NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|31980844|ref|NP_081095|]
View 

dehydrogenase/reductase SDR family member 1 [Mus musculus]

Protein Classification

dehydrogenase/reductase SDR family member 1( domain architecture ID 10176799)

dehydrogenase/reductase SDR family member 1 (DHRS1) is an uncharacterized enzyme from the short-chain dehydrogenases/reductases (SDR) family of NAD(P)(H)-dependent oxidoreductase

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 5-271 1.36e-163

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: 455.75  E-value: 1.36e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQK 83
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTiLPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  84 GRLDVLVNNAYAGVQAILNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNVPY 163
Cdd:cd09763  81 GRLDILVNNAYAAVQLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVAY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMakeDTPEDPLFKKMKPDFSSAESPEMSGKCVVALATDP 243
Cdd:cd09763 161 GVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMP---EDDEGSWHAKERDAFLNGETTEYSGRCVVALAADP 237

                       250       260
                ....*....|....*....|....*...
gi 31980844 244 NILNLSGKVLPSCDLARRYGLKDIDGRP 271
Cdd:cd09763 238 DLMELSGRVLITGELAREYGFTDVDGRQ 265
 
Name Accession Description Interval E-value
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 5-271 1.36e-163

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: 455.75  E-value: 1.36e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQK 83
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTiLPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  84 GRLDVLVNNAYAGVQAILNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNVPY 163
Cdd:cd09763  81 GRLDILVNNAYAAVQLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVAY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMakeDTPEDPLFKKMKPDFSSAESPEMSGKCVVALATDP 243
Cdd:cd09763 161 GVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMP---EDDEGSWHAKERDAFLNGETTEYSGRCVVALAADP 237

                       250       260
                ....*....|....*....|....*...
gi 31980844 244 NILNLSGKVLPSCDLARRYGLKDIDGRP 271
Cdd:cd09763 238 DLMELSGRVLITGELAREYGFTDVDGRQ 265
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 3-242 2.13e-59

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: 190.38  E-value: 2.13e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQ 82
Cdd:COG1028   2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAA-VAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  83 KGRLDVLVNNayAGVQAilnttNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN-V 161
Cdd:COG1028  81 FGRLDILVNN--AGITP-----PGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGqA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 162 PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDplFKKMKPdFSSAESPEMSGKCVVALAT 241
Cdd:COG1028 154 AYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREA--LAARIP-LGRLGTPEEVAAAVLFLAS 230


                .
gi 31980844 242 D 242
Cdd:COG1028 231 D 231
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 1-271 6.60e-58

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 188.28  E-value: 6.60e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHL----------DTLRATAQEAQSLGGRCVPVVCDSSQESE 70
Cdd:PRK08303   2 MMKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTrarrseydrpETIEETAELVTAAGGRGIAVQVDHLVPEQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   71 VKSLFEQVDREQkGRLDVLVNNAYAGvqAILNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVS 150
Cdd:PRK08303  82 VRALVERIDREQ-GRLDILVNDIWGG--EKLFEWGKPVWEHSLDKGLRMLRLAIDTHLITSHFALPLLIRRPGGLVVEIT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  151 SpGGLQH-----MFNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKE-FMAKEDTPEDPLFKkmKPDFS 224
Cdd:PRK08303 159 D-GTAEYnathyRLSVFYDLAKTSVNRLAFSLAHELAPHGATAVALTPGWLRSEMMLDaFGVTEENWRDALAK--EPHFA 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 31980844  225 SAESPEMSGKCVVALATDPNILNLSGKVLPSCDLARRYGLKDIDG-RP 271
Cdd:PRK08303 236 ISETPRYVGRAVAALAADPDVARWNGQSLSSGQLARVYGFTDLDGsRP 283
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 8-209 1.09e-46

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 155.85  E-value: 1.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844     8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRLD 87
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQA-VERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    88 VLVNNayAGVQAilnttNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNVP-YGVG 166
Cdd:pfam00106  80 ILVNN--AGITG-----LGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSaYSAS 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 31980844   167 KAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKED 209
Cdd:pfam00106 153 KAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 7-203 1.56e-13

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. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 69.27  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844     7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGR-----HLDTLRATAQE----AQSLGGRCVPVVCDSSQESEVKSLFEQ 77
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVDLcaddpAVGYPLATRAEldavAAACPDQVLPVIADVRDPAALAAAVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    78 VdREQKGRLDVLVnnAYAGVQAilntTNKSFWEVPASIWDDINNVGLRGhylcsVYG-ARLMVPA-------GKGLIVIV 149
Cdd:TIGR04504  81 A-VERWGRLDAAV--AAAGVIA----GGRPLWETTDAELDLLLDVNLRG-----VWNlARAAVPAmlarpdpRGGRFVAV 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 31980844   150 SSPGGLQHMFNVP-YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKE 203
Cdd:TIGR04504 149 ASAAATRGLPHLAaYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLAA 203
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 9-111 2.03e-04

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: 41.31  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844      9 VCVVTGASRGIGRGIALQLCKAGA-TVYITGRH---LDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGArRLVLLSRSgpdAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAI-PAVEG 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 31980844     85 RLDVLVNNayAGV---QAILNTTNKSFWEV 111
