVVDG 238

                  .
gi 1915223084 290 G 290
Cdd:cd05359   239 G 239
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
46-290 2.33e-49

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 164.29  E-value: 2.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEekDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK12429    1 MLKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDE--AAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVET 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK12429   79 FGGVDILVNNAG-IQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGggRIINMASVHGLVGSAGKAAYVSAK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVL--------QSSGGQPMEKVKE--FGGDTPLGRPGQPVEIAPLYVTLA 273
Cdd:PRK12429  158 HGLIGLTKVVALEGATHGVTVNAICPGYVDTPLvrkqipdlAKERGISEEEVLEdvLLPLVPQKRFTTVEEIADYALFLA 237
                         250
                  ....*....|....*..
gi 1915223084 274 SDACSYTSGQVWCSDGG 290
Cdd:PRK12429  238 SFAAKGVTGQAWVVDGG 254
PRK12743 PRK12743
SDR family oxidoreductase;
50-290 9.35e-49

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 162.51  E-value: 9.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGL 129
Cdd:PRK12743    3 QVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEE-GAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV---IINTSSVQAVKPSPVLLDYAQTKACL 206
Cdd:PRK12743   82 DVLVNNAG-AMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQggrIINITSVHEHTPLPGASAYTAAKHAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 207 AVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQssgGQPMEKVKE-FGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQVW 285
Cdd:PRK12743  161 GGLTKAMALELVEHGILVNAVAPGAIATPMN---GMDDSDVKPdSRPGIPLGRPGDTHEIASLVAWLCSEGASYTTGQSL 237

                  ....*
gi 1915223084 286 CSDGG 290
Cdd:PRK12743  238 IVDGG 242
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
50-290 2.97e-48

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 161.28  E-value: 2.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGL 129
Cdd:PRK12745    3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDE-ELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAGRQ-QYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--------VIINTSSVQAVKPSPVLLDYA 200
Cdd:PRK12745   82 DCLVNNAGVGvKVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPepeelphrSIVFVSSVNAIMVSPNRGEYC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAVAPGpywtVLQSsggqPM-EKVKEF------GGDTPLGRPGQPVEIAPLYVTLA 273
Cdd:PRK12745  162 ISKAGLSMAAQLFAARLAEEGIGVYEVRPG----LIKT----DMtAPVTAKydaliaKGLVPMPRWGEPEDVARAVAALA 233
                         250
                  ....*....|....*..
gi 1915223084 274 SDACSYTSGQVWCSDGG 290
Cdd:PRK12745  234 SGDLPYSTGQAIHVDGG 250
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
50-290 4.85e-48

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 160.70  E-value: 4.85e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINYLpeEEKDAAEviALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGL 129
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFAREGARVVVNYY--RSTESAE--AVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAGRQQ-----YRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQT 202
Cdd:cd05349    77 DTIVNNALIDFpfdpdQRKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKErgSGRVINIGTNLFQNPVVPYHDYTTA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGpYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSG 282
Cdd:cd05349   157 KAALLGFTRNMAKELGPYGITVNMVSGG-LLKVTDASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAVTG 235

                  ....*...
gi 1915223084 283 QVWCSDGG 290
Cdd:cd05349   236 QNLVVDGG 243
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
46-290 5.44e-48

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup includes TR-I and TR-II; these proteins are members of the SDR family. TRs catalyze the NADPH-dependent reductions of the 3-carbonyl group of tropinone, to a beta-hydroxyl group. TR-I and TR-II produce different stereoisomers from tropinone, TR-I produces tropine (3alpha-hydroxytropane), and TR-II, produces pseudotropine (sigma-tropine, 3beta-hydroxytropane). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 160.69  E-value: 5.44e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDaaEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:cd05329     3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELD--ECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGG-LDILINNAGRQQYRESLEeLTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSPVLLDYAQT 202
Cdd:cd05329    81 FGGkLNILVNNAGTNIRKEAKD-YTEEDYSLIMSTNFEAAYHLSRLAHPLLKASgnGNIVFISSVAGVIAVPSGAPYGAT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSG 282
Cdd:cd05329   160 KGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENLDKVIERTPLKRFGEPEEVAALVAFLCMPAASYITG 239

                  ....*...
gi 1915223084 283 QVWCSDGG 290
Cdd:cd05329   240 QIIAVDGG 247
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
46-290 6.14e-47

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 157.88  E-value: 6.14e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLpeeekDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK07067    3 RLQGKVALLTGAASGIGEAVAERYLAEGARVVIADI-----KPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV---IINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK07067   78 FGGIDILFNNAALFDMA-PILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGRggkIINMASQAGRRGEALVSHYCAT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPG----PYWTVLQS-----SGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLA 273
Cdd:PRK07067  157 KAAVISYTQSAALALIRHGINVNAIAPGvvdtPMWDQVDAlfaryENRPPGEKKRLVGEAVPLGRMGVPDDLTGMALFLA 236
                         250
                  ....*....|....*..
gi 1915223084 274 SDACSYTSGQVWCSDGG 290
Cdd:PRK07067  237 SADADYIVAQTYNVDGG 253
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
45-291 1.48e-46

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 156.77  E-value: 1.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEE--KDAAEVialikaeGRKAIALPGDIRDETFCQNLVEEA 122
Cdd:cd05341     1 NRLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEgqAAAAEL-------GDAARFFHLDVTDEDGWTAVVDTA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 123 VSKLGGLDILINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSPVLLDYA 200
Cdd:cd05341    74 REAFGRLDVLVNNAGILTGG-TVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAggGSIINMSSIEGLVGDPALAAYN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 201 QTKACLAVFTKSLAKQLGPK--GIRVNAVAPGPYWT-VLQSSGGQPMEKVKEFGgdTPLGRPGQPVEIAPLYVTLASDAC 277
Cdd:cd05341   153 ASKGAVRGLTKSAALECATQgyGIRVNSVHPGYIYTpMTDELLIAQGEMGNYPN--TPMGRAGEPDEIAYAVVYLASDES 230
                         250
                  ....*....|....
gi 1915223084 278 SYTSGQVWCSDGGD 291
Cdd:cd05341   231 SFVTGSELVVDGGY 244
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
40-290 2.03e-46

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 156.55  E-value: 2.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  40 SYKGHGRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEGRKAIALPGDIRDETFCQNLV 119
Cdd:PRK06113    2 FNSDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADA--ANHVVDEIQQLGGQAFACRCDITSEQELSALA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 120 EEAVSKLGGLDILINNAGRQQYRESleELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSPVLL 197
Cdd:PRK06113   80 DFALSKLGKVDILVNNAGGGGPKPF--DMPMADFRRAYELNVFSFFHLSQLVAPEMEKNggGVILTITSMAAENKNINMT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 198 DYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWT-----VLQSSGGQPMEKvkefggDTPLGRPGQPVEIAPLYVTL 272
Cdd:PRK06113  158 SYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTdalksVITPEIEQKMLQ------HTPIRRLGQPQDIANAALFL 231
                         250
                  ....*....|....*...
gi 1915223084 273 ASDACSYTSGQVWCSDGG 290
Cdd:PRK06113  232 CSPAASWVSGQILTVSGG 249
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
45-290 2.11e-46

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 156.40  E-value: 2.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLpeeEKDAAEVIAliKAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:cd05345     1 MRLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADI---NADGAERVA--ADIGEAAIAIQADVTKRADVEAMVEAALS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLK--ASSVIINTSSVQAVKPSPVLLDYAQT 202
Cdd:cd05345    76 KFGRLDILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEeqGGGVIINIASTAGLRPRPGLTWYNAS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPM--EKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYT 280
Cdd:cd05345   156 KGWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFMGEDtpENRAKFRATIPLGRLSTPDDIANAALYLASDEASFI 235
                         250
                  ....*....|
gi 1915223084 281 SGQVWCSDGG 290
Cdd:cd05345   236 TGVALEVDGG 245
PRK06172 PRK06172
SDR family oxidoreductase;
46-290 3.06e-46

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 156.06  E-value: 3.06e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLpeEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK06172    4 TFSGKVALVTGGAAGIGRATALAFAREGAKVVVADR--DAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK06172   82 YGRLDYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAqgGGAIVNTASVAGLGAAPKMSIYAASK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEF-GGDTPLGRPGQPVEIAPLYVTLASDACSYTSG 282
Cdd:PRK06172  162 HAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYEADPRKAEFaAAMHPVGRIGKVEEVASAVLYLCSDGASFTTG 241

                  ....*...
gi 1915223084 283 QVWCSDGG 290
Cdd:PRK06172  242 HALMVDGG 249
PRK12827 PRK12827
short chain dehydrogenase; Provisional
45-290 3.39e-46

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 156.03  E-value: 3.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAI--NYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEA 122
Cdd:PRK12827    2 ASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVldIHPMRGRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 123 VSKLGGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHL---KASSVIINTSSVQAVKPSPVLLDY 199
Cdd:PRK12827   82 VEEFGRLDILVNNAGIATD-AAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMiraRRGGRIVNIASVAGVRGNRGQVNY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 200 AQTKACLAVFTKSLAKQLGPKGIRVNAVAPGpywtVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSY 279
Cdd:PRK12827  161 AASKAGLIGLTKTLANELAPRGITVNAVAPG----AINTPMADNAAPTEHLLNPVPVQRLGEPDEVAALVAFLVSDAASY 236
                         250
                  ....*....|.
gi 1915223084 280 TSGQVWCSDGG 290
Cdd:PRK12827  237 VTGQVIPVDGG 247
PRK07478 PRK07478
short chain dehydrogenase; Provisional
46-290 3.59e-46

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 155.86  E-value: 3.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAaeVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK07478    3 RLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQ--LVAEIRAEGGEAVALAGDVRDEAYAKALVALAVER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKA---ALRHLKASSVIINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK07478   81 FGGLDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHqipAMLARGGGSLIFTSTFVGHTAGFPGMAAYAAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGqPMEKVKEF-GGDTPLGRPGQPVEIAPLYVTLASDACSYTS 281
Cdd:PRK07478  161 KAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMG-DTPEALAFvAGLHALKRMAQPEEIAQAALFLASDAASFVT 239

                  ....*....
gi 1915223084 282 GQVWCSDGG 290
Cdd:PRK07478  240 GTALLVDGG 248
PRK09730 PRK09730
SDR family oxidoreductase;
52-290 5.40e-46

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 155.39  E-value: 5.40e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAINYLpEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLDI 131
Cdd:PRK09730    4 ALVTGGSRGIGRATALLLAQEGYTVAVNYQ-QNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPLAA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGRQQYRESLEELTTEDFDATFKTNVYAPFW-----ITKAALRHLKASSVIINTSSVQAVKPSP-VLLDYAQTKAC 205
Cdd:PRK09730   83 LVNNAGILFTQCTVENLTAERINRVLSTNVTGYFLccreaVKRMALKHGGSGGAIVNVSSAASRLGAPgEYVDYAASKGA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 206 LAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPmEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQVW 285
Cdd:PRK09730  163 IDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEP-GRVDRVKSNIPMQRGGQPEEVAQAIVWLLSDKASYVTGSFI 241

                  ....*
gi 1915223084 286 CSDGG 290
Cdd:PRK09730  242 DLAGG 246
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
52-290 5.74e-46

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 155.31  E-value: 5.74e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLDI 131
Cdd:cd05337     4 AIVTGASRGIGRAIATELAARGFDIAINDLPDDDQ-ATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGRQ-QYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--------SSVIINTSSVQAVKPSPVLLDYAQT 202
Cdd:cd05337    83 LVNNAGIAvRPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEqpdrfdgpHRSIIFVTSINAYLVSPNRGEYCIS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPME-KVKEfgGDTPLGRPGQPVEIAPLYVTLASDACSYTS 281
Cdd:cd05337   163 KAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDeLIAA--GLVPIRRWGQPEDIAKAVRTLASGLLPYST 240

                  ....*....
gi 1915223084 282 GQVWCSDGG 290
Cdd:cd05337   241 GQPINIDGG 249
PRK07890 PRK07890
short chain dehydrogenase; Provisional
47-291 1.04e-45

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 154.73  E-value: 1.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEE--EKDAAEVIALikaeGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK07890    3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAErlDEVAAEIDDL----GRRALAVPTDITDEDQCANLVALALE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS-VIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK07890   79 RFGRVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGgSIVMINSMVLRHSQPKYGAYKMAK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYW-TVLQ-------SSGGQPMEKV-KEFGGDTPLGRPGQPVEIAPLYVTLAS 274
Cdd:PRK07890  159 GALLAASQSLATELGPQGIRVNSVAPGYIWgDPLKgyfrhqaGKYGVTVEQIyAETAANSDLKRLPTDDEVASAVLFLAS 238
                         250
                  ....*....|....*..
gi 1915223084 275 DACSYTSGQVWCSDGGD 291
Cdd:PRK07890  239 DLARAITGQTLDVNCGE 255
PRK07814 PRK07814
SDR family oxidoreductase;
46-290 1.19e-45

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 154.94  E-value: 1.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDaaEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK07814    7 RLDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLD--EVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYRESLEElTTEDFDATFKTNVYAPFWITKAALRHLKASS---VIINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK07814   85 FGRLDIVVNNVGGTMPNPLLST-STKDLADAFTFNVATAHALTVAAVPLMLEHSgggSVINISSTMGRLAGRGFAAYGTA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKgIRVNAVAPGPYWT-VLQSSGG-----QPMEKVkefggdTPLGRPGQPVEIAPLYVTLASDA 276
Cdd:PRK07814  164 KAALAHYTRLAALDLCPR-IRVNAIAPGSILTsALEVVAAndelrAPMEKA------TPLRRLGDPEDIAAAAVYLASPA 236
                         250
                  ....*....|....
gi 1915223084 277 CSYTSGQVWCSDGG 290
Cdd:PRK07814  237 GSYLTGKTLEVDGG 250
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
49-290 9.36e-45

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 152.60  E-value: 9.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGG 128
Cdd:cd08940     2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 LDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSSVQAVKPSPVLLDYAQTKACL 206
Cdd:cd08940    82 VDILVNNAG-IQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWgrIINIASVHGLVASANKSAYVAAKHGV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 207 AVFTKSLAKQLGPKGIRVNAVAPGPYWTVL--------QSSGGQPMEKVKEfggdtPLGRPGQPV-------EIAPLYVT 271
Cdd:cd08940   161 VGLTKVVALETAGTGVTCNAICPGWVLTPLvekqisalAQKNGVPQEQAAR-----ELLLEKQPSkqfvtpeQLGDTAVF 235
                         250
                  ....*....|....*....
gi 1915223084 272 LASDACSYTSGQVWCSDGG 290
Cdd:cd08940   236 LASDAASQITGTAVSVDGG 254
PRK06500 PRK06500
SDR family oxidoreductase;
46-290 2.25e-44

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 151.26  E-value: 2.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEvialiKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK06500    3 RLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAAR-----AELGESALVIRADAGDVAAQKALAQALAEA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHL-KASSVIINTsSVQAVKPSPVLLDYAQTKA 204
Cdd:PRK06500   78 FGRLDAVFINAGVAKFA-PLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLaNPASIVLNG-SINAHIGMPNSSVYAASKA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGD----TPLGRPGQPVEIAPLYVTLASDACSYT 280
Cdd:PRK06500  156 ALLSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLGLPEATLDAVAAQiqalVPLGRFGTPEEIAKAVLYLASDESAFI 235
                         250
                  ....*....|
gi 1915223084 281 SGQVWCSDGG 290
Cdd:PRK06500  236 VGSEIIVDGG 245
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
46-290 5.00e-44

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 150.30  E-value: 5.00e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEeekDAAEviALIKAEGRKAIA-LPGDIRDETFCQNLVEEAVS 124
Cdd:cd05326     1 RLDGKVAIITGGASGIGEATARLFAKHGARVVIADIDD---DAGQ--AVAAELGDPDISfVHCDVTVEADVRAAVDTAVA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGR-QQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQ 201
Cdd:cd05326    76 RFGRLDIMFNNAGVlGAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMipAKKGSIVSVASVAGVVGGLGPHAYTA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 202 TKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSG-GQPMEKVKEF--GGDTPLGRPGQPVEIAPLYVTLASDACS 278
Cdd:cd05326   156 SKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGfGVEDEAIEEAvrGAANLKGTALRPEDIAAAVLYLASDDSR 235
                         250
                  ....*....|..
gi 1915223084 279 YTSGQVWCSDGG 290
Cdd:cd05326   236 YVSGQNLVVDGG 247
PRK06123 PRK06123
SDR family oxidoreductase;
50-282 8.49e-44

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 149.54  E-value: 8.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINYLpeEEKDAAE-VIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGG 128
Cdd:PRK06123    3 KVMIITGASRGIGAATALLAAERGYAVCLNYL--RNRDAAEaVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 LDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAAL-----RHLKASSVIINTSSVQAVKPSP-VLLDYAQT 202
Cdd:PRK06123   81 LDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFLCAREAVkrmstRHGGRGGAIVNVSSMAARLGSPgEYIDYAAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPmEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSG 282
Cdd:PRK06123  161 KGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEP-GRVDRVKAGIPMGRGGTAEEVARAILWLLSDEASYTTG 239
PRK09134 PRK09134
SDR family oxidoreductase;
50-290 1.13e-43

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 149.69  E-value: 1.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGL 129
Cdd:PRK09134   10 RAALVTGAARRIGRAIALDLAAHGFDVAVHYNRSRD-EAEALAAEIRALGRRAVALQADLADEAEVRALVARASAALGPI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTKACLA 207
Cdd:PRK09134   89 TLLVNNASLFEY-DSAASFTRASWDRHMATNLRAPFVLAQAFARALpaDARGLVVNMIDQRVWNLNPDFLSYTLSKAALW 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 208 VFTKSLAKQLGPKgIRVNAVAPGPywtVLQsSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLAsDACSYTsGQVWCS 287
Cdd:PRK09134  168 TATRTLAQALAPR-IRVNAIGPGP---TLP-SGRQSPEDFARQHAATPLGRGSTPEEIAAAVRYLL-DAPSVT-GQMIAV 240

                  ...
gi 1915223084 288 DGG 290
Cdd:PRK09134  241 DGG 243
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
46-294 1.95e-43

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 148.94  E-value: 1.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEviALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK08213    9 DLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAA--AHLEALGIDALWIAADVADEADIERLAEETLER 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHL---KASSVIINTSSVQAVKPS-PVLLD--- 198
Cdd:PRK08213   87 FGHVDILVNNAG-ATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSmipRGYGRIINVASVAGLGGNpPEVMDtia 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 199 YAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWT-----VLQSSGgqpmEKVKEfggDTPLGRPGQPVEIAPLYVTLA 273
Cdd:PRK08213  166 YNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTkmtrgTLERLG----EDLLA---HTPLGRLGDDEDLKGAALLLA 238
                         250       260
                  ....*....|....*....|.
gi 1915223084 274 SDACSYTSGQVWCSDGGDGVI 294
Cdd:PRK08213  239 SDASKHITGQILAVDGGVSAV 259
PRK06138 PRK06138
SDR family oxidoreductase;
45-290 3.91e-43

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 147.99  E-value: 3.91e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAinyLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK06138    1 MRLAGRVAIVTGAGSGIGRATAKLFAREGARVV---VADRDAEAAERVAAAIAAGGRAFARQGDVGSAEAVEALVDFVAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLK--ASSVIINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK06138   78 RWGRLDVLVNNAGFGC-GGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQrqGGGSIVNTASQLALAGGRGRAAYVAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPG----PYWTVLQSSGGQPmEKVKE-FGGDTPLGRPGQPVEIAPLYVTLASDAC 277
Cdd:PRK06138  157 KGAIASLTRAMALDHATDGIRVNAVAPGtidtPYFRRIFARHADP-EALREaLRARHPMNRFGTAEEVAQAALFLASDES 235
                         250
                  ....*....|...
gi 1915223084 278 SYTSGQVWCSDGG 290
Cdd:PRK06138  236 SFATGTTLVVDGG 248
PRK09242 PRK09242
SDR family oxidoreductase;
46-290 6.38e-43

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 147.59  E-value: 6.38e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK09242    6 RLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEFPEREVHGLAADVSDDEDRRAILDWVEDH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYRESLeELTTEDFDATFKTNVYAPFWITKAALRHLK--ASSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK09242   86 WDGLHILVNNAGGNIRKAAI-DYTEDEWRGIFETNLFSAFELSRYAHPLLKqhASSAIVNIGSVSGLTHVRSGAPYGMTK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQ 283
Cdd:PRK09242  165 AALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYEQVIERTPMRRVGEPEEVAAAVAFLCMPAASYITGQ 244

                  ....*..
gi 1915223084 284 VWCSDGG 290
Cdd:PRK09242  245 CIAVDGG 251
PRK06124 PRK06124
SDR family oxidoreductase;
47-290 6.94e-43

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 147.55  E-value: 6.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINylpeeEKDAAEV---IALIKAEGRKAIALPGDIRDETFCQNLVEEAV 123
Cdd:PRK06124    9 LAGQVALVTGSARGLGFEIARALAGAGAHVLVN-----GRNAATLeaaVAALRAAGGAAEALAFDIADEEAVAAAFARID 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLK--ASSVIINTSSV--QAVKPSPVLldY 199
Cdd:PRK06124   84 AEHGRLDILVNNVGARD-RRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKrqGYGRIIAITSIagQVARAGDAV--Y 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 200 AQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTvlqsSGGQPMEKVKEFG----GDTPLGRPGQPVEIAPLYVTLASD 275
Cdd:PRK06124  161 PAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFAT----ETNAAMAADPAVGpwlaQRTPLGRWGRPEEIAGAAVFLASP 236
                         250
                  ....*....|....*
gi 1915223084 276 ACSYTSGQVWCSDGG 290
Cdd:PRK06124  237 AASYVNGHVLAVDGG 251
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
47-290 1.82e-42

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 146.10  E-value: 1.82e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLpeeEKDAAEVIALIKAEGrkAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:cd08944     1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADI---DGGAAQAVVAQIAGG--ALALRVDVTDEQQVAALFERAVEEF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:cd08944    76 GGLDLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARggGSIVNLSSIAGQSGDPGYGAYGASKA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGG-----DTPLGRPGQPVEIAPLYVTLASDACSY 279
Cdd:cd08944   156 AIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEGALGPGGfhlliHQLQGRLGRPEDVAAAVVFLLSDDASF 235
                         250
                  ....*....|.
gi 1915223084 280 TSGQVWCSDGG 290
Cdd:cd08944   236 ITGQVLCVDGG 246
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
52-290 3.90e-42

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 144.73  E-value: 3.90e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLDI 131
Cdd:cd05357     3 ALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEA-EAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCDV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSSVQAVKPSPVLLDYAQTKACLAVF 209
Cdd:cd05357    82 LVNNAS-AFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNgsIINIIDAMTDRPLTGYFAYCMSKAALEGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 210 TKSLAKQLGPKgIRVNAVAPGPywTVLQSSGGQPM-EKVKEFggdTPLGRPGQPVEIAPLYVTLASdaCSYTSGQVWCSD 288
Cdd:cd05357   161 TRSAALELAPN-IRVNGIAPGL--ILLPEDMDAEYrENALRK---VPLKRRPSAEEIADAVIFLLD--SNYITGQIIKVD 232

                  ..
gi 1915223084 289 GG 290
Cdd:cd05357   233 GG 234
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
44-290 1.24e-41

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 144.16  E-value: 1.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  44 HGRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKdAAEVialikaEGRKAIALPGDIRDETFCQNLVEEAV 123
Cdd:PRK06463    2 SMRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENE-AKEL------REKGVFTIKCDVGNRDQVKKSKEVVE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPSPVLLD-YA 200
Cdd:PRK06463   75 KEFGRVDVLVNNAG-IMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKngAIVNIASNAGIGTAAEGTTfYA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQP--MEKVKE-FGGDTPLGRPGQPVEIAPLYVTLASDAC 277
Cdd:PRK06463  154 ITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQeeAEKLRElFRNKTVLKTTGKPEDIANIVLFLASDDA 233
                         250
                  ....*....|...
gi 1915223084 278 SYTSGQVWCSDGG 290
Cdd:PRK06463  234 RYITGQVIVADGG 246
PRK06484 PRK06484
short chain dehydrogenase; Validated
49-290 1.50e-41

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 150.00  E-value: 1.50e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAInylpeEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGG 128
Cdd:PRK06484  269 PRVVAITGGARGIGRAVADRFAAAGDRLLI-----IDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGR 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 LDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLLDYAQTKACLAV 208
Cdd:PRK06484  344 LDVLVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQGGVIVNLGSIASLLALPPRNAYCASKAAVTM 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 209 FTKSLAKQLGPKGIRVNAVAPG----PYWTVLQSSGGQPMEKVKEfggDTPLGRPGQPVEIAPLYVTLASDACSYTSGQV 284
Cdd:PRK06484  424 LSRSLACEWAPAGIRVNTVAPGyietPAVLALKASGRADFDSIRR---RIPLGRLGDPEEVAEAIAFLASPAASYVNGAT 500

                  ....*.
gi 1915223084 285 WCSDGG 290
Cdd:PRK06484  501 LTVDGG 506
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
48-290 1.83e-41

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 143.38  E-value: 1.83e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  48 TGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALIKAegRKAialpgDIRDetfcQNLVEEAVSKLG 127
Cdd:cd05368     1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERGPGITT--RVL-----DVTD----KEQVAALAKEEG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 128 GLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQA-VKPSPVLLDYAQTKA 204
Cdd:cd05368    70 RIDVLFNCAGFVHH-GSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLArkDGSIINMSSVASsIKGVPNRFVYSTTKA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGPYWT-VLQSSGGQ---PMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYT 280
Cdd:cd05368   149 AVIGLTKSVAADFAQQGIRCNAICPGTVDTpSLEERIQAqpdPEEALKAFAARQPLGRLATPEEVAALAVYLASDESAYV 228
                         250
                  ....*....|
gi 1915223084 281 SGQVWCSDGG 290
Cdd:cd05368   229 TGTAVVIDGG 238
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
46-290 3.69e-41

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 142.95  E-value: 3.69e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEekdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK06935   12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTN---WDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK06935   89 FGKIDILVNNAGTIR-RAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMakQGSGKIINIASMLSFQGGKFVPAYTASK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGpYwtvLQSSGGQPM----EKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSY 279
Cdd:PRK06935  168 HGVAGLTKAFANELAAYNIQVNAIAPG-Y---IKTANTAPIradkNRNDEILKRIPAGRWGEPDDLMGAAVFLASRASDY 243
                         250
                  ....*....|.
gi 1915223084 280 TSGQVWCSDGG 290
Cdd:PRK06935  244 VNGHILAVDGG 254
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
44-290 4.81e-41

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 150.38  E-value: 4.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  44 HGRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEGRkAIALPGDIRDETFCQNLVEEAV 123
Cdd:PRK08324  417 PKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEA--AEAAAAELGGPDR-ALGVACDVTDEAAVQAAFEEAA 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS---SVIINTSSVQAVKPSPVLLDYA 200
Cdd:PRK08324  494 LAFGGVDIVVSNAGIAISG-PIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQglgGSIVFIASKNAVNPGPNFGAYG 572
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAVAPGpywTVLQSSG--------------GQPMEKVKEF-GGDTPLGRPGQPVEI 265
Cdd:PRK08324  573 AAKAAELHLVRQLALELGPDGIRVNGVNPD---AVVRGSGiwtgewiearaaayGLSEEELEEFyRARNLLKREVTPEDV 649
                         250       260
                  ....*....|....*....|....*
gi 1915223084 266 APLYVTLASDACSYTSGQVWCSDGG 290
Cdd:PRK08324  650 AEAVVFLASGLLSKTTGAIITVDGG 674
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
47-288 2.73e-40

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 140.61  E-value: 2.73e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAI----------NYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQ 116
Cdd:cd05338     1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVaaktasegdnGSAKSLPGTIEETAEEIEAAGGQALPIVVDVRDEDQVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 117 NLVEEAVSKLGGLDILINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSSVQAVKPSP 194
Cdd:cd05338    81 ALVEATVDQFGRLDILVNNAGAIWLS-LVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQghILNISPPLSLRPAR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 195 VLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGpywTVLQSSGGQPMekvkeFGGDTPlgRPGQPVEIAPL--YVTL 272
Cdd:cd05338   160 GDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPS---TAIETPAATEL-----SGGSDP--ARARSPEILSDavLAIL 229
                         250
                  ....*....|....*.
gi 1915223084 273 ASDACSYTsGQVWCSD 288
Cdd:cd05338   230 SRPAAERT-GLVVIDE 244
PRK06198 PRK06198
short chain dehydrogenase; Provisional
44-288 8.40e-40

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 139.76  E-value: 8.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  44 HGRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAeVIALIKAEGRKAIALPGDIRDETFCQNLVEEAV 123
Cdd:PRK06198    1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEA-QAAELEALGAKAVFVQADLSDVEDCRRVVAAAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHL---KASSVIINTSSVQAVKPSPVLLDYA 200
Cdd:PRK06198   80 EAFGRLDALVNAAGLTD-RGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMrrrKAEGTIVNIGSMSAHGGQPFLAAYC 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAVAPGpyWT-------VLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLA 273
Cdd:PRK06198  159 ASKGALATLTRNAAYALLRNRIRVNGLNIG--WMategedrIQREFHGAPDDWLEKAAATQPFGRLLDPDEVARAVAFLL 236
                         250
                  ....*....|....*
gi 1915223084 274 SDACSYTSGQVWCSD 288
Cdd:PRK06198  237 SDESGLMTGSVIDFD 251
PRK07035 PRK07035
SDR family oxidoreductase;
47-290 9.63e-40

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 139.38  E-value: 9.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINylpEEEKDAAEVIA-LIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK07035    6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVS---SRKLDGCQAVAdAIVAAGGKAEALACHIGEMEQIDALFAHIRER 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK07035   83 HGRLDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGggSIVNVASVNGVSPGDFQGIYSITK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQ 283
Cdd:PRK07035  163 AAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKNDAILKQALAHIPLRRHAEPSEMAGAVLYLASDASSYTTGE 242

                  ....*..
gi 1915223084 284 VWCSDGG 290
Cdd:PRK07035  243 CLNVDGG 249
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
48-290 9.80e-40

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 139.48  E-value: 9.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  48 TGKKALITGGDSGIGRAVAIAYAREGADVAI-NYLPEEEKDAAEVIaliKAEGRKAIALPGDI--RDETFcqNLVEEAVS 124
Cdd:PRK08643    1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIvDYNEETAQAAADKL---SKDGGKAIAVKADVsdRDQVF--AAVRQVVD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA---SSVIINTSSVQAVKPSPVLLDYAQ 201
Cdd:PRK08643   76 TFGDLNVVVNNAGVAP-TTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKlghGGKIINATSQAGVVGNPELAVYSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 202 TKACLAVFTKSLAKQLGPKGIRVNAVAPG----PYWT----VLQSSGGQPME-KVKEFGGDTPLGRPGQPVEIAPLYVTL 272
Cdd:PRK08643  155 TKFAVRGLTQTAARDLASEGITVNAYAPGivktPMMFdiahQVGENAGKPDEwGMEQFAKDITLGRLSEPEDVANCVSFL 234
                         250
                  ....*....|....*...
gi 1915223084 273 ASDACSYTSGQVWCSDGG 290
Cdd:PRK08643  235 AGPDSDYITGQTIIVDGG 252
PRK06523 PRK06523
short chain dehydrogenase; Provisional
46-290 1.06e-39

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 139.27  E-value: 1.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAIN--YLPEEEKDAAEVIAlikaegrkaialpGDIRDETFCQNLVEEAV 123
Cdd:PRK06523    6 ELAGKRALVTGGTKGIGAATVARLLEAGARVVTTarSRPDDLPEGVEFVA-------------ADLTTAEGCAAVARAVL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGRQQYRES-LEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSP-VLLDY 199
Cdd:PRK06523   73 ERLGGVDILVHVLGGSSAPAGgFAALTDEEWQDELNLNLLAAVRLDRALLPGMIArgSGVIIHVTSIQRRLPLPeSTTAY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 200 AQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTV--------LQSSGGQPMEKVKEFGGDT----PLGRPGQPVEIAP 267
Cdd:PRK06523  153 AAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEaavalaerLAEAAGTDYEGAKQIIMDSlggiPLGRPAEPEEVAE 232
                         250       260
                  ....*....|....*....|...
gi 1915223084 268 LYVTLASDACSYTSGQVWCSDGG 290
Cdd:PRK06523  233 LIAFLASDRAASITGTEYVIDGG 255
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
47-290 1.12e-39

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 139.13  E-value: 1.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEviALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK07523    8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAA--ESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:PRK07523   86 GPIDILVNNAG-MQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMiaRGAGKIINIASVQSALARPGIAPYTATKG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQssggQPMEKVKEFGG----DTPLGRPGQPVEIAPLYVTLASDACSYT 280
Cdd:PRK07523  165 AVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLN----AALVADPEFSAwlekRTPAGRWGKVEELVGACVFLASDASSFV 240
                         250
                  ....*....|
gi 1915223084 281 SGQVWCSDGG 290
Cdd:PRK07523  241 NGHVLYVDGG 250
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
46-293 1.14e-39

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 139.00  E-value: 1.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYL--PEEEKDAAEviaLIKAEGRKAIALPGDIRDETFCQNLVEEAV 123
Cdd:cd05352     5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNsaPRAEEKAEE---LAKKYGVKTKAYKCDVSSQESVEKTFKQIQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS---SVIINTS--SVQAVKPSPVLLd 198
Cdd:cd05352    82 KDFGKIDILIANAG-ITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQgkgSLIITASmsGTIVNRPQPQAA- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 199 YAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLqsSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACS 278
Cdd:cd05352   160 YNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDL--TDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDASS 237
                         250
                  ....*....|....*
gi 1915223084 279 YTSGQVWCSDGGDGV 293
Cdd:cd05352   238 YTTGSDLIIDGGYTC 252
PRK07063 PRK07063
SDR family oxidoreductase;
45-294 2.31e-39

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 138.26  E-value: 2.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKD-AAEVIALIKAEGRkAIALPGDIRDETFCQNLVEEAV 123
Cdd:PRK07063    3 NRLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAErAAAAIARDVAGAR-VLAVPADVTDAASVAAAVAAAE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGRQQYRESLeELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQ 201
Cdd:PRK07063   82 EAFGPLDVLVNNAGINVFADPL-AMTDEDWRRCFAVDLDGAWNGCRAVLPGMveRGRGSIVNIASTHAFKIIPGCFPYPV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 202 TKACLAVFTKSLAKQLGPKGIRVNAVAPG--------PYWtvlqSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLA 273
Cdd:PRK07063  161 AKHGLLGLTRALGIEYAARNVRVNAIAPGyietqlteDWW----NAQPDPAAARAETLALQPMKRIGRPEEVAMTAVFLA 236
                         250       260
                  ....*....|....*....|.
gi 1915223084 274 SDACSYTSGQVWCSDGGDGVI 294
Cdd:PRK07063  237 SDEAPFINATCITIDGGRSVL 257
PRK07774 PRK07774
SDR family oxidoreductase;
45-290 2.79e-39

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 137.95  E-value: 2.79e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLpeeEKDAAE-VIALIKAEGRKAIALPGDIRDETFCQNLVEEAV 123
Cdd:PRK07774    2 GRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADI---NAEGAErVAKQIVADGGTAIAVQVDVSDPDSAKAMADATV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNA----GRQQYreSLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPSPVll 197
Cdd:PRK07774   79 SAFGGIDYLVNNAaiygGMKLD--LLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGggAIVNQSSTAAWLYSNF-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 198 dYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVlQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDAC 277
Cdd:PRK07774  155 -YGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTE-ATRTVTPKEFVADMVKGIPLSRMGTPEDLVGMCLFLLSDEA 232
                         250
                  ....*....|...
gi 1915223084 278 SYTSGQVWCSDGG 290
Cdd:PRK07774  233 SWITGQIFNVDGG 245
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
45-293 1.12e-38

2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 136.62  E-value: 1.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAInylpeEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK06200    2 GWLHGQVALITGGGSGIGRALVERFLAEGARVAV-----LERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQYRESLEELTTED----FDATFKTNVYAPFWITKAALRHLKAS-SVIINTSSVQAVKPSPVLLDY 199
Cdd:PRK06200   77 AFGKLDCFVGNAGIWDYNTSLVDIPAETldtaFDEIFNVNVKGYLLGAKAALPALKASgGSMIFTLSNSSFYPGGGGPLY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 200 AQTKACLAVFTKSLAKQLGPKgIRVNAVAPGPYWTVLQ-----SSGGQPMEKV----KEFGGDTPLGRPGQPVEIAPLYV 270
Cdd:PRK06200  157 TASKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDLRgpaslGQGETSISDSpglaDMIAAITPLQFAPQPEDHTGPYV 235
                         250       260
                  ....*....|....*....|....
gi 1915223084 271 TLASDACS-YTSGQVWCSDGGDGV 293
Cdd:PRK06200  236 LLASRRNSrALTGVVINADGGLGI 259
PRK08589 PRK08589
SDR family oxidoreductase;
45-290 1.29e-38

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 136.83  E-value: 1.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVialIKAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK08589    2 KRLENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDK---IKSNGGKAKAYHVDISDEQQVKDFASEIKE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALR-HLKASSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK08589   79 QFGRVDVLFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPlMMEQGGSIINTSSFSGQAADLYRSGYNAAK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVL--QSSGGQPMEKVKEFGGD----TPLGRPGQPVEIAPLYVTLASDAC 277
Cdd:PRK08589  159 GAVINFTKSIAIEYGRDGIRANAIAPGTIETPLvdKLTGTSEDEAGKTFRENqkwmTPLGRLGKPEEVAKLVVFLASDDS 238
                         250
                  ....*....|...
gi 1915223084 278 SYTSGQVWCSDGG 290
Cdd:PRK08589  239 SFITGETIRIDGG 251
PRK09135 PRK09135
pteridine reductase; Provisional
49-290 1.95e-38

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 135.83  E-value: 1.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAINY---LPEEEKDAAEVIALikaegR--KAIALPGDIRDETFCQNLVEEAV 123
Cdd:PRK09135    6 AKVALITGGARRIGAAIARTLHAAGYRVAIHYhrsAAEADALAAELNAL-----RpgSAAALQADLLDPDALPELVAACV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGRqQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS-VIINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK09135   81 AAFGRLDALVNNASS-FYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQRgAIVNITDIHAERPLKGYPVYCAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKgIRVNAVAPGPywtVLQSSGGQPMEKVKEFG--GDTPLGRPGQPVEIAPLYVTLASDAcSYT 280
Cdd:PRK09135  160 KAALEMLTRSLALELAPE-VRVNAVAPGA---ILWPEDGNSFDEEARQAilARTPLKRIGTPEDIAEAVRFLLADA-SFI 234
                         250
                  ....*....|
gi 1915223084 281 SGQVWCSDGG 290
Cdd:PRK09135  235 TGQILAVDGG 244
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-290 2.06e-38

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 135.97  E-value: 2.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGD--SGIGRAVAIAYAREGADVAINYLPE---------EEKDAAEVIALIKAEGRKAIALPGDIRDETFC 115
Cdd:PRK12748    3 LMKKIALVTGASrlNGIGAAVCRRLAAKGIDIFFTYWSPydktmpwgmHDKEPVLLKEEIESYGVRCEHMEIDLSQPYAP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 116 QNLVEEAVSKLGGLDILINNAgRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRH--LKASSVIINTSSVQAVKPS 193
Cdd:PRK12748   83 NRVFYAVSERLGDPSILINNA-AYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQydGKAGGRIINLTSGQSLGPM 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 194 PVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPywtvlQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLA 273
Cdd:PRK12748  162 PDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGP-----TDTGWITEELKHHLVPKFPQGRVGEPVDAARLIAFLV 236
                         250
                  ....*....|....*..
gi 1915223084 274 SDACSYTSGQVWCSDGG 290
Cdd:PRK12748  237 SEEAKWITGQVIHSEGG 253
PRK07791 PRK07791
short chain dehydrogenase; Provisional
44-290 2.39e-38

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 136.34  E-value: 2.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  44 HGRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYL-------PEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQ 116
Cdd:PRK07791    1 MGLLDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIgvgldgsASGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 117 NLVEEAVSKLGGLDILINNAG--RQQYRESLEElttEDFDATFKTNVYAPFWITKAALRHLKASS--------VIINTSS 186
Cdd:PRK07791   81 NLVDAAVETFGGLDVLVNNAGilRDRMIANMSE---EEWDAVIAVHLKGHFATLRHAAAYWRAESkagravdaRIINTSS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 187 VQAVKPSPVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTplgrpGQPVEIA 266
Cdd:PRK07791  158 GAGLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPAARTRMTETVFAEMMAKPEEGEFDA-----MAPENVS 232
                         250       260
                  ....*....|....*....|....
gi 1915223084 267 PLYVTLASDACSYTSGQVWCSDGG 290
Cdd:PRK07791  233 PLVVWLGSAESRDVTGKVFEVEGG 256
PRK06841 PRK06841
short chain dehydrogenase; Provisional
38-290 7.50e-38

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 134.40  E-value: 7.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  38 EKSYKGHGRLTGKKALITGGDSGIGRAVAIAYAREGADVAinyLPEEEKDAAEVIALIKAEGRKAIALpgDIRDETFCQN 117
Cdd:PRK06841    4 TKQFDLAFDLSGKVAVVTGGASGIGHAIAELFAAKGARVA---LLDRSEDVAEVAAQLLGGNAKGLVC--DVSDSQSVEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 118 LVEEAVSKLGGLDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPV 195
Cdd:PRK06841   79 AVAAVISAFGRIDILVNSAG-VALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAagGGKIVNLASQAGVVALER 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 196 LLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSG--GQPMEKVKEfggDTPLGRPGQPVEIAPLYVTLA 273
Cdd:PRK06841  158 HVAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGKKAwaGEKGERAKK---LIPAGRFAYPEEIAAAALFLA 234
                         250
                  ....*....|....*..
gi 1915223084 274 SDACSYTSGQVWCSDGG 290
Cdd:PRK06841  235 SDAAAMITGENLVIDGG 251
PRK07856 PRK07856
SDR family oxidoreductase;
47-290 1.85e-37

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 133.14  E-value: 1.85e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKdaaevialikAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK07856    4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPET----------VDGRPAEFHAADVRDPDQVAALVDAIVERH 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYRESLEelTTEDF-DATFKTNVYAPFWITKAALRHLKASS---VIINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK07856   74 GRLDVLVNNAGGSPYALAAE--ASPRFhEKIVELNLLAPLLVAQAANAVMQQQPgggSIVNIGSVSGRRPSPGTAAYGAA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKgIRVNAVAPGPYWTVL--QSSGGQpmEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYT 280
Cdd:PRK07856  152 KAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQseLHYGDA--EGIAAVAATVPLGRLATPADIAWACLFLASDLASYV 228
                         250
                  ....*....|
gi 1915223084 281 SGQVWCSDGG 290
Cdd:PRK07856  229 SGANLEVHGG 238
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
46-290 2.41e-37

enoyl-[acyl-carrier-protein] reductase FabL;


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 132.92  E-value: 2.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLpeEEKDAA-EVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK08063    1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNYA--RSRKAAeETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQYRESLeELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKpspVLLDYAQ- 201
Cdd:PRK08063   79 EFGRLDVFVNNAASGVLRPAM-ELEESHWDWTMNINAKALLFCAQEAAKLMekVGGGKIISLSSLGSIR---YLENYTTv 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 202 --TKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSY 279
Cdd:PRK08063  155 gvSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPNREELLEDARAKTPAGRMVEPEDVANAVLFLCSPEADM 234
                         250
                  ....*....|.
gi 1915223084 280 TSGQVWCSDGG 290
Cdd:PRK08063  235 IRGQTIIVDGG 245
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
44-290 2.49e-37

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 132.99  E-value: 2.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  44 HGRLTGKKALITGGD--SGIGRAVAIAYAREGADVAINYLPEEEK------DAAEVIAL---IKAEGRKAIALPGDIRDE 112
Cdd:PRK12859    1 MNQLKNKVAVVTGVSrlDGIGAAICKELAEAGADIFFTYWTAYDKempwgvDQDEQIQLqeeLLKNGVKVSSMELDLTQN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 113 TFCQNLVEEAVSKLGGLDILINNAGrqqYRESL--EELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQ 188
Cdd:PRK12859   81 DAPKELLNKVTEQLGYPHILVNNAA---YSTNNdfSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSggRIINMTSGQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 189 AVKPSPVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPywtvlqSSGGQPMEKVKEF-GGDTPLGRPGQPVEIAP 267
Cdd:PRK12859  158 FQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGP------TDTGWMTEEIKQGlLPMFPFGRIGEPKDAAR 231
                         250       260
                  ....*....|....*....|...
gi 1915223084 268 LYVTLASDACSYTSGQVWCSDGG 290
Cdd:PRK12859  232 LIKFLASEEAEWITGQIIHSEGG 254
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-290 1.18e-36

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 131.00  E-value: 1.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK06077    4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAE-EMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYR---ESLEELTTEDFDATFKTNVYApfwiTKAALRHLKASSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK06077   83 GVADILVNNAGLGLFSpflNVDDKLIDKHISTDFKSVIYC----SQELAKEMREGGAIVNIASVAGIRPAYGLSIYGAMK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKgIRVNAVAPGpywtVLQSSGGQPMEKV-----KEFGGD-TPLGRPGQPVEIAPLYVTLASdaC 277
Cdd:PRK06077  159 AAVINLTKYLALELAPK-IRVNAIAPG----FVKTKLGESLFKVlgmseKEFAEKfTLMGKILDPEEVAEFVAAILK--I 231
                         250
                  ....*....|...
gi 1915223084 278 SYTSGQVWCSDGG 290
Cdd:PRK06077  232 ESITGQVFVLDSG 244
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
45-290 2.11e-36

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 130.69  E-value: 2.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVA-INYLPEEEKDAAEvialIKAEGRKAIALPGDIRDETFCQNLVEEAV 123
Cdd:PRK08226    2 GKLTGKTALITGALQGIGEGIARVFARHGANLIlLDISPEIEKLADE----LCGRGHRCTAVVADVRDPASVAAAIKRAK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQA-VKPSPVLLDYA 200
Cdd:PRK08226   78 EKEGRIDILVNNAGVCRL-GSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMiaRKDGRIVMMSSVTGdMVADPGETAYA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVL------QSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLAS 274
Cdd:PRK08226  157 LTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMaesiarQSNPEDPESVLTEMAKAIPLRRLADPLEVGELAAFLAS 236
                         250
                  ....*....|....*.
gi 1915223084 275 DACSYTSGQVWCSDGG 290
Cdd:PRK08226  237 DESSYLTGTQNVIDGG 252
PRK05867 PRK05867
SDR family oxidoreductase;
47-290 2.25e-36

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 130.54  E-value: 2.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAInylPEEEKDAAEVIA-LIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK05867    7 LHGKRALITGASTGIGKRVALAYVEAGAQVAI---AARHLDALEKLAdEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYRESLeELTTEDFDATFKTNVYAPFWITKAALRHL---KASSVIINTSSVQA--VKPSPVLLDYA 200
Cdd:PRK05867   84 LGGIDIAVCNAGIITVTPML-DMPLEEFQRLQNTNVTGVFLTAQAAAKAMvkqGQGGVIINTASMSGhiINVPQQVSHYC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQssggQPM-EKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSY 279
Cdd:PRK05867  163 ASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELV----EPYtEYQPLWEPKIPLGRLGRPEELAGLYLYLASEASSY 238
                         250
                  ....*....|.
gi 1915223084 280 TSGQVWCSDGG 290
Cdd:PRK05867  239 MTGSDIVIDGG 249
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
47-290 2.84e-36

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 130.52  E-value: 2.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVainylpeeekdaaeVIALIKAEGRKAIAL---PGDIRDETFCQNLVEEAV 123
Cdd:PRK06171    7 LQGKIIIVTGGSSGIGLAIVKELLANGANV--------------VNADIHGGDGQHENYqfvPTDVSSAEEVNHTVAEII 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGRQQYR--------ESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPS 193
Cdd:PRK06171   73 EKFGRIDGLVNNAGINIPRllvdekdpAGKYELNEAAFDKMFNINQKGVFLMSQAVARQMvkQHDGVIVNMSSEAGLEGS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 194 PVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPG----------PYWTVLQSSGGQPMEKVKE---FGGDTPLGRPG 260
Cdd:PRK06171  153 EGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGileatglrtpEYEEALAYTRGITVEQLRAgytKTSTIPLGRSG 232
                         250       260       270
                  ....*....|....*....|....*....|
gi 1915223084 261 QPVEIAPLYVTLASDACSYTSGQVWCSDGG 290
Cdd:PRK06171  233 KLSEVADLVCYLLSDRASYITGVTTNIAGG 262
PRK06114 PRK06114
SDR family oxidoreductase;
46-290 3.37e-36

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 129.90  E-value: 3.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK06114    5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDD-GLAETAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSPVLLD--YAQ 201
Cdd:PRK06114   84 LGALTLAVNAAGIAN-ANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENggGSIVNIASMSGIIVNRGLLQahYNA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 202 TKACLAVFTKSLAKQLGPKGIRVNAVAPGpYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTS 281
Cdd:PRK06114  163 SKAGVIHLSKSLAMEWVGRGIRVNSISPG-YTATPMNTRPEMVHQTKLFEEQTPMQRMAKVDEMVGPAVFLLSDAASFCT 241

                  ....*....
gi 1915223084 282 GQVWCSDGG 290
Cdd:PRK06114  242 GVDLLVDGG 250
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
47-290 4.05e-36

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 130.18  E-value: 4.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAevIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK07097    8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKG--LAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:PRK07097   86 GVIDILVNNAGIIK-RIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMikKGHGKIINICSMMSELGRETVSAYAAAKG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGPYWT-------VLQSSG-GQPMEkvkEF-GGDTPLGRPGQPVEIAPLYVTLASD 275
Cdd:PRK07097  165 GLKMLTKNIASEYGEANIQCNGIGPGYIATpqtaplrELQADGsRHPFD---QFiIAKTPAARWGDPEDLAGPAVFLASD 241
                         250
                  ....*....|....*
gi 1915223084 276 ACSYTSGQVWCSDGG 290
Cdd:PRK07097  242 ASNFVNGHILYVDGG 256
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
46-290 4.10e-36

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 129.82  E-value: 4.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLpeEEKDAAEviALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK08642    2 QISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYH--QSEDAAE--ALADELGDRAIALQADVTDREQVQAMFATATEH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LG-GLDILINNA-------GRQqyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS----VIINTSSVQavkpS 193
Cdd:PRK08642   78 FGkPITTVVNNAladfsfdGDA--RKKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGfgriINIGTNLFQ----N 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 194 PVLL--DYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVlQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVT 271
Cdd:PRK08642  152 PVVPyhDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTT-DASAATPDEVFDLIAATTPLRKVTTPQEFADAVLF 230
                         250
                  ....*....|....*....
gi 1915223084 272 LASDACSYTSGQVWCSDGG 290
Cdd:PRK08642  231 FASPWARAVTGQNLVVDGG 249
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
47-290 9.22e-36

RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 128.75  E-value: 9.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVainYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:cd08942     4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARV---IISARKAEACADAAEELSAYGECIAIPADLSSEEGIEALVARVAERS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV------IINTSSVQA-VKPSPVLLDY 199
Cdd:cd08942    81 DRLDVLVNNAG-ATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaenparVINIGSIAGiVVSGLENYSY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 200 AQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSY 279
Cdd:cd08942   160 GASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNDPAALEAEEKSIPLGRWGRPEDMAGLAIMLASRAGAY 239
                         250
                  ....*....|.
gi 1915223084 280 TSGQVWCSDGG 290
Cdd:cd08942   240 LTGAVIPVDGG 250
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
46-290 1.09e-35

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 128.58  E-value: 1.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYlpEEEKDAAE-VIALIKAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK12935    3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINY--NSSKEAAEnLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK12935   81 HFGKVDILVNNAGITRDR-TFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEegRIISISSIIGQAGGFGQTNYSAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSggQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDAcSYTSG 282
Cdd:PRK12935  160 KAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAE--VPEEVRQKIVAKIPKKRFGQADEIAKGVVYLCRDG-AYITG 236

                  ....*...
gi 1915223084 283 QVWCSDGG 290
Cdd:PRK12935  237 QQLNINGG 244
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-229 1.17e-35

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 128.27  E-value: 1.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK07666    5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGL--LARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:PRK07666   83 GSIDILINNAGISKF-GKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMieRQSGDIINISSTAGQKGAAVTSAYSASKF 161
                         170       180
                  ....*....|....*....|....*
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAP 229
Cdd:PRK07666  162 GVLGLTESLMQEVRKHNIRVTALTP 186
PRK07060 PRK07060
short chain dehydrogenase; Provisional
42-290 1.58e-35

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 127.91  E-value: 1.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  42 KGHGRLTGKKALITGGDSGIGRAVAIAYAREGADVAinylpEEEKDAAEVIALIKAEGRKAIALpgDIRDETFcqnlVEE 121
Cdd:PRK07060    2 NMAFDFSGKSVLVTGASSGIGRACAVALAQRGARVV-----AAARNAAALDRLAGETGCEPLRL--DVGDDAA----IRA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 122 AVSKLGGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV---IINTSSVQAVKPSPVLLD 198
Cdd:PRK07060   71 ALAAAGAFDGLVNCAGIASL-ESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRggsIVNVSSQAALVGLPDHLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 199 YAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACS 278
Cdd:PRK07060  150 YCASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAWSDPQKSGPMLAAIPLGRFAEVDDVAAPILFLLSDAAS 229
                         250
                  ....*....|..
gi 1915223084 279 YTSGQVWCSDGG 290
Cdd:PRK07060  230 MVSGVSLPVDGG 241
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
47-290 1.83e-35

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 128.47  E-value: 1.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAaeVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK13394    5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANA--VADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHL---KASSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK13394   83 GSVDILVSNAG-IQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMykdDRGGVVIYMGSVHSHEASPLKSAYVTAK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSggQPMEKVKEFG------------GDTPLGRPGQPVEIAPLYVT 271
Cdd:PRK13394  162 HGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDK--QIPEQAKELGiseeevvkkvmlGKTVDGVFTTVEDVAQTVLF 239
                         250
                  ....*....|....*....
gi 1915223084 272 LASDACSYTSGQVWCSDGG 290
Cdd:PRK13394  240 LSSFPSAALTGQSFVVSHG 258
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
46-291 1.95e-35

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 128.03  E-value: 1.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAinyLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:cd08937     1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVL---LVDRSELVHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSV--QAVKPSPvlldYAQ 201
Cdd:cd08937    78 FGRVDVLINNVGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLErqQGVIVNVSSIatRGIYRIP----YSA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 202 TKACLAVFTKSLAKQLGPKGIRVNAVAPG----PYWTVLQSSggQPMEK---------VKEFGGDTPLGRPGQPVEIAPL 268
Cdd:cd08937   154 AKGGVNALTASLAFEHARDGIRVNAVAPGgteaPPRKIPRNA--APMSEqekvwyqriVDQTLDSSLMGRYGTIDEQVRA 231
                         250       260
                  ....*....|....*....|...
gi 1915223084 269 YVTLASDACSYTSGQVWCSDGGD 291
Cdd:cd08937   232 ILFLASDEASYITGTVLPVGGGD 254
PRK12828 PRK12828
short chain dehydrogenase; Provisional
45-290 2.14e-35

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 127.61  E-value: 2.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVIALIKAEGRKAIALpgDIRDETFCQNLVEEAVS 124
Cdd:PRK12828    3 HSLQGKVVAITGGFGGLGRATAAWLAARGARVAL--IGRGAAPLSQTLPGVPADALRIGGI--DLVDPQAARRAVDEVNR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK12828   79 QFGRLDALVNIAGAFVW-GTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGgrIVNIGAGAALKAGPGMGAYAAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTvlqssggqPMEKVKEFGGDtpLGRPGQPVEIAPLYVTLASDACSYTSG 282
Cdd:PRK12828  158 KAGVARLTEALAAELLDRGITVNAVLPSIIDT--------PPNRADMPDAD--FSRWVTPEQIAAVIAFLLSDEAQAITG 227

                  ....*...
gi 1915223084 283 QVWCSDGG 290
Cdd:PRK12828  228 ASIPVDGG 235
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
50-284 3.81e-35

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 126.32  E-value: 3.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAevialiKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGL 129
Cdd:cd08932     1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAAL------SASGGDVEAVPYDARDPEDARALVDALRDRFGRI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTKACLA 207
Cdd:cd08932    75 DVLVHNAGIGR-PTTLREGSDAELEAHFSINVIAPAELTRALLPALreAGSGRVVFLNSLSGKRVLAGNAGYSASKFALR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1915223084 208 VFTKSLAKQLGPKGIRVNAVAPGPYWTvlqssggqPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQV 284
Cdd:cd08932   154 ALAHALRQEGWDHGVRVSAVCPGFVDT--------PMAQGLTLVGAFPPEEMIQPKDIANLVRMVIELPENITSVAV 222
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
47-291 9.10e-35

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 126.19  E-value: 9.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYL-PEEEKDAAEVIalikaeGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:cd05363     1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADInLEAARATAAEI------GPAACAISLDVTDQASIDRCVAALVDR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYRESLEElTTEDFDATFKTNVYAPFWITKAALRHLKAS---SVIINTSSVQAVKPSPVLLDYAQT 202
Cdd:cd05363    75 WGSIDILVNNAALFDLAPIVDI-TRESYDRLFAINVSGTLFMMQAVARAMIAQgrgGKIINMASQAGRRGEALVGVYCAT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPG----PYW----TVLQSSGGQPM-EKVKEFGGDTPLGRPGQPVEIAPLYVTLA 273
Cdd:cd05363   154 KAAVISLTQSAGLNLIRHGINVNAIAPGvvdgEHWdgvdAKFARYENRPRgEKKRLVGEAVPFGRMGRAEDLTGMAIFLA 233
                         250
                  ....*....|....*...
gi 1915223084 274 SDACSYTSGQVWCSDGGD 291
Cdd:cd05363   234 STDADYIVAQTYNVDGGN 251
PRK08265 PRK08265
short chain dehydrogenase; Provisional
46-290 9.38e-35

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 126.28  E-value: 9.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAInylpeEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK08265    3 GLAGKVAIVTGGATLIGAAVARALVAAGARVAI-----VDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVAR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGrqQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS-SVIINTSSVQAvkpspvllDYAQT-- 202
Cdd:PRK08265   78 FGRVDILVNLAC--TYLDDGLASSRADWLAALDVNLVSAAMLAQAAHPHLARGgGAIVNFTSISA--------KFAQTgr 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 ------KACLAVFTKSLAKQLGPKGIRVNAVAPGpyWT---VLQSSGGQPMEKVKEFGGDT-PLGRPGQPVEIAPLYVTL 272
Cdd:PRK08265  148 wlypasKAAIRQLTRSMAMDLAPDGIRVNSVSPG--WTwsrVMDELSGGDRAKADRVAAPFhLLGRVGDPEEVAQVVAFL 225
                         250
                  ....*....|....*...
gi 1915223084 273 ASDACSYTSGQVWCSDGG 290
Cdd:PRK08265  226 CSDAASFVTGADYAVDGG 243
PRK07576 PRK07576
short chain dehydrogenase; Provisional
46-290 1.91e-34

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 125.84  E-value: 1.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAevIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK07576    6 DFAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAA--VAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHL-KASSVIINTSSVQAVKPSPvlldyAQTKA 204
Cdd:PRK07576   84 FGPIDVLVSGAA-GNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLrRPGASIIQISAPQAFVPMP-----MQAHV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLA-----VFTKSLAKQLGPKGIRVNAVAPGPYwtvlqsSGGQPMEKV-------KEFGGDTPLGRPGQPVEIAPLYVTL 272
Cdd:PRK07576  158 CAAkagvdMLTRTLALEWGPEGIRVNSIVPGPI------AGTEGMARLapspelqAAVAQSVPLKRNGTKQDIANAALFL 231
                         250
                  ....*....|....*...
gi 1915223084 273 ASDACSYTSGQVWCSDGG 290
Cdd:PRK07576  232 ASDMASYITGVVLPVDGG 249
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
50-251 1.98e-34

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 125.04  E-value: 1.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADV--------AINYLPEEEKDAAEVIALikaegrkaialpgDIRDETFCQNLVEE 121
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQGYRViatarnpdKLESLGELLNDNLEVLEL-------------DVTDEESIKAAVKE 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 122 AVSKLGGLDILINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDY 199
Cdd:cd05374    68 VIERFGRIDVLVNNAGYGLFG-PLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKqgSGRIVNVSSVAGLVPTPFLGPY 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1915223084 200 AQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFG 251
Cdd:cd05374   147 CASKAALEALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGSALEDPEIS 198
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
47-290 2.61e-34

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 125.65  E-value: 2.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDaaEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:cd08935     3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGD--KVAKEITALGGRAIALAADVLDRASLERAREEIVAQF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAG-------------RQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVK 191
Cdd:cd08935    81 GTVDILINGAGgnhpdattdpehyEPETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMleQKGGSIINISSMNAFS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 192 PSPVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWT-----VLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIA 266
Cdd:cd08935   161 PLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTpqnrkLLINPDGSYTDRSNKILGRTPMGRFGKPEELL 240
                         250       260
                  ....*....|....*....|....*
gi 1915223084 267 PLYVTLASD-ACSYTSGQVWCSDGG 290
Cdd:cd08935   241 GALLFLASEkASSFVTGVVIPVDGG 265
PRK06398 PRK06398
aldose dehydrogenase; Validated
47-290 2.80e-34

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 124.94  E-value: 2.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALikaegrkaialpgDIRDETFCQNLVEEAVSKL 126
Cdd:PRK06398    4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYNDVDYFKV-------------DVSNKEQVIKGIDYVISKY 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:PRK06398   71 GRIDILVNNAGIESY-GAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDkgVIINIASVQSFAVTRNAAAYVTSKH 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKgIRVNAVAPGPY------WTVLQSSGGQPM---EKVKEFGGDTPLGRPGQPVEIAPLYVTLASD 275
Cdd:PRK06398  150 AVLGLTRSIAVDYAPT-IRCVAVCPGSIrtplleWAAELEVGKDPEhveRKIREWGEMHPMKRVGKPEEVAYVVAFLASD 228
                         250
                  ....*....|....*
gi 1915223084 276 ACSYTSGQVWCSDGG 290
Cdd:PRK06398  229 LASFITGECVTVDGG 243
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
48-290 2.86e-34

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 124.75  E-value: 2.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  48 TGKKALITGGDSGIGRAVAIAYAREGADVaINYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLG 127
Cdd:cd08930     1 EDKIILITGAAGLIGKAFCKALLSAGARL-ILADINAPALEQLKEELTNLYKNRVIALELDITSKESIKELIESYLEKFG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 128 GLDILINNAG--RQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAV---------KPSP 194
Cdd:cd08930    80 RIDILINNAYpsPKVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGkgSIINIASIYGViapdfriyeNTQM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 195 VL-LDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTvlqssgGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLA 273
Cdd:cd08930   160 YSpVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILN------NQPSEFLEKYTKKCPLKRMLNPEDLRGAIIFLL 233
                         250
                  ....*....|....*..
gi 1915223084 274 SDACSYTSGQVWCSDGG 290
Cdd:cd08930   234 SDASSYVTGQNLVIDGG 250
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
45-290 3.76e-34

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 124.36  E-value: 3.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYL-------PEEEKDAAEVIALIKAEGRKAIALPGDIRDEtfcQN 117
Cdd:cd05353     1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLggdrkgsGKSSSAADKVVDEIKAAGGKAVANYDSVEDG---EK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 118 LVEEAVSKLGGLDILINNAG--RQQyreSLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPS 193
Cdd:cd05353    78 IVKTAIDAFGRVDILVNNAGilRDR---SFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfgRIINTSSAAGLYGN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 194 PVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSggQPMEKVKEFGgdtplgrpgqPVEIAPLYVTLA 273
Cdd:cd05353   155 FGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPAAGSRMTETV--MPEDLFDALK----------PEYVAPLVLYLC 222
                         250
                  ....*....|....*..
gi 1915223084 274 SDACSYTsGQVWCSDGG 290
Cdd:cd05353   223 HESCEVT-GGLFEVGAG 238
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
47-290 5.57e-34

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 124.12  E-value: 5.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADV-AINylpeeeKDAAEVIALIKaEGRKAIALPGDIRDetfcQNLVEEAVSK 125
Cdd:cd05351     5 FAGKRALVTGAGKGIGRATVKALAKAGARVvAVS------RTQADLDSLVR-ECPGIEPVCVDLSD----WDATEEALGS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV---IINTSSVQAVKPSPVLLDYAQT 202
Cdd:cd05351    74 VGPVDLLVNNAAVAIL-QPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVpgsIVNVSSQASQRALTNHTVYCST 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPgpywTVLQSSGGQ-----PmEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDAC 277
Cdd:cd05351   153 KAALDMLTKVMALELGPHKIRVNSVNP----TVVMTDMGRdnwsdP-EKAKKMLNRIPLGKFAEVEDVVNAILFLLSDKS 227
                         250
                  ....*....|...
gi 1915223084 278 SYTSGQVWCSDGG 290
Cdd:cd05351   228 SMTTGSTLPVDGG 240
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
50-290 8.80e-34

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 123.34  E-value: 8.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINYLPEeeKDAAEVIALIKAEGRKAI-ALPGDIRDETFCQNLVEEAVSKLGG 128
Cdd:PRK12824    3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSG--NDCAKDWFEEYGFTEDQVrLKELDVTDTEECAEALAEIEEEEGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 LDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTKACL 206
Cdd:PRK12824   81 VDILVNNAGITR-DSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMceQGYGRIINISSVNGLKGQFGQTNYSAAKAGM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 207 AVFTKSLAKQLGPKGIRVNAVAPGPYWT-VLQSSGGQPMEKVKEfggDTPLGRPGQPVEIAPLYVTLASDACSYTSGQVW 285
Cdd:PRK12824  160 IGFTKALASEGARYGITVNCIAPGYIATpMVEQMGPEVLQSIVN---QIPMKRLGTPEEIAAAVAFLVSEAAGFITGETI 236

                  ....*
gi 1915223084 286 CSDGG 290
Cdd:PRK12824  237 SINGG 241
PRK07326 PRK07326
SDR family oxidoreductase;
47-230 8.93e-34

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 123.20  E-value: 8.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINylPEEEKDAAEVIALIKAEGRkAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK07326    4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAIT--ARDQKELEEAAAELNNKGN-VLGLAADVRDEADVQRAVDAIVAAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS-VIINTSSVQAVKPSPVLLDYAQTKAC 205
Cdd:PRK07326   81 GGLDVLIANAGVGHFA-PVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGgYIINISSLAGTNFFAGGAAYNASKFG 159
                         170       180
                  ....*....|....*....|....*
gi 1915223084 206 LAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:PRK07326  160 LVGFSEAAMLDLRQYGIKVSTIMPG 184
PRK07069 PRK07069
short chain dehydrogenase; Validated
51-290 1.58e-33

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 122.90  E-value: 1.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  51 KALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKdAAEVIALIKAE--GRKAIALPGDIRDETFCQNLVEEAVSKLGG 128
Cdd:PRK07069    1 RAFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAG-LDAFAAEINAAhgEGVAFAAVQDVTDEAQWQALLAQAADAMGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 LDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSPVLLDYAQTKACL 206
Cdd:PRK07069   80 LSVLVNNAGVGS-FGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASqpASIVNISSVAAFKAEPDYTAYNASKAAV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 207 AVFTKSLAKQLGPKG--IRVNAVAPGPYWTVLQSSGGQPMEK---VKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTS 281
Cdd:PRK07069  159 ASLTKSIALDCARRGldVRCNSIHPTFIRTGIVDPIFQRLGEeeaTRKLARGVPLGRLGEPDDVAHAVLYLASDESRFVT 238

                  ....*....
gi 1915223084 282 GQVWCSDGG 290
Cdd:PRK07069  239 GAELVIDGG 247
PRK07831 PRK07831
SDR family oxidoreductase;
43-284 2.41e-33

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 122.84  E-value: 2.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  43 GHGRLTGKKALITGG-DSGIGRAVAIAYAREGADVAI-NYLPEEEKDAAEVIALIKAEGRKAiALPGDIRDETFCQNLVE 120
Cdd:PRK07831   11 GHGLLAGKVVLVTAAaGTGIGSATARRALEEGARVVIsDIHERRLGETADELAAELGLGRVE-AVVCDVTSEAQVDALID 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 121 EAVSKLGGLDILINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHLKA---SSVIINTSSVQAVKPSPVLL 197
Cdd:PRK07831   90 AAVERLGRLDVLVNNAGLGGQT-PVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRArghGGVIVNNASVLGWRAQHGQA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 198 DYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPG----PYWTVLQSSggqpmEKVKEFGGDTPLGRPGQPVEIAPLYVTLA 273
Cdd:PRK07831  169 HYAAAKAGVMALTRCSALEAAEYGVRINAVAPSiamhPFLAKVTSA-----ELLDELAAREAFGRAAEPWEVANVIAFLA 243
                         250
                  ....*....|.
gi 1915223084 274 SDACSYTSGQV 284
Cdd:PRK07831  244 SDYSSYLTGEV 254
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
45-291 2.77e-33

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 122.36  E-value: 2.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAinyLPEEEKDAAEVIALIKAEGRKAIALPGDIrdETF--CQNLVEEA 122
Cdd:PRK12823    4 QRFAGKVVVVTGAAQGIGRGVALRAAAEGARVV---LVDRSELVHEVAAELRAAGGEALALTADL--ETYagAQAAMAAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 123 VSKLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSV--QAVKPSPvlld 198
Cdd:PRK12823   79 VEAFGRIDVLINNVGGTIWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAqgGGAIVNVSSIatRGINRVP---- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 199 YAQTKACLAVFTKSLAKQLGPKGIRVNAVAPG----PYWTVLQSSGGQ-PMEK------VKEFGGDTPLGRPGQPVEIAP 267
Cdd:PRK12823  155 YSAAKGGVNALTASLAFEYAEHGIRVNAVAPGgteaPPRRVPRNAAPQsEQEKawyqqiVDQTLDSSLMKRYGTIDEQVA 234
                         250       260
                  ....*....|....*....|....
gi 1915223084 268 LYVTLASDACSYTSGQVWCSDGGD 291
Cdd:PRK12823  235 AILFLASDEASYITGTVLPVGGGD 258
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
46-276 4.53e-33

retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the short-chain dehydrogenases/reductase family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 121.87  E-value: 4.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEViALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:cd08933     6 RYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALES-ELNRAGPGSCKFVPCDVTKEEDIKTLISVTVER 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHL-KASSVIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:cd08933    85 FGRIDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLrKSQGNIINLSSLVGSIGQKQAAPYVATKG 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPG----PYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDA 276
Cdd:cd08933   165 AITAMTKALAVDESRYGVRVNCISPGniwtPLWEELAAQTPDTLATIKEGELAQLLGRMGTEAESGLAALFLAAEA 240
PRK06125 PRK06125
short chain dehydrogenase; Provisional
46-290 4.91e-33

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 121.69  E-value: 4.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAinyLPEEEKDAAEVIA--LIKAEGRKAIALPGDIRDETFCQNLVEEAv 123
Cdd:PRK06125    4 HLAGKRVLITGASKGIGAAAAEAFAAEGCHLH---LVARDADALEALAadLRAAHGVDVAVHALDLSSPEAREQLAAEA- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 sklGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQ 201
Cdd:PRK06125   80 ---GDIDILVNNAGAIP-GGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKArgSGVIVNVIGAAGENPDADYICGSA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 202 TKACLAVFTKSLAKQLGPKGIRVNAVAPGP-----YWTVLQSSGGQPM---EKVKEFGGDTPLGRPGQPVEIAPLYVTLA 273
Cdd:PRK06125  156 GNAALMAFTRALGGKSLDDGVRVVGVNPGPvatdrMLTLLKGRARAELgdeSRWQELLAGLPLGRPATPEEVADLVAFLA 235
                         250
                  ....*....|....*..
gi 1915223084 274 SDACSYTSGQVWCSDGG 290
Cdd:PRK06125  236 SPRSGYTSGTVVTVDGG 252
PRK08628 PRK08628
SDR family oxidoreductase;
46-290 5.48e-33

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 121.60  E-value: 5.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGAdvaINYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK08628    4 NLKDKVVIVTGGASGIGAAISLRLAEEGA---IPVIFGRSAPDDEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQyRESLEElTTEDFDATFKTNVYAPFWITKAALRHLKAS-SVIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:PRK08628   81 FGRIDGLVNNAGVND-GVGLEA-GREAFVASLERNLIHYYVMAHYCLPHLKASrGAIVNISSKTALTGQGGTSGYAAAKG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQ----SSGGQPMEKVKEFGGDTPLG-RPGQPVEIAPLYVTLASDACSY 279
Cdd:PRK08628  159 AQLALTREWAVALAKDGVRVNAVIPAEVMTPLYenwiATFDDPEAKLAAITAKIPLGhRMTTAEEIADTAVFLLSERSSH 238
                         250
                  ....*....|.
gi 1915223084 280 TSGQVWCSDGG 290
Cdd:PRK08628  239 TTGQWLFVDGG 249
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
46-229 6.81e-33

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 121.04  E-value: 6.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAI---NylpeeekdaAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEA 122
Cdd:COG3967     2 KLTGNTILITGGTSGIGLALAKRLHARGNTVIItgrR---------EEKLEEAAAANPGLHTIVLDVADPASIAALAEQV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 123 VSKLGGLDILINNAGrQQYRESL--EELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLD 198
Cdd:COG3967    73 TAEFPDLNVLINNAG-IMRAEDLldEAEDLADAEREITTNLLGPIRLTAAFLPHLKAqpEAAIVNVSSGLAFVPLAVTPT 151
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1915223084 199 YAQTKACLAVFTKSLAKQLGPKGIRVNAVAP 229
Cdd:COG3967   152 YSATKAALHSYTQSLRHQLKDTSVKVIELAP 182
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
47-290 8.12e-33

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 121.11  E-value: 8.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAevIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:cd08936     8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRA--VATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLK---ASSVIInTSSVQAVKPSPVLLDYAQTK 203
Cdd:cd08936    86 GGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEkrgGGSVVI-VSSVAAFHPFPGLGPYNVSK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQ 283
Cdd:cd08936   165 TALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMDKAVEESMKETLRIRRLGQPEDCAGIVSFLCSEDASYITGE 244

                  ....*..
gi 1915223084 284 VWCSDGG 290
Cdd:cd08936   245 TVVVGGG 251
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
47-231 9.28e-33

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 121.15  E-value: 9.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEG-RKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:cd05332     1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREER--LEEVKSECLELGaPSPHVVPLDMSDLEDAEQVVEEALKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSSVQAVKPSPVLLDYAQTK 203
Cdd:cd05332    79 FGGLDILINNAGISM-RSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQgsIVVVSSIAGKIGVPFRTAYAASK 157
                         170       180
                  ....*....|....*....|....*...
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGP 231
Cdd:cd05332   158 HALQGFFDSLRAELSEPNISVTVVCPGL 185
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
47-290 9.88e-33

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 121.09  E-value: 9.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:cd05330     1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPDAEVLLIKADVSDEAQVEAYVDATVEQF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLK--ASSVIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:cd05330    81 GRIDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMReqGSGMIVNTASVGGIRGVGNQSGYAAAKH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVL------QSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACS 278
Cdd:cd05330   161 GVVGLTRNSAVEYGQYGIRINAIAPGAILTPMvegslkQLGPENPEEAGEEFVSVNPMKRFGEPEEVAAVVAFLLSDDAG 240
                         250
                  ....*....|..
gi 1915223084 279 YTSGQVWCSDGG 290
Cdd:cd05330   241 YVNAAVVPIDGG 252
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
46-293 1.05e-32

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 120.92  E-value: 1.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAInylpeEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:cd05348     1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAV-----LDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVER 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYRESL----EELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIInTSSVQAVKPSPVLLDY 199
Cdd:cd05348    76 FGKLDCFIGNAGIWDYSTSLvdipEEKLDEAFDELFHINVKGYILGAKAALPALYATegSVIF-TVSNAGFYPGGGGPLY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 200 AQTKACLAVFTKSLAKQLGPKgIRVNAVAPGPYWTVLQ--SSGGQPMEKVKEFGGD------TPLGRPGQPVEIAPLYVT 271
Cdd:cd05348   155 TASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDLRgpASLGQGETSISTPPLDdmlksiLPLGFAPEPEDYTGAYVF 233
                         250       260
                  ....*....|....*....|...
gi 1915223084 272 LASDACSYT-SGQVWCSDGGDGV 293
Cdd:cd05348   234 LASRGDNRPaTGTVINYDGGMGV 256
PRK06181 PRK06181
SDR family oxidoreductase;
49-230 1.17e-32

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 120.85  E-value: 1.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAaeVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGG 128
Cdd:PRK06181    1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLAS--LAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 LDILINNAGRqQYRESLEELT-TEDFDATFKTNVYAPFWITKAALRHLKASS-VIINTSSVQAVKPSPVLLDYAQTKACL 206
Cdd:PRK06181   79 IDILVNNAGI-TMWSRFDELTdLSVFERVMRVNYLGAVYCTHAALPHLKASRgQIVVVSSLAGLTGVPTRSGYAASKHAL 157
                         170       180
                  ....*....|....*....|....
gi 1915223084 207 AVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:PRK06181  158 HGFFDSLRIELADDGVAVTVVCPG 181
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
49-290 3.85e-32

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 119.22  E-value: 3.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVIaliKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGG 128
Cdd:cd09761     1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVF--ADIDEERGADFA---EAEGPNLFFVHGDVADETLVKFVVYAMLEKLGR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 LDILINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHL-KASSVIINTSSVQAVKPSPVLLDYAQTKACLA 207
Cdd:cd09761    76 IDVLVNNAARGSKG-ILSSLLLEEWDRILSVNLTGPYELSRYCRDELiKNKGRIINIASTRAFQSEPDSEAYAASKGGLV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 208 VFTKSLAKQLGPKgIRVNAVAPGpyWTVLQSSGGQPMEKVKEFGGDT-PLGRPGQPVEIAPLYVTLASDACSYTSGQVWC 286
Cdd:cd09761   155 ALTHALAMSLGPD-IRVNCISPG--WINTTEQQEFTAAPLTQEDHAQhPAGRVGTPKDIANLVLFLCQQDAGFITGETFI 231

                  ....
gi 1915223084 287 SDGG 290
Cdd:cd09761   232 VDGG 235
PRK12742 PRK12742
SDR family oxidoreductase;
47-292 9.34e-32

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 117.94  E-value: 9.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYlpEEEKDAAEVIAliKAEGRKAIALPGDIRDEtfcqnlVEEAVSKL 126
Cdd:PRK12742    4 FTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTY--AGSKDAAERLA--QETGATAVQTDSADRDA------VIDVVRKS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYRESLEeLTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVK-PSPVLLDYAQTKAC 205
Cdd:PRK12742   74 GALDILVVNAGIAVFGDALE-LDADDIDRLFKINIHAPYHASVEAARQMPEGGRIIIIGSVNGDRmPVAGMAAYAASKSA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 206 LAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFggdTPLGRPGQPVEIAPLYVTLASDACSYTSGQVW 285
Cdd:PRK12742  153 LQGMARGLARDFGPRGITINVVQPGPIDTDANPANGPMKDMMHSF---MAIKRHGRPEEVAGMVAWLAGPEASFVTGAMH 229

                  ....*..
gi 1915223084 286 CSDGGDG 292
Cdd:PRK12742  230 TIDGAFG 236
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-290 1.48e-31

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 119.12  E-value: 1.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSkL 126
Cdd:PRK07792   10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASAL-DASDVLDEIRAAGAKAVAVAGDISQRATADELVATAVG-L 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV---------IINTSSVQAVKPSPVLL 197
Cdd:PRK07792   88 GGLDIVVNNAGITRDR-MLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRAKAKaaggpvygrIVNTSSEAGLVGPVGQA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 198 DYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEkvKEFGGDTPLGrpgqPVEIAPLYVTLASDAC 277
Cdd:PRK07792  167 NYGAAKAGITALTLSAARALGRYGVRANAICPRARTAMTADVFGDAPD--VEAGGIDPLS----PEHVVPLVQFLASPAA 240
                         250
                  ....*....|...
gi 1915223084 278 SYTSGQVWCSDGG 290
Cdd:PRK07792  241 AEVNGQVFIVYGP 253
PRK06484 PRK06484
short chain dehydrogenase; Validated
49-290 2.15e-31

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 122.27  E-value: 2.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAInylpeEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGG 128
Cdd:PRK06484    5 SRVVLVTGAAGGIGRAACQRFARAGDQVVV-----ADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 LDILINNAG-RQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS---SVIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:PRK06484   80 IDVLVNNAGvTDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQghgAAIVNVASGAGLVALPKRTAYSASKA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPG----PYWTVLQSSGGQPMEKVKefgGDTPLGRPGQPVEIAPLYVTLASDACSYT 280
Cdd:PRK06484  160 AVISLTRSLACEWAAKGIRVNAVLPGyvrtQMVAELERAGKLDPSAVR---SRIPLGRLGRPEEIAEAVFFLASDQASYI 236
                         250
                  ....*....|
gi 1915223084 281 SGQVWCSDGG 290
Cdd:PRK06484  237 TGSTLVVDGG 246
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-290 2.98e-31

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 116.60  E-value: 2.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADV-AINYlpEEEKDAAEVIALIKAegrkaialpgDIRDEtfcqnlVEEAVSK 125
Cdd:PRK06550    3 FMTKTVLITGAASGIGLAQARAFLAQGAQVyGVDK--QDKPDLSGNFHFLQL----------DLSDD------LEPLFDW 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK06550   65 VPSVDILCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLErkSGIIINMCSIASFVAGGGGAAYTASK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQ 283
Cdd:PRK06550  145 HALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMTAADFEPGGLADWVARETPIKRWAEPEEVAELTLFLASGKADYMQGT 224

                  ....*..
gi 1915223084 284 VWCSDGG 290
Cdd:PRK06550  225 IVPIDGG 231
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
47-290 4.79e-31

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 116.51  E-value: 4.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGAD-VAINYLpeeekDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK08993    8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDiVGINIV-----EPTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS---SVIINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK08993   83 FGHIDILVNNAGLIR-REDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgngGKIINIASMLSFQGGIRVPSYTAS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSG 282
Cdd:PRK08993  162 KSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRSAEILDRIPAGRWGLPSDLMGPVVFLASSASDYING 241

                  ....*...
gi 1915223084 283 QVWCSDGG 290
Cdd:PRK08993  242 YTIAVDGG 249
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
49-290 5.15e-31

rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has bifunctional proteins with an N-terminal aldolase and a C-terminal classical SDR domain. One member is identified as a rhamnulose-1-phosphate aldolase/alcohol dehydrogenase. The SDR domain has a canonical SDR glycine-rich NAD(P) binding motif and a match to the characteristic active site triad. However, it lacks an upstream active site Asn typical of SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 116.34  E-value: 5.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEekdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGG 128
Cdd:cd08943     1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPE---IAEKVAEAAQGGPRALGVQCDVTSEAQVQSAFEQAVLEFGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 LDILINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAA---LRHLKASSVIINTSSVQAVKPSPVLLDYAQTKAC 205
Cdd:cd08943    78 LDIVVSNAGIATSS-PIAETSLEDWNRSMDINLTGHFLVSREAfriMKSQGIGGNIVFNASKNAVAPGPNAAAYSAAKAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 206 LAVFTKSLAKQLGPKGIRVNAVAP-----GPYWTVLQSSGGQPMEK---VKEFGGDTPLGRPGQPVEIAPLYVTLASDAC 277
Cdd:cd08943   157 EAHLARCLALEGGEDGIRVNTVNPdavfrGSKIWEGVWRAARAKAYgllEEEYRTRNLLKREVLPEDVAEAVVAMASEDF 236
                         250
                  ....*....|...
gi 1915223084 278 SYTSGQVWCSDGG 290
Cdd:cd08943   237 GKTTGAIVTVDGG 249
PRK06057 PRK06057
short chain dehydrogenase; Provisional
45-290 9.76e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 115.60  E-value: 9.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAevialikAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK06057    3 QRLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAA-------ADEVGGLFVPTDVTDEDAVNALFDTAAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQYRE-SLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPV-LLDYA 200
Cdd:PRK06057   76 TYGSVDIAFNNAGISPPEDdSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRqgKGSIINTASFVAVMGSATsQISYT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWT-VLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSY 279
Cdd:PRK06057  156 ASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTpLLQELFAKDPERAARRLVHVPMGRFAEPEEIAAAVAFLASDDASF 235
                         250
                  ....*....|.
gi 1915223084 280 TSGQVWCSDGG 290
Cdd:PRK06057  236 ITASTFLVDGG 246
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
52-290 1.04e-30

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 115.26  E-value: 1.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAaevialikaEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLDI 131
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLE---------YGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQTKACLAVF 209
Cdd:cd05331    72 LVNCAGVLRP-GATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDrrTGAIVTVASNAAHVPRISMAAYGASKAALASL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 210 TKSLAKQLGPKGIRVNAVAPGP-----YWTVLQSSGG--QPMEKVKE-FGGDTPLGRPGQPVEIAPLYVTLASDACSYTS 281
Cdd:cd05331   151 SKCLGLELAPYGVRCNVVSPGStdtamQRTLWHDEDGaaQVIAGVPEqFRLGIPLGKIAQPADIANAVLFLASDQAGHIT 230

                  ....*....
gi 1915223084 282 GQVWCSDGG 290
Cdd:cd05331   231 MHDLVVDGG 239
PRK07062 PRK07062
SDR family oxidoreductase;
47-282 1.11e-30

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 115.91  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK07062    6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFPGARLLAARCDVLDEADVAAFAAAVEARF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:PRK07062   86 GGVDMLVNNAG-QGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAasIVCVNSLLALQPEPHMVATSAARA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGpywtvLQSSG---------GQPMEKVKEFGGD------TPLGRPGQPVEIAPLY 269
Cdd:PRK07062  165 GLLNLVKSLATELAPKGVRVNSILLG-----LVESGqwrrryearADPGQSWEAWTAAlarkkgIPLGRLGRPDEAARAL 239
                         250
                  ....*....|...
gi 1915223084 270 VTLASDACSYTSG 282
Cdd:PRK07062  240 FFLASPLSSYTTG 252
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
47-294 1.16e-30

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 115.40  E-value: 1.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAaeviaLIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK12936    4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEA-----LAAELGERVKIFPANLSDRDEVKALGQKAEADL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQqyRESL-EELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK12936   79 EGVDILVNNAGIT--KDGLfVRMSDEDWDSVLEVNLTATFRLTRELTHPMmrRRYGRIINITSVVGVTGNPGQANYCASK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQssgGQPMEKVKE-FGGDTPLGRPGQPVEIAPLYVTLASDACSYTSG 282
Cdd:PRK12936  157 AGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMT---GKLNDKQKEaIMGAIPMKRMGTGAEVASAVAYLASSEAAYVTG 233
                         250
                  ....*....|..
gi 1915223084 283 QVWCSDGGDGVI 294
Cdd:PRK12936  234 QTIHVNGGMAMI 245
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
47-230 1.58e-30

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 114.94  E-value: 1.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEE--EKDAAEvialIKAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:cd08934     1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDrlEALADE----LEAEGGKALVLELDVTDEQQVDAAVERTVE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSSVQAVKPSPVLLDYAQT 202
Cdd:cd08934    77 ALGRLDILVNNAGIMLL-GPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKgtIVNISSVAGRVAVRNSAVYNAT 155
                         170       180
                  ....*....|....*....|....*...
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:cd08934   156 KFGVNAFSEGLRQEVTERGVRVVVIEPG 183
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
47-290 1.76e-30

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 114.85  E-value: 1.76e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK08085    7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAER--AELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:PRK08085   85 GPIDVLINNAGIQR-RHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMvkRQAGKIINICSMQSELGRDTITPYAASKG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQssggQPMEKVKEFGG----DTPLGRPGQPVEIAPLYVTLASDACSYT 280
Cdd:PRK08085  164 AVKMLTRGMCVELARHNIQVNGIAPGYFKTEMT----KALVEDEAFTAwlckRTPAARWGDPQELIGAAVFLSSKASDFV 239
                         250
                  ....*....|
gi 1915223084 281 SGQVWCSDGG 290
Cdd:PRK08085  240 NGHLLFVDGG 249
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
48-290 3.17e-30

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 114.31  E-value: 3.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  48 TGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEvialikAEGRKAIALPGDIRDETFCQNLVEEAVSKLG 127
Cdd:cd05371     1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVA------KLGDNCRFVPVDVTSEKDVKAALALAKAKFG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 128 GLDILINNAG-----RQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--------VIINTSSVQAVKPSP 194
Cdd:cd05371    75 RLDIVVNCAGiavaaKTYNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEpdqggergVIINTASVAAFEGQI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 195 VLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLqsSGGQPmEKVKEFGGDT--PLGRPGQPVEIAPLYVTL 272
Cdd:cd05371   155 GQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPL--LAGLP-EKVRDFLAKQvpFPSRLGDPAEYAHLVQHI 231
                         250
                  ....*....|....*...
gi 1915223084 273 ASDacSYTSGQVWCSDGG 290
Cdd:cd05371   232 IEN--PYLNGEVIRLDGA 247
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
45-290 5.67e-30

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 113.44  E-value: 5.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVA---INYLPEEEKDAAEVIAlikaegrkaialpgDIRDETFCQNLVEE 121
Cdd:PRK08220    4 MDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIgfdQAFLTQEDYPFATFVL--------------DVSDAAAVAQVCQR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 122 AVSKLGGLDILINNAG--RQQyreSLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLL 197
Cdd:PRK08220   70 LLAETGPLDVLVNAAGilRMG---ATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRqrSGAIVTVGSNAAHVPRIGMA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 198 DYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSS---GGQPMEKVKEFGGDT-----PLGRPGQPVEIAPLY 269
Cdd:PRK08220  147 AYGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMQRTlwvDEDGEQQVIAGFPEQfklgiPLGKIARPQEIANAV 226
                         250       260
                  ....*....|....*....|.
gi 1915223084 270 VTLASDACSYTSGQVWCSDGG 290
Cdd:PRK08220  227 LFLASDLASHITLQDIVVDGG 247
PRK12744 PRK12744
SDR family oxidoreductase;
47-231 8.25e-30

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 113.30  E-value: 8.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGAD-VAINY-LPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK12744    6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKaVAIHYnSAASKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQqYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLK--ASSVIINTSSVQAVkpSPVLLDYAQT 202
Cdd:PRK12744   86 AFGRPDIAINTVGKV-LKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHLNdnGKIVTLVTSLLGAF--TPFYSAYAGS 162
                         170       180
                  ....*....|....*....|....*....
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGP 231
Cdd:PRK12744  163 KAPVEHFTRAASKEFGARGISVTAVGPGP 191
PRK07677 PRK07677
short chain dehydrogenase; Provisional
49-290 9.00e-30

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 113.23  E-value: 9.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEviALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGG 128
Cdd:PRK07677    1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAK--LEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 LDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHL---KASSVIINTSSVQAVKPSPVLLDYAQTKAC 205
Cdd:PRK07677   79 IDALINNAA-GNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWiekGIKGNIINMVATYAWDAGPGVIHSAAAKAG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 206 LAVFTKSLAKQLGPK-GIRVNAVAPGPywtvLQSSGG-----QPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSY 279
Cdd:PRK07677  158 VLAMTRTLAVEWGRKyGIRVNAIAPGP----IERTGGadklwESEEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAAY 233
                         250
                  ....*....|.
gi 1915223084 280 TSGQVWCSDGG 290
Cdd:PRK07677  234 INGTCITMDGG 244
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
47-290 1.80e-29

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 113.07  E-value: 1.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK08277    8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAI--LDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAG--------RQQYRESLEELTT------EDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAV 190
Cdd:PRK08277   86 GPCDILINGAGgnhpkattDNEFHELIEPTKTffdldeEGFEFVFDLNLLGTLLPTQVFAKDMvgRKGGNIINISSMNAF 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 191 KPSPVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWT-----VLQSSGGQPMEKVKEFGGDTPLGRPGQPVEI 265
Cdd:PRK08277  166 TPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTeqnraLLFNEDGSLTERANKILAHTPMGRFGKPEEL 245
                         250       260
                  ....*....|....*....|....*.
gi 1915223084 266 APLYVTLASD-ACSYTSGQVWCSDGG 290
Cdd:PRK08277  246 LGTLLWLADEkASSFVTGVVLPVDGG 271
PRK12747 PRK12747
short chain dehydrogenase; Provisional
47-290 2.48e-29

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 112.09  E-value: 2.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkDAAEVIALIKAEGRKAIALPGDIRD----ETFCQNLVEEA 122
Cdd:PRK12747    2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKE-EAEETVYEIQSNGGSAFSIGANLESlhgvEALYSSLDNEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 123 VSKLGG--LDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLLDYA 200
Cdd:PRK12747   81 QNRTGStkFDILINNAGIGP-GAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNSRIINISSAATRISLPDFIAYS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSS-GGQPMekVKEFGGD-TPLGRPGQPVEIAPLYVTLASDACS 278
Cdd:PRK12747  160 MTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAElLSDPM--MKQYATTiSAFNRLGEVEDIADTAAFLASPDSR 237
                         250
                  ....*....|..
gi 1915223084 279 YTSGQVWCSDGG 290
Cdd:PRK12747  238 WVTGQLIDVSGG 249
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
47-290 4.01e-29

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 111.54  E-value: 4.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGAD-VAINYlpeeeKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK12481    6 LNGKVAIITGCNTGLGQGMAIGLAKAGADiVGVGV-----AEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS---VIINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK12481   81 MGHIDILINNAGIIR-RQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGnggKIINIASMLSFQGGIRVPSYTAS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSG 282
Cdd:PRK12481  160 KSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALRADTARNEAILERIPASRWGTPDDLAGPAIFLSSSASDYVTG 239

                  ....*...
gi 1915223084 283 QVWCSDGG 290
Cdd:PRK12481  240 YTLAVDGG 247
PRK12746 PRK12746
SDR family oxidoreductase;
47-290 4.13e-29

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 111.28  E-value: 4.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYlPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK12746    4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIHY-GRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 ------GGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLLDYA 200
Cdd:PRK12746   83 qirvgtSEIDILVNNAGIGT-QGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAEGRVINISSAEVRLGFTGSIAYG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEkVKEFGGDTPL-GRPGQPVEIAPLYVTLASDACSY 279
Cdd:PRK12746  162 LSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDDPE-IRNFATNSSVfGRIGQVEDIADAVAFLASSDSRW 240
                         250
                  ....*....|.
gi 1915223084 280 TSGQVWCSDGG 290
Cdd:PRK12746  241 VTGQIIDVSGG 251
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
52-230 7.94e-29

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 110.41  E-value: 7.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLDI 131
Cdd:cd05339     2 VLITGGGSGIGRLLALEFAKRGAKVVI--LDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTKACLAVF 209
Cdd:cd05339    80 LINNAGVVSGK-KLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMleRNHGHIVTIASVAGLISPAGLADYCASKAAAVGF 158
                         170       180
                  ....*....|....*....|....
gi 1915223084 210 TKSLA---KQLGPKGIRVNAVAPG 230
Cdd:cd05339   159 HESLRlelKAYGKPGIKTTLVCPY 182
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
49-230 1.04e-28

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 110.78  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVIALIKAEGRKAI--------ALPGDIRdeTFCQNLVE 120
Cdd:cd05327     1 GKVVVITGANSGIGKETARELAKRGAHVII--ACRNEEKGEEAAAEIKKETGNAKveviqldlSSLASVR--QFAEEFLA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 121 eavsKLGGLDILINNAGrqqYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSV----------- 187
Cdd:cd05327    77 ----RFPRLDILINNAG---IMAPPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASapSRIVNVSSIahragpidfnd 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1915223084 188 ----QAVKPSPVLLdYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:cd05327   150 ldleNNKEYSPYKA-YGQSKLANILFTRELARRLEGTGVTVNALHPG 195
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
50-230 2.70e-28

classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 108.36  E-value: 2.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINylpeeEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGL 129
Cdd:cd08929     1 KAALVTGASRGIGEATARLLHAEGYRVGIC-----ARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAGRQQYReSLEELTTEDFDATFKTNVY-APFWITKAALRHLKAS-SVIINTSSVQAVKPSPVLLDYAQTKACLA 207
Cdd:cd08929    76 DALVNNAGVGVMK-PVEELTPEEWRLVLDTNLTgAFYCIHKAAPALLRRGgGTIVNVGSLAGKNAFKGGAAYNASKFGLL 154
                         170       180
                  ....*....|....*....|...
gi 1915223084 208 VFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:cd08929   155 GLSEAAMLDLREANIRVVNVMPG 177
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
49-290 3.97e-28

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 108.44  E-value: 3.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITG--GDSGIGRAVAIAYAREGADVAINYLPEEEKDaaEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:cd05372     1 GKRILITGiaNDRSIAWGIAKALHEAGAELAFTYQPEALRK--RVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDIL---INNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:cd05372    79 GKLDGLvhsIAFAPKVQLKGPFLDTSRKGFLKALDISAYSLVSLAKAALPIMNPGGSIVTLSYLGSERVVPGYNVMGVAK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTvLQSSGGQPMEKVKEFGGDT-PLGRPGQPVEIAPLYVTLASDACSYTSG 282
Cdd:cd05372   159 AALESSVRYLAYELGRKGIRVNAISAGPIKT-LAASGITGFDKMLEYSEQRaPLGRNVTAEEVGNTAAFLLSDLSSGITG 237

                  ....*...
gi 1915223084 283 QVWCSDGG 290
Cdd:cd05372   238 EIIYVDGG 245
PRK06949 PRK06949
SDR family oxidoreductase;
47-292 4.44e-28

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 108.70  E-value: 4.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK06949    7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVER--LKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV----------IINTSSVQAVKPSPVL 196
Cdd:PRK06949   85 GTIDILVNNSGVST-TQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKgagntkpggrIINIASVAGLRVLPQI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 197 LDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPG--------PYWtvlQSSGGQPMEKVkefggdTPLGRPGQPVEIAPL 268
Cdd:PRK06949  164 GLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGyidteinhHHW---ETEQGQKLVSM------LPRKRVGKPEDLDGL 234
                         250       260
                  ....*....|....*....|....
gi 1915223084 269 YVTLASDACSYTSGQVWCSDGGDG 292
Cdd:PRK06949  235 LLLLAADESQFINGAIISADDGFG 258
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
47-246 5.26e-28

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 107.78  E-value: 5.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAevialiKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:cd05370     3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEA------KKELPNIHTIVLDVGDAESVEALAEALLSEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYRESL-EELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:cd05370    77 PNLDILINNAGIQRPIDLRdPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKqpEATIVNVSSGLAFVPMAANPVYCATK 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEK 246
Cdd:cd05370   157 AALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGG 199
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
50-255 7.42e-28

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 107.32  E-value: 7.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGA-DVainYL-PEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLG 127
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSGPgTV---ILtARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 128 GLDILINNAG-----RQQYRESLEELTTedfdaTFKTNVYAPFWITKAALRHLKASSV--IINTSSVQAVKPSPvlldYA 200
Cdd:cd05324    78 GLDILVNNAGiafkgFDDSTPTREQARE-----TMKTNFFGTVDVTQALLPLLKKSPAgrIVNVSSGLGSLTSA----YG 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGqpmEKVKEFGGDTP 255
Cdd:cd05324   149 VSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGGGKA---PKTPEEGAETP 200
PRK05650 PRK05650
SDR family oxidoreductase;
50-239 1.11e-27

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 107.82  E-value: 1.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGL 129
Cdd:PRK05650    1 NRVMITGAASGLGRAIALRWAREGWRLALADVNEEG--GEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSSVQAVKPSPVLLDYAQTKACLA 207
Cdd:PRK05650   79 DVIVNNAGVASG-GFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSgrIVNIASMAGLMQGPAMSSYNVAKAGVV 157
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1915223084 208 VFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSS 239
Cdd:PRK05650  158 ALSETLLVELADDEIGVHVVCPSFFQTNLLDS 189
PRK08263 PRK08263
short chain dehydrogenase; Provisional
48-240 3.41e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 106.66  E-value: 3.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  48 TGKKALITGGDSGIGRAVAIAYAREGADVAinylpEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLG 127
Cdd:PRK08263    2 MEKVWFITGASRGFGRAWTEAALERGDRVV-----ATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 128 GLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQTKAC 205
Cdd:PRK08263   77 RLDIVVNNAGYGLF-GMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREqrSGHIIQISSIGGISAFPMSGIYHASKWA 155
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1915223084 206 LAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSG 240
Cdd:PRK08263  156 LEGMSEALAQEVAEFGIKVTLVEPGGYSTDWAGTS 190
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
47-290 3.51e-27

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 106.26  E-value: 3.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITG--GDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIAlikAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:COG0623     3 LKGKRGLITGvaNDRSIAWGIAKALHEEGAELAFTYQGEALKKRVEPLA---EELGSALVLPCDVTDDEQIDALFDEIKE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDIL---INNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKpspVLLDY-- 199
Cdd:COG0623    80 KWGKLDFLvhsIAFAPKEELGGRFLDTSREGFLLAMDISAYSLVALAKAAEPLMNEGGSIVTLTYLGAER---VVPNYnv 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 200 -AQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTvLQSSGgqpmekVKEFGGD-------TPLGRPGQPVEIAPLYVT 271
Cdd:COG0623   157 mGVAKAALEASVRYLAADLGPKGIRVNAISAGPIKT-LAASG------IPGFDKLldyaeerAPLGRNVTIEEVGNAAAF 229
                         250
                  ....*....|....*....
gi 1915223084 272 LASDACSYTSGQVWCSDGG 290
Cdd:COG0623   230 LLSDLASGITGEIIYVDGG 248
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
52-230 1.42e-26

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 103.91  E-value: 1.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAI----NylpeeEKDAAEVIALIKAEGRkAIALPGDIRDETfcQNLVEEAVSKLG 127
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGNNTVIatcrD-----PSAATELAALGASHSR-LHILELDVTDEI--AESAEAVAERLG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 128 --GLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTS----SVQAVKPSPVLLdY 199
Cdd:cd05325    73 daGLDVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGarAKIINISsrvgSIGDNTSGGWYS-Y 151
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1915223084 200 AQTKACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:cd05325   152 RASKAALNMLTKSLAVELKRDGITVVSLHPG 182
PRK08278 PRK08278
SDR family oxidoreductase;
47-229 3.06e-26

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 104.22  E-value: 3.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAI--------NYLPEEEKDAAEVIaliKAEGRKAIALPGDIRDETFCQNL 118
Cdd:PRK08278    4 LSGKTLFITGASRGIGLAIALRAARDGANIVIaaktaephPKLPGTIHTAAEEI---EAAGGQALPLVGDVRDEDQVAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 119 VEEAVSKLGGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSsvqavkPsPVL 196
Cdd:PRK08278   81 VAKAVERFGGIDICVNNASAINL-TGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENphILTLS------P-PLN 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1915223084 197 LD---------YAQTKACLAVFTKSLAKQLGPKGIRVNAVAP 229
Cdd:PRK08278  153 LDpkwfaphtaYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
PRK07454 PRK07454
SDR family oxidoreductase;
50-233 4.15e-26

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 103.12  E-value: 4.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGL 129
Cdd:PRK07454    7 PRALITGASSGIGKATALAFAKAGWDLAL--VARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPSPVLLDYAQTKACLA 207
Cdd:PRK07454   85 DVLINNAG-MAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGggLIINVSSIAARNAFPQWGAYCVSKAALA 163
                         170       180       190
                  ....*....|....*....|....*....|
gi 1915223084 208 VFTKSLAKQLGPKGIRVNAVAPG----PYW 233
Cdd:PRK07454  164 AFTKCLAEEERSHGIRVCTITLGavntPLW 193
PRK05855 PRK05855
SDR family oxidoreductase;
42-230 4.82e-26

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 107.37  E-value: 4.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  42 KGHGRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEE 121
Cdd:PRK05855  308 RPRGPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAA--AERTAELIRAAGAVAHAYRVDVSDADAMEAFAEW 385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 122 AVSKLGGLDILINNAGRQQYRESLEElTTEDFDATFKTNVYAPFWITKAALRHLKASSV---IINTSSVQAVKPSPVLLD 198
Cdd:PRK05855  386 VRAEHGVPDIVVNNAGIGMAGGFLDT-SAEDWDRVLDVNLWGVIHGCRLFGRQMVERGTgghIVNVASAAAYAPSRSLPA 464
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1915223084 199 YAQTKACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:PRK05855  465 YATSKAAVLMLSECLRAELAAAGIGVTAICPG 496
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
47-283 7.42e-26

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 102.27  E-value: 7.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVIALIKAEGR-KAIALPGDIRDET--FCQNLVEEAV 123
Cdd:cd05340     2 LNDRIILVTGASDGIGREAALTYARYGATVIL--LGRNEEKLRQVADHINEEGGrQPQWFILDLLTCTseNCQQLAQRIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSPVLLDYAQ 201
Cdd:cd05340    80 VNYPRLDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSdaGSLVFTSSSVGRQGRANWGAYAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 202 TKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTvlqssggqPMeKVKEFGGDTPLGRPgQPVEIAPLYVTLASDACSYTS 281
Cdd:cd05340   160 SKFATEGL*QVLADEYQQRNLRVNCINPGGTRT--------AM-RASAFPTEDPQKLK-TPADIMPLYLWLMGDDSRRKT 229

                  ..
gi 1915223084 282 GQ 283
Cdd:cd05340   230 GM 231
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
47-290 1.39e-25

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 102.01  E-value: 1.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK12938    1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPR-RVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:PRK12938   80 GEIDVLVNNAGITR-DVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMveRGWGRIINISSVNGQKGQFGQTNYSTAKA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGPYWT-VLQSSGGQPMEKVKefgGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQ 283
Cdd:PRK12938  159 GIHGFTMSLAQEVATKGVTVNTVSPGYIGTdMVKAIRPDVLEKIV---ATIPVRRLGSPDEIGSIVAWLASEESGFSTGA 235

                  ....*..
gi 1915223084 284 VWCSDGG 290
Cdd:PRK12938  236 DFSLNGG 242
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
46-290 1.96e-25

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 101.58  E-value: 1.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEviALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK08217    2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAV--AECGALGTEVRGYAANVTDEEDVEATFAQIAED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAG--------RQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHL---KASSVIINTSSVqAVKPSP 194
Cdd:PRK08217   80 FGQLNGLINNAGilrdgllvKAKDGKVTSKMSLEQFQSVIDVNLTGVFLCGREAAAKMiesGSKGVIINISSI-ARAGNM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 195 VLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLqsSGGQPMEKVKEFGGDTPLGRPGQPVEIAPL--YVtL 272
Cdd:PRK08217  159 GQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEM--TAAMKPEALERLEKMIPVGRLGEPEEIAHTvrFI-I 235
                         250
                  ....*....|....*...
gi 1915223084 273 ASDacsYTSGQVWCSDGG 290
Cdd:PRK08217  236 END---YVTGRVLEIDGG 250
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
45-290 1.98e-25

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 100.99  E-value: 1.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAINylPEEEKDAAEVIALIKAEGrKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK05786    1 MRLKGKKVAIIGVSEGLGYAVAYFALKEGAQVCIN--SRNENKLKRMKKTLSKYG-NIHYVVGDVSSTESARNVIEKAAK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGrqqyreSLEELTTEDF---DATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAV-KPSPVLLDYA 200
Cdd:PRK05786   78 VLNAIDGLVVTVG------GYVEDTVEEFsglEEMLTNHIKIPLYAVNASLRFLKEGSSIVLVSSMSGIyKASPDQLSYA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAVAPGpyWTVLQSSGGQPMEKVKefggdtPLGRPGQPVE-IAPLYVTLASDACSY 279
Cdd:PRK05786  152 VAKAGLAKAVEILASELLGRGIRVNGIAPT--TISGDFEPERNWKKLR------KLGDDMAPPEdFAKVIIWLLTDEADW 223
                         250
                  ....*....|.
gi 1915223084 280 TSGQVWCSDGG 290
Cdd:PRK05786  224 VDGVVIPVDGG 234
PRK06179 PRK06179
short chain dehydrogenase; Provisional
50-250 9.65e-25

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 99.98  E-value: 9.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADV---AINYLPEEEKDAAEVIALikaegrkaialpgDIRDETFCQNLVEEAVSKL 126
Cdd:PRK06179    5 KVALVTGASSGIGRATAEKLARAGYRVfgtSRNPARAAPIPGVELLEL-------------DVTDDASVQAAVDEVIARA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRqqyreSL----EELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYA 200
Cdd:PRK06179   72 GRIDVLVNNAGV-----GLagaaEESSIAQAQALFDTNVFGILRMTRAVLPHMRAqgSGRIINISSVLGFLPAPYMALYA 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEF 250
Cdd:PRK06179  147 ASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNFDANAPEPDSPLAEY 196
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
54-230 1.04e-24

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 98.99  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  54 ITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLDILI 133
Cdd:cd05360     5 ITGASSGIGRATALAFAERGAKVVL--AARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDTWV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 134 NNAGRQQYREsLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPSPVLLDYAQTKACLAVFTK 211
Cdd:cd05360    83 NNAGVAVFGR-FEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGggALINVGSLLGYRSAPLQAAYSASKHAVRGFTE 161
                         170       180
                  ....*....|....*....|.
gi 1915223084 212 SLAKQLGPKG--IRVNAVAPG 230
Cdd:cd05360   162 SLRAELAHDGapISVTLVQPT 182
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
50-294 1.16e-24

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 99.30  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIAliKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGL 129
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELQA--INPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAG---RQQYRESLEEltTEDFDATFKTNVYAPFWITKAALRHLKASS-----VIINTSSVQAVKPSPVLLDYAQ 201
Cdd:cd05323    79 DILINNAGildEKSYLFAGKL--PPPWEKTIDVNLTGVINTTYLALHYMDKNKggkggVIVNIGSVAGLYPAPQFPVYSA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 202 TKACLAVFTKSLAKQLGPK-GIRVNAVAPGPYWTVLqssgGQPMEK-VKEFGGDTPLgrpgQPVE-IAPLYVTLASDACS 278
Cdd:cd05323   157 SKHGVVGFTRSLADLLEYKtGVRVNAICPGFTNTPL----LPDLVAkEAEMLPSAPT----QSPEvVAKAIVYLIEDDEK 228
                         250
                  ....*....|....*.
gi 1915223084 279 ytSGQVWCSDGGDGVI 294
Cdd:cd05323   229 --NGAIWIVDGGKLIE 242
PRK05866 PRK05866
SDR family oxidoreductase;
46-227 1.34e-24

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 100.20  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK05866   37 DLTGKRILLTGASSGIGEAAAEQFARRGATVVA--VARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKR 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYRESLEELTT-EDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSvQAVKP--SPVLLDYA 200
Cdd:PRK05866  115 IGGVDILINNAGRSIRRPLAESLDRwHDVERTMVLNYYAPLRLIRGLAPGMleRGDGHIINVAT-WGVLSeaSPLFSVYN 193
                         170       180
                  ....*....|....*....|....*..
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAV 227
Cdd:PRK05866  194 ASKAALSAVSRVIETEWGDRGVHSTTL 220
PRK07201 PRK07201
SDR family oxidoreductase;
45-222 2.10e-24

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 102.72  E-value: 2.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK07201  367 GPLVGKVVLITGASSGIGRATAIKVAEAGATVFL--VARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILA 444
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRqQYRESLeELTTE---DFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDY 199
Cdd:PRK07201  445 EHGHVDYLVNNAGR-SIRRSV-ENSTDrfhDYERTMAVNYFGAVRLILGLLPHMRErrFGHVVNVSSIGVQTNAPRFSAY 522
                         170       180
                  ....*....|....*....|...
gi 1915223084 200 AQTKACLAVFTKSLAKQLGPKGI 222
Cdd:PRK07201  523 VASKAALDAFSDVAASETLSDGI 545
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
50-230 2.82e-24

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 98.51  E-value: 2.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVainYLPEEEKDAAEVIA--LIKAEGRKAIALPGDIRD----ETFCQNLVEEav 123
Cdd:cd05346     1 KTVLITGASSGIGEATARRFAKAGAKL---ILTGRRAERLQELAdeLGAKFPVKVLPLQLDVSDresiEAALENLPEE-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 skLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQ 201
Cdd:cd05346    76 --FRDIDILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIArnQGHIINLGSIAGRYPYAGGNVYCA 153
                         170       180
                  ....*....|....*....|....*....
gi 1915223084 202 TKACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:cd05346   154 TKAAVRQFSLNLRKDLIGTGIRVTNIEPG 182
PRK07109 PRK07109
short chain dehydrogenase; Provisional
44-213 8.45e-24

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 98.84  E-value: 8.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  44 HGRLTGKKALITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAV 123
Cdd:PRK07109    3 LKPIGRQVVVITGASAGVGRATARAFARRGAKVVL--LARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPSPVLLDYAQ 201
Cdd:PRK07109   81 EELGPIDTWVNNAMVTVF-GPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDrgAIIQVGSALAYRSIPLQSAYCA 159
                         170
                  ....*....|..
gi 1915223084 202 TKACLAVFTKSL 213
Cdd:PRK07109  160 AKHAIRGFTDSL 171
PRK06180 PRK06180
short chain dehydrogenase; Provisional
53-234 8.94e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 97.68  E-value: 8.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  53 LITGGDSGIGRAVAIAYAREGADVAINYlpeeeKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLDIL 132
Cdd:PRK06180    8 LITGVSSGFGRALAQAALAAGHRVVGTV-----RSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFGPIDVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 133 INNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQTKACLAVFT 210
Cdd:PRK06180   83 VNNAG-YGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRArrRGHIVNITSMGGLITMPGIGYYCGSKFALEGIS 161
                         170       180
                  ....*....|....*....|....
gi 1915223084 211 KSLAKQLGPKGIRVNAVAPGPYWT 234
Cdd:PRK06180  162 ESLAKEVAPFGIHVTAVEPGSFRT 185
PRK05875 PRK05875
short chain dehydrogenase; Provisional
47-293 9.88e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 97.57  E-value: 9.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAI-NYLPEEEKDAAEVIALIKAEGrKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK05875    5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIvGRNPDKLAAAAEEIEALKGAG-AVRYEPADVTDEDQVARAVDAATAW 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK05875   84 HGRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGggSFVGISSIAASNTHRWFGAYGVTK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTSGQ 283
Cdd:PRK05875  164 SAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITESPELSADYRACTPLPRVGEVEDVANLAMFLLSDAASWITGQ 243
                         250
                  ....*....|
gi 1915223084 284 VWCSDGGDGV 293
Cdd:PRK05875  244 VINVDGGHML 253
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
49-230 1.20e-23

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 96.55  E-value: 1.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVIALIKAE----GRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:cd08939     1 GKHVLITGGSSGIGKALAKELVKEGANVII--VARSESKLEEAVEEIEAEanasGQKVSYISADLSDYEEVEQAFAQAVE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGrqqYRES--LEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYA 200
Cdd:cd08939    79 KGGPPDLVVNCAG---ISIPglFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEqrPGHIVFVSSQAALVGIYGYSAYC 155
                         170       180       190
                  ....*....|....*....|....*....|
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:cd08939   156 PSKFALRGLAESLRQELKPYNIRVSVVYPP 185
PRK07577 PRK07577
SDR family oxidoreductase;
47-290 1.35e-23

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 96.33  E-value: 1.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGAdvainylpeeekdaaEVIALikaeGRKAialPGDIRDETFCQNLVEEA---- 122
Cdd:PRK07577    1 MSSRTVLVTGATKGIGLALSLRLANLGH---------------QVIGI----ARSA---IDDFPGELFACDLADIEqtaa 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 123 ----VSKLGGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSSvQAVKPSPVL 196
Cdd:PRK07577   59 tlaqINEIHPVDAIVNNVGIALP-QPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQgrIVNICS-RAIFGALDR 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 197 LDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSgGQPM--EKVKEFGGDTPLGRPGQPVEIAPLYVTLAS 274
Cdd:PRK07577  137 TSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETELFRQ-TRPVgsEEEKRVLASIPMRRLGTPEEVAAAIAFLLS 215
                         250
                  ....*....|....*.
gi 1915223084 275 DACSYTSGQVWCSDGG 290
Cdd:PRK07577  216 DDAGFITGQVLGVDGG 231
PRK06914 PRK06914
SDR family oxidoreductase;
49-274 2.75e-23

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 96.25  E-value: 2.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADV-AINYLPEEEKDAAEVIALIKAEGR-KAIALpgDIRDETFCQNlVEEAVSKL 126
Cdd:PRK06914    3 KKIAIVTGASSGFGLLTTLELAKKGYLViATMRNPEKQENLLSQATQLNLQQNiKVQQL--DVTDQNSIHN-FQLVLKEI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLK--ASSVIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:PRK06914   80 GRIDLLVNNAG-YANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRkqKSGKIINISSISGRVGFPGLSPYVSSKY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGPY----WTV------LQSSGGQP----MEKVKEF---GGDTplgrPGQPVEIAP 267
Cdd:PRK06914  159 ALEGFSESLRLELKPFGIDVALIEPGSYntniWEVgkqlaeNQSETTSPykeyMKKIQKHinsGSDT----FGNPIDVAN 234

                  ....*..
gi 1915223084 268 LYVTLAS 274
Cdd:PRK06914  235 LIVEIAE 241
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
47-229 2.97e-23

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 95.59  E-value: 2.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINY--------LPEEEKDAAEVIaliKAEGRKAIALPGDIRDETFCQNL 118
Cdd:cd09762     1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAktaephpkLPGTIYTAAEEI---EAAGGKALPCIVDIRDEDQVRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 119 VEEAVSKLGGLDILINNAGRQQYRESLeELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSsvqavkpSPVL 196
Cdd:cd09762    78 VEKAVEKFGGIDILVNNASAISLTGTL-DTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNphILNLS-------PPLN 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1915223084 197 LD---------YAQTKACLAVFTKSLAKQLGPKGIRVNAVAP 229
Cdd:cd09762   150 LNpkwfknhtaYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PRK05693 PRK05693
SDR family oxidoreductase;
52-247 7.06e-23

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 95.24  E-value: 7.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAINylpeeEKDAAEVIALiKAEGRKAIALpgDIRDETFCQNLVEEAVSKLGGLDI 131
Cdd:PRK05693    4 VLITGCSSGIGRALADAFKAAGYEVWAT-----ARKAEDVEAL-AAAGFTAVQL--DVNDGAALARLAEELEAEHGGLDV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGrqqYRE--SLEELTTEDFDATFKTNVYAPFWITKA---ALRhlKASSVIINTSSVQAVKPSPVLLDYAQTKACL 206
Cdd:PRK05693   76 LINNAG---YGAmgPLLDGGVEAMRRQFETNVFAVVGVTRAlfpLLR--RSRGLVVNIGSVSGVLVTPFAGAYCASKAAV 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1915223084 207 AVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKV 247
Cdd:PRK05693  151 HALSDALRLELAPFGVQVMEVQPGAIASQFASNASREAEQL 191
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
52-230 9.01e-23

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 93.93  E-value: 9.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDaaEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLDI 131
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLD--ELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAELGGLDL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGrqQYR-ESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQTKACLAV 208
Cdd:cd05350    79 VIINAG--VGKgTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAkgRGHLVLISSVAALRGLPGAAAYSASKAALSS 156
                         170       180
                  ....*....|....*....|..
gi 1915223084 209 FTKSLAKQLGPKGIRVNAVAPG 230
Cdd:cd05350   157 LAESLRYDVKKRGIRVTVINPG 178
PRK08264 PRK08264
SDR family oxidoreductase;
49-246 1.03e-22

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 93.80  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRA-VAIAYAREGADVainYLpeeekdAAEVIALIKAEGRKAIALPGDIRDETfcqnLVEEAVSKLG 127
Cdd:PRK08264    6 GKVVLVTGANRGIGRAfVEQLLARGAAKV---YA------AARDPESVTDLGPRVVPLQLDVTDPA----SVAAAAEAAS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 128 GLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQTKAC 205
Cdd:PRK08264   73 DVTILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAAngGGAIVNVLSVLSWVNFPNLGTYSASKAA 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1915223084 206 LAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSsgGQPMEK 246
Cdd:PRK08264  153 AWSLTQALRAELAPQGTRVLGVHPGPIDTDMAA--GLDAPK 191
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
52-290 1.64e-22

haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. Haloalcohol dehalogenase show low sequence similarity to short-chain dehydrogenases/reductases (SDRs). Like the SDRs, haloalcohol dehalogenases have a conserved catalytic triad (Ser-Tyr-Lys/Arg), and form a Rossmann fold. However, the normal classical SDR NAD(P)-binding motif (TGXXGXG) and NAD-binding function is replaced with a halide binding site, allowing the enzyme to catalyze a dehalogenation reaction. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 93.41  E-value: 1.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAINylPEEEKDAAEVIAL-IKAEGRKAIAlpgdirdETFCQNLVEEAVSKLGGLD 130
Cdd:cd05361     4 ALVTHARHFAGPASAEALTEDGYTVVCH--DASFADAAERQAFeSENPGTKALS-------EQKPEELVDAVLQAGGAID 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 131 ILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAA---LRHLKASSVIINTSSVqAVKPSPVLLDYAQTKACLA 207
Cdd:cd05361    75 VLVSNDYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAiaqMKKAGGGSIIFITSAV-PKKPLAYNSLYGPARAAAV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 208 VFTKSLAKQLGPKGIRVNAVAP----GPYW--TVLQSSGGQPMEKVKEfggDTPLGRPGQPVEIAPLYVTLASDACSYTS 281
Cdd:cd05361   154 ALAESLAKELSRDNILVYAIGPnffnSPTYfpTSDWENNPELRERVKR---DVPLGRLGRPDEMGALVAFLASRRADPIT 230

                  ....*....
gi 1915223084 282 GQVWCSDGG 290
Cdd:cd05361   231 GQFFAFAGG 239
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
47-290 2.12e-22

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 93.63  E-value: 2.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITG--GDSGIGRAVAIAYAREGADVAINYLPEE----EKDAAEVIALIKAEgrkaIALPGDIRDETFCQNLVE 120
Cdd:PRK07370    4 LTGKKALVTGiaNNRSIAWGIAQQLHAAGAELGITYLPDEkgrfEKKVRELTEPLNPS----LFLPCDVQDDAQIEETFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 121 EAVSKLGGLDILINN---AGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLL 197
Cdd:PRK07370   80 TIKQKWGKLDILVHClafAGKEELIGDFSATSREGFARALEISAYSLAPLCKAAKPLMSEGGSIVTLTYLGGVRAIPNYN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 198 DYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDAC 277
Cdd:PRK07370  160 VMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTLASSAVGGILDMIHHVEEKAPLRRTVTQTEVGNTAAFLLSDLA 239
                         250
                  ....*....|...
gi 1915223084 278 SYTSGQVWCSDGG 290
Cdd:PRK07370  240 SGITGQTIYVDAG 252
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
46-230 2.53e-22

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 92.96  E-value: 2.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAI--NYLPEEEKDAAEviaLIKAEGRKAIALPGDIRDETFCQNLVEEAV 123
Cdd:cd05343     3 RWRGRVALVTGASVGIGAAVARALVQHGMKVVGcaRRVDKIEALAAE---CQSAGYPTLFPYQCDLSNEEQILSMFSAIR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV----IINTSSV--QAVKPSPVLL 197
Cdd:cd05343    80 TQHQGVDVCINNAG-LARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVddghIININSMsgHRVPPVSVFH 158
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1915223084 198 DYAQTKACLAVFTKSLAKQL--GPKGIRVNAVAPG 230
Cdd:cd05343   159 FYAATKHAVTALTEGLRQELreAKTHIRATSISPG 193
PRK08339 PRK08339
short chain dehydrogenase; Provisional
47-290 7.56e-22

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 92.23  E-value: 7.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVIALIKAEGRKAIA-LPGDIRDETFCQNLVEEaVSK 125
Cdd:PRK08339    6 LSGKLAFTTASSKGIGFGVARVLARAGADVIL--LSRNEENLKKAREKIKSESNVDVSyIVADLTKREDLERTVKE-LKN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK08339   83 IGEPDIFFFSTGGPK-PGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMerKGFGRIIYSTSVAIKEPIPNIALSNVVR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWT---------VLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLAS 274
Cdd:PRK08339  162 ISMAGLVRTLAKELGPKGITVNGIMPGIIRTdrviqlaqdRAKREGKSVEEALQEYAKPIPLGRLGEPEEIGYLVAFLAS 241
                         250
                  ....*....|....*.
gi 1915223084 275 DACSYTSGQVWCSDGG 290
Cdd:PRK08339  242 DLGSYINGAMIPVDGG 257
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
52-292 1.36e-21

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 91.45  E-value: 1.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLDI 131
Cdd:cd08945     6 ALVTGATSGIGLAIARRLGKEGLRVFVCARGEEG--LATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPIDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGRQQYRESlEELTTEDFDATFKTNVYAPFWITKAALRH----LKASSVIINTSSVQA----VKPSPvlldYAQTK 203
Cdd:cd08945    84 LVNNAGRSGGGAT-AELADELWLDVVETNLTGVFRVTKEVLKAggmlERGTGRIINIASTGGkqgvVHAAP----YSASK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPG------------PYWTVLQSSGGQPMEKVKEfggDTPLGRPGQPVEIAPLYVT 271
Cdd:cd08945   159 HGVVGFTKALGLELARTGITVNAVCPGfvetpmaasvreHYADIWEVSTEEAFDRITA---RVPLGRYVTPEEVAGMVAY 235
                         250       260
                  ....*....|....*....|.
gi 1915223084 272 LASDACSYTSGQVWCSDGGDG 292
Cdd:cd08945   236 LIGDGAAAVTAQALNVCGGLG 256
PRK08340 PRK08340
SDR family oxidoreductase;
51-289 2.30e-21

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 90.63  E-value: 2.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  51 KALITGGDSGIGRAVAIAYAREGADVAINYLPEE--EKDAAEVIALIKAEGRKAialpgDIRDETFCQNLVEEAVSKLGG 128
Cdd:PRK08340    2 NVLVTASSRGIGFNVARELLKKGARVVISSRNEEnlEKALKELKEYGEVYAVKA-----DLSDKDDLKNLVKEAWELLGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 LDILINNAGRQQYRES-LEELTTEDFDATFKTNVYAPFWITKAALRHL---KASSVIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:PRK08340   77 IDALVWNAGNVRCEPCmLHEAGYSDWLEAALLHLVAPGYLTTLLIQAWlekKMKGVLVYLSSVSVKEPMPPLVLADVTRA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGPYWT--------VLQSSGGQPMEKV--KEFGGDTPLGRPGQPVEIAPLYVTLAS 274
Cdd:PRK08340  157 GLVQLAKGVSRTYGGKGIRAYTVLLGSFDTpgarenlaRIAEERGVSFEETweREVLERTPLKRTGRWEELGSLIAFLLS 236
                         250
                  ....*....|....*
gi 1915223084 275 DACSYTSGQVWCSDG 289
Cdd:PRK08340  237 ENAEYMLGSTIVFDG 251
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
52-224 2.44e-21

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 90.13  E-value: 2.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALIKAEGRkAIALPGDIRDETFCQNLVEEAVSKLGGLDI 131
Cdd:cd05373     2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGS-AKAVPTDARDEDEVIALFDLIEEEIGPLEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTKACLAVF 209
Cdd:cd05373    81 LVYNAGANVWF-PILETTPRVFEKVWEMAAFGGFLAAREAAKRMlaRGRGTIIFTGATASLRGRAGFAAFAGAKFALRAL 159
                         170
                  ....*....|....*
gi 1915223084 210 TKSLAKQLGPKGIRV 224
Cdd:cd05373   160 AQSMARELGPKGIHV 174
PLN02253 PLN02253
xanthoxin dehydrogenase
46-290 6.02e-21

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 89.88  E-value: 6.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLpeeEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PLN02253   15 RLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDL---QDDLGQNVCDSLGGEPNVCFFHCDVTVEDDVSRAVDFTVDK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQ-QYRESLEELTTEDFDATFKTNVYAPFWITKAALR---HLKASSvIINTSSVQAVKPSPVLLDYAQ 201
Cdd:PLN02253   92 FGTLDIMVNNAGLTgPPCPDIRNVELSEFEKVFDVNVKGVFLGMKHAARimiPLKKGS-IVSLCSVASAIGGLGPHAYTG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 202 TKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLqSSGGQPMEKVKE---------FGGDTPL-GRPGQPVEIAPLYVT 271
Cdd:PLN02253  171 SKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTAL-ALAHLPEDERTEdalagfrafAGKNANLkGVELTVDDVANAVLF 249
                         250
                  ....*....|....*....
gi 1915223084 272 LASDACSYTSGQVWCSDGG 290
Cdd:PLN02253  250 LASDEARYISGLNLMIDGG 268
PRK07074 PRK07074
SDR family oxidoreductase;
52-290 7.49e-21

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 89.44  E-value: 7.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVainYLPEEEKDAAEVIALIKAEGRkAIALPGDIRDETFCQNLVEEAVSKLGGLDI 131
Cdd:PRK07074    5 ALVTGAAGGIGQALARRFLAAGDRV---LALDIDAAALAAFADALGDAR-FVPVACDLTDAASLAAALANAAAERGPVDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQ--AVKPSPVlldYAQTKACLA 207
Cdd:PRK07074   81 LVANAGAAR-AASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSrgAVVNIGSVNgmAALGHPA---YSAAKAGLI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 208 VFTKSLAKQLGPKGIRVNAVAPG----PYWTVLQSSGGQPMEKVKEFggdTPLGRPGQPVEIAPLYVTLASDACSYTSGQ 283
Cdd:PRK07074  157 HYTKLLAVEYGRFGIRANAVAPGtvktQAWEARVAANPQVFEELKKW---YPLQDFATPDDVANAVLFLASPAARAITGV 233

                  ....*..
gi 1915223084 284 VWCSDGG 290
Cdd:PRK07074  234 CLPVDGG 240
PRK05717 PRK05717
SDR family oxidoreductase;
42-290 1.21e-20

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 88.79  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  42 KGHGRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLpeeekDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEE 121
Cdd:PRK05717    3 EPNPGHNGRVALVTGAARGIGLGIAAWLIAEGWQVVLADL-----DRERGSKVAKALGENAWFIAMDVADEAQVAAGVAE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 122 AVSKLGGLDILINNAG-RQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA-SSVIINTSSVQAVKPSPVLLDY 199
Cdd:PRK05717   78 VLGQFGRLDALVCNAAiADPHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAhNGAIVNLASTRARQSEPDTEAY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 200 AQTKACLAVFTKSLAKQLGPKgIRVNAVAPGpyWTVLQSSGGQPMEKVKEFGGDT-PLGRPGQPVEIAPLYVTLASDACS 278
Cdd:PRK05717  158 AASKGGLLALTHALAISLGPE-IRVNAVSPG--WIDARDPSQRRAEPLSEADHAQhPAGRVGTVEDVAAMVAWLLSRQAG 234
                         250
                  ....*....|..
gi 1915223084 279 YTSGQVWCSDGG 290
Cdd:PRK05717  235 FVTGQEFVVDGG 246
PRK07041 PRK07041
SDR family oxidoreductase;
53-290 4.50e-20

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 86.63  E-value: 4.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  53 LITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAeviALIKAEGRKAIALPGDIRDETFCQNLVEEAvsklGGLDIL 132
Cdd:PRK07041    1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAA---ARALGGGAPVRTAALDITDEAAVDAFFAEA----GPFDHV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 133 INNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAAlrHLKASSVIINTSSVQAVKPSPVLLDYAQTKACLAVFTKS 212
Cdd:PRK07041   74 VITAA-DTPGGPVRALPLAAAQAAMDSKFWGAYRVARAA--RIAPGGSLTFVSGFAAVRPSASGVLQGAINAALEALARG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 213 LAKQLGPkgIRVNAVAPG----PYWTVLQSSGGQPMekvkeFGGDT---PLGRPGQPVEIAPLYVTLASDAcsYTSGQVW 285
Cdd:PRK07041  151 LALELAP--VRVNTVSPGlvdtPLWSKLAGDAREAM-----FAAAAerlPARRVGQPEDVANAILFLAANG--FTTGSTV 221

                  ....*
gi 1915223084 286 CSDGG 290
Cdd:PRK07041  222 LVDGG 226
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
49-230 5.00e-20

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 86.50  E-value: 5.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADV-AINYLPEEEKDAAEVIAL-IKAEGRKAIAlpGDIRDETFCQNLVEEavskL 126
Cdd:cd05356     1 GTWAVVTGATDGIGKAYAEELAKRGFNViLISRTQEKLDAVAKEIEEkYGVETKTIAA--DFSAGDDIYERIEKE----L 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDI--LINNAGR-QQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKPSPVLLDYAQ 201
Cdd:cd05356    75 EGLDIgiLVNNVGIsHSIPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKkgAIVNISSFAGLIPTPLLATYSA 154
                         170       180
                  ....*....|....*....|....*....
gi 1915223084 202 TKACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:cd05356   155 SKAFLDFFSRALYEEYKSQGIDVQSLLPY 183
PRK07825 PRK07825
short chain dehydrogenase; Provisional
46-230 5.40e-20

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 87.30  E-value: 5.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEeekDAAEVIAlikAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK07825    2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDE---ALAKETA---AELGLVVGGPLDVTDPASFAAFLDAVEAD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYRESLEElTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK07825   76 LGPIDVLVNNAGVMPVGPFLDE-PDAVTRRILDVNVYGVILGSKLAAPRMVPrgRGHVVNVASLAGKIPVPGMATYCASK 154
                         170       180
                  ....*....|....*....|....*..
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:PRK07825  155 HAVVGFTDAARLELRGTGVHVSVVLPS 181
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
47-284 5.93e-20

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 86.47  E-value: 5.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVIALIKAEG-RKAIALPGDIRDETF--CQNLVEEAV 123
Cdd:PRK08945   10 LKDRIILVTGAGDGIGREAALTYARHGATVIL--LGRTEEKLEAVYDEIEAAGgPQPAIIPLDLLTATPqnYQQLADTIE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS---SVIINTSSVQAvKPSPVLLDYA 200
Cdd:PRK08945   88 EQFGRLDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSpaaSLVFTSSSVGR-QGRANWGAYA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTvlqssggqPMeKVKEFGGDTPLGRPGqPVEIAPLYVTLASDACSYT 280
Cdd:PRK08945  167 VSKFATEGMMQVLADEYQGTNLRVNCINPGGTRT--------AM-RASAFPGEDPQKLKT-PEDIMPLYLYLMGDDSRRK 236

                  ....
gi 1915223084 281 SGQV 284
Cdd:PRK08945  237 NGQS 240
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
47-245 6.77e-20

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 86.31  E-value: 6.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGAdvAINYLPEeeKDAAEVIALIKAEGRKAIALPGDIRDETfcqnLVEEAVSKL 126
Cdd:cd05354     1 IKDKTVLVTGANRGIGKAFVESLLAHGA--KKVYAAV--RDPGSAAHLVAKYGDKVVPLRLDVTDPE----SIKAAAAQA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:cd05354    73 KDVDVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANggGAIVNLNSVASLKNFPAMGTYSASKS 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPME 245
Cdd:cd05354   153 AAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAGGPKE 193
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-230 1.23e-19

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 88.35  E-value: 1.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALIKAEgrkaiALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK08261  208 LAGKVALVTGAARGIGAAIAEVLARDGAHVVCLDVPAAGEALAAVANRVGGT-----ALALDITAPDAPARIAEHLAERH 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAG--RQQyreSLEELTTEDFDATFKTNVYAPFWITKAALR--HLKASSVIINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK08261  283 GGLDIVVHNAGitRDK---TLANMDEARWDSVLAVNLLAPLRITEALLAagALGDGGRIVGVSSISGIAGNRGQTNYAAS 359
                         170       180
                  ....*....|....*....|....*...
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:PRK08261  360 KAGVIGLVQALAPLLAERGITINAVAPG 387
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
52-290 1.90e-19

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 85.75  E-value: 1.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETF----CQNLVEEAVSKLG 127
Cdd:TIGR02685   4 AVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTLAAELNARRPNSAVTCQADLSNSATlfsrCEAIIDACFRAFG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 128 GLDILINNAG--------RQQYRESLEELTTEDFDAT--FKTNVYAPFWITKAALRHLK--------ASSVIINTSSVQA 189
Cdd:TIGR02685  84 RCDVLVNNASafyptpllRGDAGEGVGDKKSLEVQVAelFGSNAIAPYFLIKAFAQRQAgtraeqrsTNLSIVNLCDAMT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 190 VKPSPVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGpyWTVLQSSggQPMEKVKEFGGDTPLG-RPGQPVEIAPL 268
Cdd:TIGR02685 164 DQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPG--LSLLPDA--MPFEVQEDYRRKVPLGqREASAEQIADV 239
                         250       260
                  ....*....|....*....|..
gi 1915223084 269 YVTLASDACSYTSGQVWCSDGG 290
Cdd:TIGR02685 240 VIFLVSPKAKYITGTCIKVDGG 261
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
53-238 5.31e-19

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 83.87  E-value: 5.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  53 LITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIALIkAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLDIL 132
Cdd:cd05367     3 ILTGASRGIGRALAEELLKRGSPSVVVLLARSEEPLQELKEEL-RPGLRVTTVKADLSDAAGVEQLLEAIRKLDGERDLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 133 INNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV---IINTSSVQAVKPSPVLLDYAQTKACLAVF 209
Cdd:cd05367    82 INNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkktVVNVSSGAAVNPFKGWGLYCSSKAARDMF 161
                         170       180
                  ....*....|....*....|....*....
gi 1915223084 210 TKSLAKQLgpKGIRVNAVAPGPYWTVLQS 238
Cdd:cd05367   162 FRVLAAEE--PDVRVLSYAPGVVDTDMQR 188
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
49-282 6.84e-19

dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an NAD-binding protein related to the SDRs. It converts dihydrobiopterin into tetrahydrobiopterin, a cofactor necessary in catecholamines synthesis. Dihydropteridine reductase has the YXXXK of these tyrosine-dependent oxidoreductases, but lacks the typical upstream Asn and Ser catalytic residues. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 83.14  E-value: 6.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVA-INYLPEEEKDAAevialikaegrkaIALPGDIRDETFCQNLVEEAVSKLG 127
Cdd:cd05334     1 ARVVLVYGGRGALGSAVVQAFKSRGWWVAsIDLAENEEADAS-------------IIVLDSDSFTEQAKQVVASVARLSG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 128 GLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLLDYAQTKACLA 207
Cdd:cd05334    68 KVDALICVAGGWAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLLSGGLLVLTGAKAALEPTPGMIGYGAAKAAVH 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 208 VFTKSLAKQLG--PKGIRVNAVAPgpywTVLqssggqpmekvkefggDTPLGRPGQP----------VEIAPLYVTLASD 275
Cdd:cd05334   148 QLTQSLAAENSglPAGSTANAILP----VTL----------------DTPANRKAMPdadfsswtplEFIAELILFWASG 207

                  ....*..
gi 1915223084 276 ACSYTSG 282
Cdd:cd05334   208 AARPKSG 214
PRK08267 PRK08267
SDR family oxidoreductase;
50-230 1.97e-18

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 82.68  E-value: 1.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVA---INylpeeEKDAAEVIALIKAEGRKAIALpgDIRDETFCQNLVEEAVSKL 126
Cdd:PRK08267    2 KSIFITGAASGIGRATALLFAAEGWRVGaydIN-----EAGLAALAAELGAGNAWTGAL--DVTDRAAWDAALADFAAAT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GG-LDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK08267   75 GGrLDVLFNNAG-ILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATpgARVINTSSASAIYGQPGLAVYSATK 153
                         170       180
                  ....*....|....*....|....*..
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:PRK08267  154 FAVRGLTEALDLEWRRHGIRVADVMPL 180
PRK06182 PRK06182
short chain dehydrogenase; Validated
50-230 2.10e-18

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 82.70  E-value: 2.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVainYlpeeekDAA---EVIALIKAEGRKAIALpgDIRDETFCQNLVEEAVSKL 126
Cdd:PRK06182    4 KVALVTGASSGIGKATARRLAAQGYTV---Y------GAArrvDKMEDLASLGVHPLSL--DVTDEASIKAAVDTIIAEE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:PRK06182   73 GRIDVLVNNAGYGSY-GAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAqrSGRIINISSMGGKIYTPLGAWYHATKF 151
                         170       180
                  ....*....|....*....|....*.
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:PRK06182  152 ALEGFSDALRLEVAPFGIDVVVIEPG 177
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
48-283 2.82e-18

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 82.39  E-value: 2.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  48 TGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAE-GR-KAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK12384    1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEK--AANVAQEINAEyGEgMAYGFGADATSEQSVLALSRGVDEI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHL---KASSVIINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK12384   79 FGRVDLLVYNAG-IAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMirdGIQGRIIQINSKSGKVGSKHNSGYSAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPG-----PYWTVLQSSG----GQPMEKVKEFGGD-TPLGRPGQPVEIAPLYVTL 272
Cdd:PRK12384  158 KFGGVGLTQSLALDLAEYGITVHSLMLGnllksPMFQSLLPQYakklGIKPDEVEQYYIDkVPLKRGCDYQDVLNMLLFY 237
                         250
                  ....*....|.
gi 1915223084 273 ASDACSYTSGQ 283
Cdd:PRK12384  238 ASPKASYCTGQ 248
PRK09072 PRK09072
SDR family oxidoreductase;
46-229 1.70e-17

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 79.99  E-value: 1.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVaINYLPEEEKDAAEVIALIKAEGRKAIALpgDIRDETFCQNLVEEAvSK 125
Cdd:PRK09072    2 DLKDKRVLLTGASGGIGQALAEALAAAGARL-LLVGRNAEKLEALAARLPYPGRHRWVVA--DLTSEAGREAVLARA-RE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYREsLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:PRK09072   78 MGGINVLINNAGVNHFAL-LEDQDPEAIERLLALNLTAPMQLTRALLPLLRAqpSAMVVNVGSTFGSIGYPGYASYCASK 156
                         170       180
                  ....*....|....*....|....*.
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAP 229
Cdd:PRK09072  157 FALRGFSEALRRELADTGVRVLYLAP 182
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
52-284 3.38e-17

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 78.01  E-value: 3.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVainylpeeekdaaevialIKAeGRKAIALPGDIRDETFCQNLVEEAvsklGGLDI 131
Cdd:cd11731     1 IIVIGATGTIGLAVAQLLSAHGHEV------------------ITA-GRSSGDYQVDITDEASIKALFEKV----GHFDA 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLLDYAQTKACLAVFTK 211
Cdd:cd11731    58 IVSTAGDAEF-APLAELTDADFQRGLNSKLLGQINLVRHGLPYLNDGGSITLTSGILAQRPIPGGAAAATVNGALEGFVR 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915223084 212 SLAKQLgPKGIRVNAVAPGpywtVLQSSGGQPMEKVKEFggdtplgRPGQPVEIAPLYVTLASDAcsyTSGQV 284
Cdd:cd11731   137 AAAIEL-PRGIRINAVSPG----VVEESLEAYGDFFPGF-------EPVPAEDVAKAYVRSVEGA---FTGQV 194
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
47-230 5.55e-17

Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 80.73  E-value: 5.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEGRKAIALPGDI--RDETFCQNLVEEAVS 124
Cdd:COG3347   423 LAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEA--AEAAAAELGGGYGADAVDATDVdvTAEAAVAAAFGFAGL 500
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGrqqYRESL--EELTTEDFDATFKTNVYAPFWITKAALRHLKAS---SVIINTSSVQAVKPSPVLLDY 199
Cdd:COG3347   501 DIGGSDIGVANAG---IASSSpeEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQglgGSSVFAVSKNAAAAAYGAAAA 577
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1915223084 200 AQTKACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:COG3347   578 ATAKAAAQHLLRALAAEGGANGINANRVNPD 608
PRK08219 PRK08219
SDR family oxidoreductase;
52-237 5.93e-17

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 78.05  E-value: 5.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAReGADVAINYLPEEEKDAAEvialikAEGRKAIALPGDIRDETfcqnLVEEAVSKLGGLDI 131
Cdd:PRK08219    6 ALITGASRGIGAAIARELAP-THTLLLGGRPAERLDELA------AELPGATPFPVDLTDPE----AIAAAVEQLGRLDV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGRQQYReSLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS---VIINTSSvqAVKPSPVLLDYAQTKACLAV 208
Cdd:PRK08219   75 LVHNAGVADLG-PVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHghvVFINSGA--GLRANPGWGSYAASKFALRA 151
                         170       180
                  ....*....|....*....|....*....
gi 1915223084 209 FTKSLaKQLGPKGIRVNAVAPGPYWTVLQ 237
Cdd:PRK08219  152 LADAL-REEEPGNVRVTSVHPGRTDTDMQ 179
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
53-290 7.39e-17

alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, which catalyzes the NAD-dependent oxidoreduction of hydroxysteroids, is a dimeric member of the classical SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 78.30  E-value: 7.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  53 LITGGDSGIGRAVAIAYAREGADV-AINYLPeeekdaAEVIA-LIKAEGRKAI--ALPGDIRdetfcqnlveeavsklGG 128
Cdd:cd05328     3 VITGAASGIGAATAELLEDAGHTViGIDLRE------ADVIAdLSTPEGRAAAiaDVLARCS----------------GV 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 LDILINNAGRQQyresleeltTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVK--------------- 191
Cdd:cd05328    61 LDGLVNCAGVGG---------TTVAGLVLKVNYFGLRALMEALLPRLRKGHgpAAVVVSSIAGAGwaqdklelakalaag 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 192 ------------PSPVLLDYAQTKACLAVFTKSLAKQ-LGPKGIRVNAVAPGPYWT-VLQSSGGQPMEKVKEFGGDTPLG 257
Cdd:cd05328   132 tearavalaehaGQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETpILQAFLQDPRGGESVDAFVTPMG 211
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1915223084 258 RPGQPVEIAPLYVTLASDACSYTSGQVWCSDGG 290
Cdd:cd05328   212 RRAEPDEIAPVIAFLASDAASWINGANLFVDGG 244
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
47-290 1.02e-16

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 78.25  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITG--GDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIAlikAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK08415    3 MKGKKGLIVGvaNNKSIAYGIAKACFEQGAELAFTYLNEALKKRVEPIA---QELGSDYVYELDVSKPEHFKSLAESLKK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINN---AGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLLDYAQ 201
Cdd:PRK08415   80 DLGKIDFIVHSvafAPKEALEGSFLETSKEAFNIAMEISVYSLIELTRALLPLLNDGASVLTLSYLGGVKYVPHYNVMGV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 202 TKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACSYTS 281
Cdd:PRK08415  160 AKAALESSVRYLAVDLGKKGIRVNAISAGPIKTLAASGIGDFRMILKWNEINAPLKKNVSIEEVGNSGMYLLSDLSSGVT 239

                  ....*....
gi 1915223084 282 GQVWCSDGG 290
Cdd:PRK08415  240 GEIHYVDAG 248
PRK09186 PRK09186
flagellin modification protein A; Provisional
47-230 1.04e-16

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 77.72  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEE-KDAAEviALIKAEGRKAIALP-GDIRDETFCQNLVEEAVS 124
Cdd:PRK09186    2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEAlNELLE--SLGKEFKSKKLSLVeLDITDQESLEEFLSKSAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNA--GRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSSVQAV-KP------- 192
Cdd:PRK09186   80 KYGKIDGAVNCAypRNKDYGKKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGgnLVNISSIYGVvAPkfeiyeg 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1915223084 193 ----SPVllDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:PRK09186  160 tsmtSPV--EYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPG 199
PRK07806 PRK07806
SDR family oxidoreductase;
45-136 2.03e-16

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 76.68  E-value: 2.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK07806    2 GDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPR-ANKVVAEIEAAGGRASAVGADLTDEESVAALMDTARE 80
                          90
                  ....*....|..
gi 1915223084 125 KLGGLDILINNA 136
Cdd:PRK07806   81 EFGGLDALVLNA 92
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
45-290 2.07e-16

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 77.17  E-value: 2.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITG--GDSGIGRAVAIAYAREGADVAINYLPEEEKDAaevIALIKAEGRKAIALPGDIRDETFCQNLVEEA 122
Cdd:PRK06997    2 GFLAGKRILITGllSNRSIAYGIAKACKREGAELAFTYVGDRFKDR---ITEFAAEFGSDLVFPCDVASDEQIDALFASL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 123 VSKLGGLDILINNAGRQQyRES-----LEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLL 197
Cdd:PRK06997   79 GQHWDGLDGLVHSIGFAP-REAiagdfLDGLSRENFRIAHDISAYSFPALAKAALPMLSDDASLLTLSYLGAERVVPNYN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 198 DYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTvLQSSGGQPMEKVKEFGGDT-PLGRPGQPVEIAPLYVTLASDA 276
Cdd:PRK06997  158 TMGLAKASLEASVRYLAVSLGPKGIRANGISAGPIKT-LAASGIKDFGKILDFVESNaPLRRNVTIEEVGNVAAFLLSDL 236
                         250
                  ....*....|....
gi 1915223084 277 CSYTSGQVWCSDGG 290
Cdd:PRK06997  237 ASGVTGEITHVDSG 250
PRK05872 PRK05872
short chain dehydrogenase; Provisional
44-224 2.86e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 77.32  E-value: 2.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  44 HGRLTGKKALITGGDSGIGRAVAIAYAREGADVAinyLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAV 123
Cdd:PRK05872    4 MTSLAGKVVVVTGAARGIGAELARRLHARGAKLA---LVDLEEAELAALAAELGGDDRVLTVVADVTDLAAMQAAAEEAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS---VIIntSSVQAVKPSPVLLDYA 200
Cdd:PRK05872   81 ERFGGIDVVVANAGIASG-GSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRgyvLQV--SSLAAFAAAPGMAAYC 157
                         170       180
                  ....*....|....*....|....
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRV 224
Cdd:PRK05872  158 ASKAGVEAFANALRLEVAHHGVTV 181
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
49-230 2.99e-16

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 76.74  E-value: 2.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADV--AINYLPEEEKDAAEvialIKAEGRKA--------IALPGDIRDetFCQNL 118
Cdd:cd09807     1 GKTVIITGANTGIGKETARELARRGARVimACRDMAKCEEAAAE----IRRDTLNHevivrhldLASLKSIRA--FAAEF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 119 VEEAVSklggLDILINNAGRQQYRESleelTTED-FDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSV-------- 187
Cdd:cd09807    75 LAEEDR----LDVLINNAGVMRCPYS----KTEDgFEMQFGVNHLGHFLLTNLLLDLLKKSapSRIVNVSSLahkagkin 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1915223084 188 ----QAVKPSPVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:cd09807   147 fddlNSEKSYNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPG 193
PRK07775 PRK07775
SDR family oxidoreductase;
52-234 5.43e-16

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 75.95  E-value: 5.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLDI 131
Cdd:PRK07775   13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEK--CEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPSPVLLDYAQTKACLAVF 209
Cdd:PRK07775   91 LVSGAG-DTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMieRRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAM 169
                         170       180
                  ....*....|....*....|....*
gi 1915223084 210 TKSLAKQLGPKGIRVNAVAPGPYWT 234
Cdd:PRK07775  170 VTNLQMELEGTGVRASIVHPGPTLT 194
PRK08416 PRK08416
enoyl-ACP reductase;
49-290 5.53e-16

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 75.96  E-value: 5.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIA--LIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK08416    8 GKTLVISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVE--EANKIAedLEQKYGIKAKAYPLNILEPETYKELFKKIDEDF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNA---GRQ---QYRESLEeLTTEDFDATFKTNVYApFWI--TKAALRHLK-ASSVIINTSSVQAVKPSPVLL 197
Cdd:PRK08416   86 DRVDFFISNAiisGRAvvgGYTKFMR-LKPKGLNNIYTATVNA-FVVgaQEAAKRMEKvGGGSIISLSSTGNLVYIENYA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 198 DYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWT-VLQSSGGqpMEKVK-EFGGDTPLGRPGQPVEIAPLYVTLASD 275
Cdd:PRK08416  164 GHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTdALKAFTN--YEEVKaKTEELSPLNRMGQPEDLAGACLFLCSE 241
                         250
                  ....*....|....*
gi 1915223084 276 ACSYTSGQVWCSDGG 290
Cdd:PRK08416  242 KASWLTGQTIVVDGG 256
PRK09291 PRK09291
SDR family oxidoreductase;
48-234 6.41e-16

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 75.80  E-value: 6.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  48 TGKKALITGGDSGIGRAVAIAYAREGADV--------AINYLPEEEKDAA---EVIAL-IKAEGRKAIALPGDIrdetfc 115
Cdd:PRK09291    1 MSKTILITGAGSGFGREVALRLARKGHNViagvqiapQVTALRAEAARRGlalRVEKLdLTDAIDRAQAAEWDV------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 116 qnlveeavsklgglDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQAVKPS 193
Cdd:PRK09291   75 --------------DVLLNNAGIGE-AGAVVDIPVELVRELFETNVFGPLELTQGFVRKMvaRGKGKVVFTSSMAGLITG 139
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1915223084 194 PVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWT 234
Cdd:PRK09291  140 PFTGAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLT 180
PRK08703 PRK08703
SDR family oxidoreductase;
47-231 9.25e-16

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 74.97  E-value: 9.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAInyLPEEEKDAAEVI-ALIKAEGRKAIALPGDI---RDETFCQNLVEEA 122
Cdd:PRK08703    4 LSDKTILVTGASQGLGEQVAKAYAAAGATVIL--VARHQKKLEKVYdAIVEAGHPEPFAIRFDLmsaEEKEFEQFAATIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 123 VSKLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSPVLLDYA 200
Cdd:PRK08703   82 EATQGKLDGIVHCAGYFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSpdASVIFVGESHGETPKAYWGGFG 161
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKG-IRVNAVAPGP 231
Cdd:PRK08703  162 ASKAALNYLCKVAADEWERFGnLRANVLVPGP 193
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
50-230 1.20e-15

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 74.41  E-value: 1.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINYLPEEekDAAEVIALIKAEGRKAIALpgDIRD-ETFCQNLVEEAVSKLGG 128
Cdd:cd08931     1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDED--GLAALAAELGAENVVAGAL--DVTDrAAWAAALADFAAATGGR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 LDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSSVQAVKPSPVLLDYAQTKACL 206
Cdd:cd08931    77 LDALFNNAGVGRG-GPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATpgARVINTASSSAIYGQPDLAVYSATKFAV 155
                         170       180
                  ....*....|....*....|....
gi 1915223084 207 AVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:cd08931   156 RGLTEALDVEWARHGIRVADVWPW 179
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
43-290 4.82e-15

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 73.05  E-value: 4.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  43 GHGRLTGKKALITG--GDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIA-LIKAEgrkaIALPGDIRDETFCQNLV 119
Cdd:PRK07533    4 PLLPLAGKRGLVVGiaNEQSIAWGCARAFRALGAELAVTYLNDKARPYVEPLAeELDAP----IFLPLDVREPGQLEAVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 120 EEAVSKLGGLDILINN---AGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKpspVL 196
Cdd:PRK07533   80 ARIAEEWGRLDFLLHSiafAPKEDLHGRVVDCSREGFALAMDVSCHSFIRMARLAEPLMTNGGSLLTMSYYGAEK---VV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 197 LDY---AQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTvLQSSG----GQPMEKVKEfggDTPLGRPGQPVEIAPLY 269
Cdd:PRK07533  157 ENYnlmGPVKAALESSVRYLAAELGPKGIRVHAISPGPLKT-RAASGiddfDALLEDAAE---RAPLRRLVDIDDVGAVA 232
                         250       260
                  ....*....|....*....|.
gi 1915223084 270 VTLASDACSYTSGQVWCSDGG 290
Cdd:PRK07533  233 AFLASDAARRLTGNTLYIDGG 253
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
45-290 9.18e-15

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 72.31  E-value: 9.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITG--GDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIAlikAEGRKAIALPGDIRDETFCQNLVEEA 122
Cdd:PRK08690    2 GFLQGKKILITGmiSERSIAYGIAKACREQGAELAFTYVVDKLEERVRKMA---AELDSELVFRCDVASDDEINQVFADL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 123 VSKLGGLDILINNAGRQQyRESLE-----ELTTEDFDATFKTNVYAPFWITKAALRHLKA-SSVIINTSSVQAVKPSPVL 196
Cdd:PRK08690   79 GKHWDGLDGLVHSIGFAP-KEALSgdfldSISREAFNTAHEISAYSLPALAKAARPMMRGrNSAIVALSYLGAVRAIPNY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 197 LDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTvLQSSGGQPMEKVKEFGGD-TPLGRPGQPVEIAPLYVTLASD 275
Cdd:PRK08690  158 NVMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKT-LAASGIADFGKLLGHVAAhNPLRRNVTIEEVGNTAAFLLSD 236
                         250
                  ....*....|....*
gi 1915223084 276 ACSYTSGQVWCSDGG 290
Cdd:PRK08690  237 LSSGITGEITYVDGG 251
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
119-290 1.21e-14

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 71.57  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 119 VEEAVSKLGG-LDILINNAGRQQyresleeltTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQA-------- 189
Cdd:PRK12428   38 IDAAVAALPGrIDALFNIAGVPG---------TAPVELVARVNFLGLRHLTEALLPRMAPGGAIVNVASLAGaewpqrle 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 190 -----------------VKPSPVLLD--YAQTKACLAVFTKSLAKQ-LGPKGIRVNAVAPGPYWTV----LQSSGGQpmE 245
Cdd:PRK12428  109 lhkalaatasfdegaawLAAHPVALAtgYQLSKEALILWTMRQAQPwFGARGIRVNCVAPGPVFTPilgdFRSMLGQ--E 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1915223084 246 KVKEFGgdTPLGRPGQPVEIAPLYVTLASDACSYTSGQVWCSDGG 290
Cdd:PRK12428  187 RVDSDA--KRMGRPATADEQAAVLVFLCSDAARWINGVNLPVDGG 229
PRK07984 PRK07984
enoyl-ACP reductase FabI;
45-290 5.48e-14

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 70.32  E-value: 5.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYA--REGADVAINYLPEEEKDAAEVIAlikAEGRKAIALPGDIRDETFCQNLVEEA 122
Cdd:PRK07984    2 GFLSGKRILVTGVASKLSIAYGIAQAmhREGAELAFTYQNDKLKGRVEEFA---AQLGSDIVLPCDVAEDASIDAMFAEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 123 VSKLGGLDILINNAG----RQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLLD 198
Cdd:PRK07984   79 GKVWPKFDGFVHSIGfapgDQLDGDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 199 YAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTvLQSSGGQPMEK-VKEFGGDTPLGRPGQPVEIAPLYVTLASDAC 277
Cdd:PRK07984  159 MGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRT-LAASGIKDFRKmLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLS 237
                         250
                  ....*....|...
gi 1915223084 278 SYTSGQVWCSDGG 290
Cdd:PRK07984  238 AGISGEVVHVDGG 250
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
49-230 1.05e-13

human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like SDR domain of human WWOX and related proteins. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 69.93  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAINYlpEEEKDAAEVIALIKAEGRKAI--ALPGDIRDETFCQNLVEEAVSKL 126
Cdd:cd09809     1 GKVIIITGANSGIGFETARSFALHGAHVILAC--RNMSRASAAVSRILEEWHKARveAMTLDLASLRSVQRFAEAFKAKN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAG--RQQYResleeLTTEDFDATFKTNVYAPFWIT---KAALRHLKASSVIINTS---------------S 186
Cdd:cd09809    79 SPLHVLVCNAAvfALPWT-----LTEDGLETTFQVNHLGHFYLVqllEDVLRRSAPARVIVVSSeshrftdlpdscgnlD 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1915223084 187 VQAVKPSP----VLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:cd09809   154 FSLLSPPKkkywSMLAYNRAKLCNILFSNELHRRLSPRGITSNSLHPG 201
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
53-230 3.61e-13

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 67.65  E-value: 3.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  53 LITGGDSGIGRAVAIAYAREGADVAINYLPEEEKdaaevIALIKAEGrkAIALPGDIRDETFCQNLVEEAVSKLGGLDIL 132
Cdd:PRK06483    6 LITGAGQRIGLALAWHLLAQGQPVIVSYRTHYPA-----IDGLRQAG--AQCIQADFSTNAGIMAFIDELKQHTDGLRAI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 133 INNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV----IINTSSVQAVKPSPVLLDYAQTKACLAV 208
Cdd:PRK06483   79 IHNASDWL-AEKPGAPLADVLARMMQIHVNAPYLLNLALEDLLRGHGHaasdIIHITDYVVEKGSDKHIAYAASKAALDN 157
                         170       180
                  ....*....|....*....|..
gi 1915223084 209 FTKSLAKQLGPKgIRVNAVAPG 230
Cdd:PRK06483  158 MTLSFAAKLAPE-VKVNSIAPA 178
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
42-294 6.24e-13

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 67.47  E-value: 6.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  42 KGHGRLTGKKALITG--GDSGIGRAVAIAYAREGADVAINYLPEEEKDAAEVIAlikAEGRKAIALPGDIRDETFCQNLV 119
Cdd:PRK08159    3 QASGLMAGKRGLILGvaNNRSIAWGIAKACRAAGAELAFTYQGDALKKRVEPLA---AELGAFVAGHCDVTDEASIDAVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 120 EEAVSKLGGLDILINNAG---RQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVL 196
Cdd:PRK08159   80 ETLEKKWGKLDFVVHAIGfsdKDELTGRYVDTSRDNFTMTMDISVYSFTAVAQRAEKLMTDGGSILTLTYYGAEKVMPHY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 197 LDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDA 276
Cdd:PRK08159  160 NVMGVAKAALEASVKYLAVDLGPKNIRVNAISAGPIKTLAASGIGDFRYILKWNEYNAPLRRTVTIEEVGDSALYLLSDL 239
                         250
                  ....*....|....*...
gi 1915223084 277 CSYTSGQVWCSDGGDGVI 294
Cdd:PRK08159  240 SRGVTGEVHHVDSGYHVV 257
PRK07832 PRK07832
SDR family oxidoreductase;
50-230 1.32e-12

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 66.60  E-value: 1.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINylpeeEKDA---AEVIALIKAEGRK-AIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK07832    1 KRCFVTGAASGIGRATALRLAAQGAELFLT-----DRDAdglAQTVADARALGGTvPEHRALDISDYDAVAAFAADIHAA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV---IINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK07832   76 HGSMDVVMNIAGISAW-GTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAGRgghLVNVSSAAGLVALPWHAAYSAS 154
                         170       180
                  ....*....|....*....|....*...
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:PRK07832  155 KFGLRGLSEVLRFDLARHGIGVSVVVPG 182
PRK06482 PRK06482
SDR family oxidoreductase;
48-276 1.69e-12

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 66.29  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  48 TGKKALITGGDSGIGRAV-AIAYAREGADVAINYLPEEEKDaaeviaLIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:PRK06482    1 MSKTWFITGASSGFGRGMtERLLARGDRVAATVRRPDALDD------LKARYGDRLWVLQLDVTDSAAVRAVVDRAFAAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYRESlEELTTEDFDATFKTNVYAPFWITKAALRHLKASS----VIINTSSVQAVKPSPVLldYAQT 202
Cdd:PRK06482   75 GRIDVVVSNAGYGLFGAA-EELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGggriVQVSSEGGQIAYPGFSL--YHAT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSS--GGQPMEKVKefggDTPLGR------------PGQPVEI--- 265
Cdd:PRK06482  152 KWGIEGFVEAVAQEVAPFGIEFTIVEPGPARTNFGAGldRGAPLDAYD----DTPVGDlrraladgsfaiPGDPQKMvqa 227
                         250       260
                  ....*....|....*....|
gi 1915223084 266 ---------APLYVTLASDA 276
Cdd:PRK06482  228 miasadqtpAPRRLTLGSDA 247
PRK06139 PRK06139
SDR family oxidoreductase;
44-230 3.34e-12

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 65.90  E-value: 3.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  44 HGRLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAV 123
Cdd:PRK06139    2 MGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEA--LQAVAEECRALGAEVLVVPTDVTDADQVKALATQAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQ 201
Cdd:PRK06139   80 SFGGRIDVWVNNVGVGAV-GRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKqgHGIFINMISLGGFAAQPYAAAYSA 158
                         170       180       190
                  ....*....|....*....|....*....|
gi 1915223084 202 TKACLAVFTKSLAKQLGPK-GIRVNAVAPG 230
Cdd:PRK06139  159 SKFGLRGFSEALRGELADHpDIHVCDVYPA 188
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
50-237 3.82e-12

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 65.38  E-value: 3.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINYLpEEEKDAAEVIALIKAEGRKAIALpgDIRDETFCQNLVEEAVSKLG-- 127
Cdd:cd09805     1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCL-TKNGPGAKELRRVCSDRLRTLQL--DVTKPEQIKRAAQWVKEHVGek 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 128 GLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHL-KASSVIINTSSVQAVKPSPVLLDYAQTKACL 206
Cdd:cd09805    78 GLWGLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLrRAKGRVVNVSSMGGRVPFPAGGAYCASKAAV 157
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1915223084 207 AVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQ 237
Cdd:cd09805   158 EAFSDSLRRELQPWGVKVSIIEPGNFKTGIT 188
PRK06196 PRK06196
oxidoreductase; Provisional
47-285 7.68e-12

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 64.70  E-value: 7.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAInylPEEEKDAAEViALIKAEGRKAIALpgDIRDETFCQNLVEEAVSKL 126
Cdd:PRK06196   24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIV---PARRPDVARE-ALAGIDGVEVVML--DLADLESVRAFAERFLDSG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYRESleeLTTEDFDATFKTNVYAPFWIT---KAALRHLKASSVI-----------INTSSVQAVKP 192
Cdd:PRK06196   98 RRIDILINNAGVMACPET---RVGDGWEAQFATNHLGHFALVnllWPALAAGAGARVValssaghrrspIRWDDPHFTRG 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 193 SPVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSggQPMEKVKEFGGDTPLGRPgqpveIAPLYVTL 272
Cdd:PRK06196  175 YDKWLAYGQSKTANALFAVHLDKLGKDQGVRAFSVHPGGILTPLQRH--LPREEQVALGWVDEHGNP-----IDPGFKTP 247
                         250
                  ....*....|...
gi 1915223084 273 ASDAcsytSGQVW 285
Cdd:PRK06196  248 AQGA----ATQVW 256
PRK05876 PRK05876
short chain dehydrogenase; Provisional
49-229 1.39e-11

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 63.44  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAinyLPEEEKDAAE-VIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLG 127
Cdd:PRK05876    6 GRGAVITGGASGIGLATGTEFARRGARVV---LGDVDKPGLRqAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 128 GLDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV---IINTSSVQAVKPSPVLLDYAQTKA 204
Cdd:PRK05876   83 HVDVVFSNAG-IVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTgghVVFTASFAGLVPNAGLGAYGVAKY 161
                         170       180
                  ....*....|....*....|....*
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAP 229
Cdd:PRK05876  162 GVVGLAETLAREVTADGIGVSVLCP 186
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
52-243 1.78e-11

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 62.15  E-value: 1.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAREGADVAINylpeeEKDAAEVIALikAEGRKAIALPGDIRDETFCQNLVEEAvsklGGLDI 131
Cdd:cd11730     1 ALILGATGGIGRALARALAGRGWRLLLS-----GRDAGALAGL--AAEVGALARPADVAAELEVWALAQEL----GPLDL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGRQQYRESLEElTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLLDYAQTKACLAVFTK 211
Cdd:cd11730    70 LVYAAGAILGKPLART-KPAAWRRILDANLTGAALVLKHALALLAAGARLVFLGAYPELVMLPGLSAYAAAKAALEAYVE 148
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1915223084 212 SLAKQLgpKGIRVNAVAPGPYWTVLQSSGGQP 243
Cdd:cd11730   149 VARKEV--RGLRLTLVRPPAVDTGLWAPPGRL 178
PRK06194 PRK06194
hypothetical protein; Provisional
46-232 1.88e-11

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 63.11  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAinyLPEEEKDA-AEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVS 124
Cdd:PRK06194    3 DFAGKVAVITGAASGFGLAFARIGAALGMKLV---LADVQQDAlDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQyRESLEELTTEDFDATFKTNVY---------APFWITKAAlRHLKASSVIINTSSVQAVKPSPV 195
Cdd:PRK06194   80 RFGAVHLLFNNAGVGA-GGLVWENSLADWEWVLGVNLWgvihgvrafTPLMLAAAE-KDPAYEGHIVNTASMAGLLAPPA 157
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1915223084 196 LLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPY 232
Cdd:PRK06194  158 MGIYNVSKHAVVSLTETLYQDLSLVTDQVGASVLCPY 194
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
45-294 2.65e-11

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 62.72  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITG--GDSGIGRAVAIAYAREGADVAINYlpEEEKDAAEVIALIKAEGRKAIAlPGDIRDETFCQNLVEEA 122
Cdd:PRK06603    4 GLLQGKKGLITGiaNNMSISWAIAQLAKKHGAELWFTY--QSEVLEKRVKPLAEEIGCNFVS-ELDVTNPKSISNLFDDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 123 VSKLGGLDILINN---AGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAA--LRHLKASSVIINTSSVQAVKPSPVLL 197
Cdd:PRK06603   81 KEKWGSFDFLLHGmafADKNELKGRYVDTSLENFHNSLHISCYSLLELSRSAeaLMHDGGSIVTLTYYGAEKVIPNYNVM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 198 DYAqtKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDAC 277
Cdd:PRK06603  161 GVA--KAALEASVKYLANDMGENNIRVNAISAGPIKTLASSAIGDFSTMLKSHAATAPLKRNTTQEDVGGAAVYLFSELS 238
                         250
                  ....*....|....*..
gi 1915223084 278 SYTSGQVWCSDGGDGVI 294
Cdd:PRK06603  239 KGVTGEIHYVDCGYNIM 255
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
50-250 5.43e-11

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 61.62  E-value: 5.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADV-AINylpeeEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL-- 126
Cdd:PRK06924    2 RYVIITGTSQGLGEAIANQLLEKGTHViSIS-----RTENKELTKLAEQYNSNLTFHSLDLQDVHELETNFNEILSSIqe 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 -GGLDI-LINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV---IINTSSVQAVKPSPVLLDYAQ 201
Cdd:PRK06924   77 dNVSSIhLINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVdkrVINISSGAAKNPYFGWSAYCS 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1915223084 202 TKACLAVFTKSLAKQLGPK--GIRVNAVAPGPYWTVLQ----SSGGQPMEKVKEF 250
Cdd:PRK06924  157 SKAGLDMFTQTVATEQEEEeyPVKIVAFSPGVMDTNMQaqirSSSKEDFTNLDRF 211
PRK08251 PRK08251
SDR family oxidoreductase;
48-230 7.47e-11

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 61.10  E-value: 7.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  48 TGKKALITGGDSGIGRAVAIAYAREGADVAI--NYLPEEEKDAAEVIAliKAEGRKAIALPGDIRDETFCQNLVEEAVSK 125
Cdd:PRK08251    1 TRQKILITGASSGLGAGMAREFAAKGRDLALcaRRTDRLEELKAELLA--RYPGIKVAVAALDVNDHDQVFEVFAEFRDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNAGRQQYResleELTTEDFDA---TFKTNVYAPFWITKAALRHLKASS----VIIntSSVQAVKPSP-VLL 197
Cdd:PRK08251   79 LGGLDRVIVNAGIGKGA----RLGTGKFWAnkaTAETNFVAALAQCEAAMEIFREQGsghlVLI--SSVSAVRGLPgVKA 152
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1915223084 198 DYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:PRK08251  153 AYAASKAGVASLGEGLRAELAKTPIKVSTIEPG 185
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
49-230 4.97e-10

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 58.76  E-value: 4.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAI---NYLPEEEKDAaeviALIKAEGRKAIALP-GDIRDETFCQNLVEEAVS 124
Cdd:cd09808     1 GRSFLITGANSGIGKAAALAIAKRGGTVHMvcrNQTRAEEARK----EIETESGNQNIFLHiVDMSDPKQVWEFVEEFKE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 125 KLGGLDILINNAGRQQYReslEELTTEDFDATFKTNVYAPFWITKAALRHLKAS--SVIINTSS----VQAVKPSPVLLD 198
Cdd:cd09808    77 EGKKLHVLINNAGCMVNK---RELTEDGLEKNFATNTLGTYILTTHLIPVLEKEedPRVITVSSggmlVQKLNTNNLQSE 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1915223084 199 ---------YAQTKACLAVFTKSLAKqlGPKGIRVNAVAPG 230
Cdd:cd09808   154 rtafdgtmvYAQNKRQQVIMTEQWAK--KHPEIHFSVMHPG 192
PRK08017 PRK08017
SDR family oxidoreductase;
50-245 5.72e-10

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 58.56  E-value: 5.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADV-AINYLPEEekdaaevIALIKAEGRKAIALpgDIRDETFCQNLVEEAVSKLGG 128
Cdd:PRK08017    3 KSVLITGCSSGIGLEAALELKRRGYRVlAACRKPDD-------VARMNSLGFTGILL--DLDDPESVERAADEVIALTDN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 129 -LDILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSSVQAVKPSPVLLDYAQTKAC 205
Cdd:PRK08017   74 rLYGLFNNAGFGVY-GPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEgrIVMTSSVMGLISTPGRGAYAASKYA 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1915223084 206 LAVFTKSLAKQLGPKGIRVNAVAPGPYWT-----VLQSSGGQPME 245
Cdd:PRK08017  153 LEAWSDALRMELRHSGIKVSLIEPGPIRTrftdnVNQTQSDKPVE 197
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
49-283 6.15e-10

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 58.63  E-value: 6.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEekDAAEVIALIKAE-GRKAIALPGDIRDETFCQNLVEEAVSKLG 127
Cdd:cd05322     2 NQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSE--NAEKVADEINAEyGEKAYGFGADATNEQSVIALSKGVDEIFK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 128 GLDILINNAGRQQyRESLEELTTEDFDATFKTNVYAPFW----ITKAALRHLKASSVI-INTSS--VQAVKPSpvllDYA 200
Cdd:cd05322    80 RVDLLVYSAGIAK-SAKITDFELGDFDRSLQVNLVGYFLcareFSKLMIRDGIQGRIIqINSKSgkVGSKHNS----GYS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 201 QTKACLAVFTKSLAKQLGPKGIRVNAVAPG-------------PYWTVLqssgGQPMEKVKEFGGD-TPLGRPGQPVEIA 266
Cdd:cd05322   155 AAKFGGVGLTQSLALDLAEHGITVNSLMLGnllkspmfqsllpQYAKKL----GIKESEVEQYYIDkVPLKRGCDYQDVL 230
                         250
                  ....*....|....*..
gi 1915223084 267 PLYVTLASDACSYTSGQ 283
Cdd:cd05322   231 NMLLFYASPKASYCTGQ 247
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
50-253 6.65e-10

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 58.24  E-value: 6.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADV--AINYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDEtfcqNLVEEAVSKLG 127
Cdd:cd09806     1 TVVLITGCSSGIGLHLAVRLASDPSKRfkVYATMRDLKKKGRLWEAAGALAGGTLETLQLDVCDS----KSVAAAVERVT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 128 G--LDILINNAGrQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLK--ASSVIINTSSVQAVKPSPVLLDYAQTK 203
Cdd:cd09806    77 ErhVDVLVCNAG-VGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKrrGSGRILVTSSVGGLQGLPFNDVYCASK 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1915223084 204 ACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGD 253
Cdd:cd09806   156 FALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEEVLDRTAD 205
PRK07024 PRK07024
SDR family oxidoreductase;
51-230 7.13e-10

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 58.40  E-value: 7.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  51 KALITGGDSGIGRAVAIAYAREGADVAinyLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLD 130
Cdd:PRK07024    4 KVFITGASSGIGQALAREYARQGATLG---LVARRTDALQAFAARLPKAARVSVYAADVRDADALAAAAADFIAAHGLPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 131 ILINNAG--RQQYRESLEELTTedFDATFKTNVYA------PFwitkAALRHLKASSVIINTSSVQAVKPSPVLLDYAQT 202
Cdd:PRK07024   81 VVIANAGisVGTLTEEREDLAV--FREVMDTNYFGmvatfqPF----IAPMRAARRGTLVGIASVAGVRGLPGAGAYSAS 154
                         170       180
                  ....*....|....*....|....*...
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:PRK07024  155 KAAAIKYLESLRVELRPAGVRVVTIAPG 182
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
47-230 9.70e-10

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 57.84  E-value: 9.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADVAINYlPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEE-AVSK 125
Cdd:cd09763     1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITG-RTILPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERvAREQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLDILINNA--GRQQYRESLE----ELTTEDFDATFKTNVYAPFWITKAALRHLKASS--VIINTSSVQAVKpSPVLL 197
Cdd:cd09763    80 QGRLDILVNNAyaAVQLILVGVAkpfwEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGkgLIVIISSTGGLE-YLFNV 158
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1915223084 198 DYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:cd09763   159 AYGVGKAAIDRMAADMAHELKPHGVAVVSLWPG 191
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
53-200 2.24e-09

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 55.57  E-value: 2.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084   53 LITGGDSGIGRAVAIAYAREGADvainYL------PEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKL 126
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGAR----RLvllsrsGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVE 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915223084  127 GGLDILINNAGRQQYReSLEELTTEDFDATFKTNVYApFWITKAALRHLKASSVIInTSSVQAVKPSPVLLDYA 200
Cdd:smart00822  80 GPLTGVIHAAGVLDDG-VLASLTPERFAAVLAPKAAG-AWNLHELTADLPLDFFVL-FSSIAGVLGSPGQANYA 150
PRK05993 PRK05993
SDR family oxidoreductase;
53-231 7.63e-09

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 55.42  E-value: 7.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  53 LITGGDSGIGRAVAIAYAREGADVAINYLPEEEkdaaevIALIKAEGRKAIALpgDIRDETFCQNLVEEAVSKLGG-LDI 131
Cdd:PRK05993    8 LITGCSSGIGAYCARALQSDGWRVFATCRKEED------VAALEAEGLEAFQL--DYAEPESIAALVAQVLELSGGrLDA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGRQQyRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPVLLDYAQTKACLAVF 209
Cdd:PRK05993   80 LFNNGAYGQ-PGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKqgQGRIVQCSSILGLVPMKYRGAYNASKFAIEGL 158
                         170       180
                  ....*....|....*....|..
gi 1915223084 210 TKSLAKQLGPKGIRVNAVAPGP 231
Cdd:PRK05993  159 SLTLRMELQGSGIHVSLIEPGP 180
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
53-230 1.54e-08

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 54.38  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  53 LITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAaevialIKAE-GRKAIALPGDIRDETFCQNLVEEAVSKLGGLDI 131
Cdd:PRK10538    4 LVTGATAGFGECITRRFIQQGHKVIATGRRQERLQE------LKDElGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSSVQAVKPSPVLLDYAQTKACLAVF 209
Cdd:PRK10538   78 LVNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHghIINIGSTAGSWPYAGGNVYGATKAFVRQF 157
                         170       180
                  ....*....|....*....|.
gi 1915223084 210 TKSLAKQLGPKGIRVNAVAPG 230
Cdd:PRK10538  158 SLNLRTDLHGTAVRVTDIEPG 178
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
44-235 2.47e-08

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 53.98  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  44 HGRLTGKKALITG--GDSGIGRAVAIAYAREGADVAINYlpEEEKDAAEVIALIKAEGRKAIaLPGDIRDETFCQNLVEE 121
Cdd:PRK06505    2 EGLMQGKRGLIMGvaNDHSIAWGIAKQLAAQGAELAFTY--QGEALGKRVKPLAESLGSDFV-LPCDVEDIASVDAVFEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 122 AVSKLGGLDILINNAG---RQQYRESLEELTTEDFDATFKTNVYAPFWITK--AALRHLKASSVIINTSSVQAVKPSPVL 196
Cdd:PRK06505   79 LEKKWGKLDFVVHAIGfsdKNELKGRYADTTRENFSRTMVISCFSFTEIAKraAKLMPDGGSMLTLTYGGSTRVMPNYNV 158
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1915223084 197 LDYAqtKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTV 235
Cdd:PRK06505  159 MGVA--KAALEASVRYLAADYGPQGIRVNAISAGPVRTL 195
PRK06197 PRK06197
short chain dehydrogenase; Provisional
48-234 3.73e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 53.49  E-value: 3.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  48 TGKKALITGGDSGIGRAVAIAYAREGADVAI---NylPEEEKDAAEVIALIKAEGRKAI-ALpgDIRDETFCQNLVEEAV 123
Cdd:PRK06197   15 SGRVAVVTGANTGLGYETAAALAAKGAHVVLavrN--LDKGKAAAARITAATPGADVTLqEL--DLTSLASVRAAADALR 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAG-----RQqyresleelTTED-FDATFKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAVKPSPV 195
Cdd:PRK06197   91 AAYPRIDLLINNAGvmytpKQ---------TTADgFELQFGTNHLGHFALTGLLLDRLLPvpGSRVVTVSSGGHRIRAAI 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1915223084 196 LLD-------------YAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWT 234
Cdd:PRK06197  162 HFDdlqwerrynrvaaYGQSKLANLLFTYELQRRLAAAGATTIAVAAHPGVS 213
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
51-205 4.13e-08

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 53.44  E-value: 4.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  51 KALITGGDSGIGRAVAIAYAREGADV-AINYLPEeekDAAEVIALIKAEgrkaiALPGDIRDETFCQNLVEEAvsklggl 129
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGHEVvGLDRSPP---GAANLAALPGVE-----FVRGDLRDPEALAAALAGV------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAGRQQYREsleelttEDFDATFKTNVYApfwiTKAALRHLKASSV--IINTSSVQAVKPSPVLLD--------- 198
Cdd:COG0451    66 DAVVHLAAPAGVGE-------EDPDETLEVNVEG----TLNLLEAARAAGVkrFVYASSSSVYGDGEGPIDedtplrpvs 134

                  ....*...
gi 1915223084 199 -YAQTKAC 205
Cdd:COG0451   135 pYGASKLA 142
PLN02780 PLN02780
ketoreductase/ oxidoreductase
49-229 4.52e-08

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 53.33  E-value: 4.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGAD-VAINYLPEEEKDAAEVI------ALIKAegrKAIALPGDIrDETFCQnlVEE 121
Cdd:PLN02780   53 GSWALVTGPTDGIGKGFAFQLARKGLNlVLVARNPDKLKDVSDSIqskyskTQIKT---VVVDFSGDI-DEGVKR--IKE 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 122 AVSklgGLD--ILINNAG-RQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHL--KASSVIINTSSVQA-VKPS-P 194
Cdd:PLN02780  127 TIE---GLDvgVLINNVGvSYPYARFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMlkRKKGAIINIGSGAAiVIPSdP 203
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1915223084 195 VLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAP 229
Cdd:PLN02780  204 LYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVP 238
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
53-200 8.28e-08

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 53.14  E-value: 8.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  53 LITGGDSGIGRAVAIAYAR-EGADVAI---NYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGG 128
Cdd:cd08953   209 LVTGGAGGIGRALARALARrYGARLVLlgrSPLPPEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRERYGA 288
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915223084 129 LDILINNAGRQQYReSLEELTTEDFDATFKTNVyapfwitkAALRHLKASSV------IINTSSVQAVKPSPVLLDYA 200
Cdd:cd08953   289 IDGVIHAAGVLRDA-LLAQKTAEDFEAVLAPKV--------DGLLNLAQALAdepldfFVLFSSVSAFFGGAGQADYA 357
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
47-290 3.27e-07

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 50.50  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITG--GDSGIGRAVAIAYAREGADVAINYlpEEEKDAAEVIALI-KAEGRKAIALPGDIRDE---TFCQNLVE 120
Cdd:PRK08594    5 LEGKTYVVMGvaNKRSIAWGIARSLHNAGAKLVFTY--AGERLEKEVRELAdTLEGQESLLLPCDVTSDeeiTACFETIK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 121 EAVSKLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSV--QAVKPSPVLLD 198
Cdd:PRK08594   83 EEVGVIHGVAHCIAFANKEDLRGEFLETSRDGFLLAQNISAYSLTAVAREAKKLMTEGGSIVTLTYLggERVVQNYNVMG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 199 YAqtKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSSGGQPMEKVKEFGGDTPLGRPGQPVEIAPLYVTLASDACS 278
Cdd:PRK08594  163 VA--KASLEASVKYLANDLGKDGIRVNAISAGPIRTLSAKGVGGFNSILKEIEERAPLRRTTTQEEVGDTAAFLFSDLSR 240
                         250
                  ....*....|..
gi 1915223084 279 YTSGQVWCSDGG 290
Cdd:PRK08594  241 GVTGENIHVDSG 252
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
50-241 4.85e-07

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 49.80  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINylPEEEKDAAEVIALIKAegrKAIALPGDIRDETFCQNLVEEaVSKLGGL 129
Cdd:cd08951     8 KRIFITGSSDGLGLAAARTLLHQGHEVVLH--ARSQKRAADAKAACPG---AAGVLIGDLSSLAETRKLADQ-VNAIGRF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAGrqQYRESLEELTTEDFDATFKTNVYAPFWITkAALRHLKasSVIINTSSVQavKPSPVLLD----------- 198
Cdd:cd08951    82 DAVIHNAG--ILSGPNRKTPDTGIPAMVAVNVLAPYVLT-ALIRRPK--RLIYLSSGMH--RGGNASLDdidwfnrgend 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1915223084 199 ---YAQTKACLAVFTKSLAKQlgPKGIRVNAVAPGpyWTVLQSSGG 241
Cdd:cd08951   155 spaYSDSKLHVLTLAAAVARR--WKDVSSNAVHPG--WVPTKMGGA 196
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
53-245 1.09e-06

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 49.30  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  53 LITGGDSGIGRAVAIAYAREGA-DVAINYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEaVSKLGGLDI 131
Cdd:cd05274   154 LITGGLGGLGLLVARWLAARGArHLVLLSRRGPAPRAAARAALLRAGGARVSVVRCDVTDPAALAALLAE-LAAGGPLAG 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LINNAGRqqYRE-SLEELTTEDFDATFKTNVYAPfWITKAALRHLKASSVIInTSSVQAVKPSPVLLDYAQTKACLAVft 210
Cdd:cd05274   233 VIHAAGV--LRDaLLAELTPAAFAAVLAAKVAGA-LNLHELTPDLPLDFFVL-FSSVAALLGGAGQAAYAAANAFLDA-- 306
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1915223084 211 ksLAKQLGPKGIRVNAVAPGPyWTV------------LQSSGGQPME 245
Cdd:cd05274   307 --LAAQRRRRGLPATSVQWGA-WAGggmaaaaalrarLARSGLGPLA 350
PRK07023 PRK07023
SDR family oxidoreductase;
51-230 1.37e-06

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 48.47  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  51 KALITGGDSGIGRAVAIAYAREGADV---AINYLPEEEKDAAEVIALIKAE----GRKAIALPGDIrdetfCQNLVEEAV 123
Cdd:PRK07023    3 RAIVTGHSRGLGAALAEQLLQPGIAVlgvARSRHPSLAAAAGERLAEVELDlsdaAAAAAWLAGDL-----LAAFVDGAS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLggldiLINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSV--IINTSSVQAVKPSPVLLDYAQ 201
Cdd:PRK07023   78 RVL-----LINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAErrILHISSGAARNAYAGWSVYCA 152
                         170       180
                  ....*....|....*....|....*....
gi 1915223084 202 TKACLAVFTKSLAKQlGPKGIRVNAVAPG 230
Cdd:PRK07023  153 TKAALDHHARAVALD-ANRALRIVSLAPG 180
PRK06720 PRK06720
hypothetical protein; Provisional
46-144 1.90e-06

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 47.27  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  46 RLTGKKALITGGDSGIGRAVAIAYAREGADVAINYLPEEEKDAA--EVIALikaeGRKAIALPGDIRDETFCQNLVEEAV 123
Cdd:PRK06720   13 KLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATveEITNL----GGEALFVSYDMEKQGDWQRVISITL 88
                          90       100       110
                  ....*....|....*....|....*....|
gi 1915223084 124 SKLGGLDILINNAG---------RQQYRES 144
Cdd:PRK06720   89 NAFSRIDMLFQNAGlykidsifsRQQENDS 118
PRK05854 PRK05854
SDR family oxidoreductase;
47-240 2.75e-06

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 48.14  E-value: 2.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  47 LTGKKALITGGDSGIGRAVAIAYAREGADV------------AINYLPEEEKDAAEVIALIKAEGRKAIALPGDirdetf 114
Cdd:PRK05854   12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVilpvrnrakgeaAVAAIRTAVPDAKLSLRALDLSSLASVAALGE------ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 115 cqNLVEEAVSklggLDILINNAG------RQQyresleelTTEDFDATFKTNVYAPFWITKAALRHLKA--------SSV 180
Cdd:PRK05854   86 --QLRAEGRP----IHLLINNAGvmtppeRQT--------TADGFELQFGTNHLGHFALTAHLLPLLRAgrarvtsqSSI 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1915223084 181 I-----INTSSVQAVKPSPVLLDYAQTKACLAVFTKSLAK--QLGPKGIRVNAVAPGPYWTVLQSSG 240
Cdd:PRK05854  152 AarrgaINWDDLNWERSYAGMRAYSQSKIAVGLFALELDRrsRAAGWGITSNLAHPGVAPTNLLAAR 218
PRK07578 PRK07578
short chain dehydrogenase; Provisional
50-239 5.40e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 46.34  E-value: 5.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAiayaregadvainylpEEEKDAAEVIALikaeGRKAIALPGDIRDETFCQNLVEeavsKLGGL 129
Cdd:PRK07578    1 MKILVIGASGTIGRAVV----------------AELSKRHEVITA----GRSSGDVQVDITDPASIRALFE----KVGKV 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAGRQQYrESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTSSVQAVKPSPVLLDYAQTKACLAVF 209
Cdd:PRK07578   57 DAVVSAAGKVHF-APLAEMTDEDFNVGLQSKLMGQVNLVLIGQHYLNDGGSFTLTSGILSDEPIPGGASAATVNGALEGF 135
                         170       180       190
                  ....*....|....*....|....*....|
gi 1915223084 210 TKSLAKQLgPKGIRVNAVAPgpywTVLQSS 239
Cdd:PRK07578  136 VKAAALEL-PRGIRINVVSP----TVLTES 160
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
203-290 7.20e-06

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 46.47  E-value: 7.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 203 KACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQSS--GGQPMEKVkeFGGDTPLG-RPGQPVEIAPLYVTLASDACSY 279
Cdd:PRK07889  162 KAALESTNRYLARDLGPRGIRVNLVAAGPIRTLAAKAipGFELLEEG--WDERAPLGwDVKDPTPVARAVVALLSDWFPA 239
                          90
                  ....*....|.
gi 1915223084 280 TSGQVWCSDGG 290
Cdd:PRK07889  240 TTGEIVHVDGG 250
PRK08303 PRK08303
short chain dehydrogenase; Provisional
45-135 8.28e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 46.53  E-value: 8.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITGGDSGIGRAVAIAYAREGADVainYL--------------PEEEKDAAEviaLIKAEGRKAIALPGDIR 110
Cdd:PRK08303    4 KPLRGKVALVAGATRGAGRGIAVELGAAGATV---YVtgrstrarrseydrPETIEETAE---LVTAAGGRGIAVQVDHL 77
                          90       100
                  ....*....|....*....|....*
gi 1915223084 111 DETFCQNLVEEAVSKLGGLDILINN 135
Cdd:PRK08303   78 VPEQVRALVERIDREQGRLDILVND 102
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
52-238 1.21e-05

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 45.67  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  52 ALITGGDSGIGRAVAIAYAR----EGADVAInyLPEEEKDAAEVIALIKAE--GRKAIALPGDIRDETFCQNLVEeAVSK 125
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKclksPGSVLVL--SARNDEALRQLKAEIGAErsGLRVVRVSLDLGAEAGLEQLLK-ALRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 126 LGGLD-----ILINNAGrQQYRESLEELTTEDFDATFK---TNVYAPFWITKAALRHLKASS----VIINTSSVQAVKPS 193
Cdd:TIGR01500  80 LPRPKglqrlLLINNAG-TLGDVSKGFVDLSDSTQVQNywaLNLTSMLCLTSSVLKAFKDSPglnrTVVNISSLCAIQPF 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1915223084 194 PVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTVLQS 238
Cdd:TIGR01500 159 KGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQ 203
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
53-164 1.70e-05

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 44.48  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  53 LITGGDSGIGRAVAIAYAREGAD--VAINYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSKLGGLD 130
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARhlVLLSRSAAPRPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIR 83
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1915223084 131 ILINNAGRQQYReSLEELTTEDFDAtfktnVYAP 164
Cdd:pfam08659  84 GVIHAAGVLRDA-LLENMTDEDWRR-----VLAP 111
PRK06953 PRK06953
SDR family oxidoreductase;
50-164 5.49e-05

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 43.52  E-value: 5.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVAINylpeeEKDAAEVIALiKAEGRKAIALpgDIRDEtfcqnlveEAVS----K 125
Cdd:PRK06953    2 KTVLIVGASRGIGREFVRQYRADGWRVIAT-----ARDAAALAAL-QALGAEALAL--DVADP--------ASVAglawK 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1915223084 126 LGG--LDILINNAGRQQYR-ESLEELTTEDFDATFKTNVYAP 164
Cdd:PRK06953   66 LDGeaLDAAVYVAGVYGPRtEGVEPITREDFDAVMHTNVLGP 107
PRK07102 PRK07102
SDR family oxidoreductase;
49-230 5.87e-05

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 43.37  E-value: 5.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIGRAVAIAYAREGADVainYLPEEEKDAAEVIAL-IKAEGRKAIALPG-DIRDETFCQNLVEEAVSKL 126
Cdd:PRK07102    1 MKKILIIGATSDIARACARRYAAAGARL---YLAARDVERLERLADdLRARGAVAVSTHElDILDTASHAAFLDSLPALP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYRESleeltteDFDAT---FKTNVYAPFWITKAALRHLKA--SSVIINTSSVQAV--KPSPVLldY 199
Cdd:PRK07102   78 DIVLIAVGTLGDQAACEA-------DPALAlreFRTNFEGPIALLTLLANRFEArgSGTIVGISSVAGDrgRASNYV--Y 148
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1915223084 200 AQTKACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:PRK07102  149 GSAKAALTAFLSGLRNRLFKSGVHVLTVKPG 179
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
50-230 6.46e-05

light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (Pchlide) reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 43.66  E-value: 6.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGA---DVAINYLPEEEKDAAEVIAlikAEGRKAIaLPGDIRDETFCQNLVEEAVSKL 126
Cdd:cd09810     2 GTVVITGASSGLGLAAAKALARRGEwhvVMACRDFLKAEQAAQEVGM---PKDSYSV-LHCDLASLDSVRQFVDNFRRTG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 127 GGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASS-----VII------NTSSVQA-VKPSP 194
Cdd:cd09810    78 RPLDALVCNAAVYLPTAKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLQRSEnasprIVIvgsithNPNTLAGnVPPRA 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915223084 195 VLLD-------------------------YAQTKACLAVFTKSLAKQLGPK-GIRVNAVAPG 230
Cdd:cd09810   158 TLGDleglagglkgfnsmidggefegakaYKDSKVCNMLTTYELHRRLHEEtGITFNSLYPG 219
PRK08177 PRK08177
SDR family oxidoreductase;
50-230 2.06e-04

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 41.55  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAIAYAREGADVainylpeeekdAAEVIALIKAEGRKaiALPG------DIRDetfcQNLVEEAV 123
Cdd:PRK08177    2 RTALIIGASRGLGLGLVDRLLERGWQV-----------TATVRGPQQDTALQ--ALPGvhieklDMND----PASLDQLL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 124 SKLGG--LDILINNAG----RQQyreSLEELTTEDFDATFKTNVYAPFWITKAALRHLKA-SSVIINTSSVQA---VKPS 193
Cdd:PRK08177   65 QRLQGqrFDLLFVNAGisgpAHQ---SAADATAAEIGQLFLTNAIAPIRLARRLLGQVRPgQGVLAFMSSQLGsveLPDG 141
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1915223084 194 PVLLDYAQTKACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:PRK08177  142 GEMPLYKASKAALNSMTRSFVAELGEPTLTVLSMHPG 178
PRK05884 PRK05884
SDR family oxidoreductase;
53-283 4.86e-04

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 40.56  E-value: 4.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  53 LITGGDSGIGRAVAIAYAREGADVAINylpEEEKDAAEVIAliKAEGRKAIALpgDIRDETFcqnlVEEAVSKL-GGLDI 131
Cdd:PRK05884    4 LVTGGDTDLGRTIAEGFRNDGHKVTLV---GARRDDLEVAA--KELDVDAIVC--DNTDPAS----LEEARGLFpHHLDT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 132 LIN-------NAGRQQYreSLEElTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINtssVQAVKPSPVLLDYAqTKA 204
Cdd:PRK05884   73 IVNvpapswdAGDPRTY--SLAD-TANAWRNALDATVLSAVLTVQSVGDHLRSGGSIIS---VVPENPPAGSAEAA-IKA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 205 CLAVFTKSLAKQLGPKGIRVNAVAPGpywtvlqsSGGQPmekvkefgGDTPLGRPGQPV--EIAPLYVTLASDACSYTSG 282
Cdd:PRK05884  146 ALSNWTAGQAAVFGTRGITINAVACG--------RSVQP--------GYDGLSRTPPPVaaEIARLALFLTTPAARHITG 209

                  .
gi 1915223084 283 Q 283
Cdd:PRK05884  210 Q 210
PRK06940 PRK06940
short chain dehydrogenase; Provisional
50-290 1.14e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 39.62  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  50 KKALITGGDSGIGRAVAiayAREGADVAINYLPEEEKDAAEVIALIKAEGRKAIALPGDIRDETFCQNLVEEAVSkLGGL 129
Cdd:PRK06940    2 KEVVVVIGAGGIGQAIA---RRVGAGKKVLLADYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAATAQT-LGPV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 130 DILINNAGRQQYRESLEelttedfdATFKTNVYAPFWITKAALRHLKASSVIINTSSVQ---------------AVKPSP 194
Cdd:PRK06940   78 TGLVHTAGVSPSQASPE--------AILKVDLYGTALVLEEFGKVIAPGGAGVVIASQSghrlpaltaeqeralATTPTE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 195 VLLD---------------YAQTKACLAVFTKSLAKQLGPKGIRVNAVAPGPYWTvlqssggqPMeKVKEFGGDT----- 254
Cdd:PRK06940  150 ELLSlpflqpdaiedslhaYQIAKRANALRVMAEAVKWGERGARINSISPGIIST--------PL-AQDELNGPRgdgyr 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1915223084 255 ------PLGRPGQPVEIAPLYVTLASDACSYTSGQVWCSDGG 290
Cdd:PRK06940  221 nmfaksPAGRPGTPDEIAALAEFLMGPRGSFITGSDFLVDGG 262
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
45-230 1.61e-03

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 39.32  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  45 GRLTGKKALITG--GDSGIGRAVAIAYAREGADVAINYLPEEEKD-----AAEVIALIKAEgrkaIALPGDIrDETFCQn 117
Cdd:PRK06079    3 GILSGKKIVVMGvaNKRSIAWGCAQAIKDQGATVIYTYQNDRMKKslqklVDEEDLLVECD----VASDESI-ERAFAT- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084 118 lVEEAVSKLGGLDILINNAGRQQYRESLEELTTEDFDATFKTNVYAPFWITKAALRHLKASSVIINTS---SVQAVkPSP 194
Cdd:PRK06079   77 -IKERVGKIDGIVHAIAYAKKEELGGNVTDTSRDGYALAQDISAYSLIAVAKYARPLLNPGASIVTLTyfgSERAI-PNY 154
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1915223084 195 VLLDYAqtKACLAVFTKSLAKQLGPKGIRVNAVAPG 230
Cdd:PRK06079  155 NVMGIA--KAALESSVRYLARDLGKKGIRVNAISAG 188
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
49-148 5.45e-03

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 37.71  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915223084  49 GKKALITGGDSGIG-RAVAIAYARegadvainylpeeekdAAEVIALIKAEGRKAIAlpGDIRDETFCQNLVEEAVSKLG 127
Cdd:PRK13771  163 GETVLVTGAGGGVGiHAIQVAKAL----------------GAKVIAVTSSESKAKIV--SKYADYVIVGSKFSEEVKKIG 224
                          90       100
                  ....*....|....*....|.
gi 1915223084 128 GLDILINNAGRQQYRESLEEL 148
Cdd:PRK13771  225 GADIVIETVGTPTLEESLRSL 245
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH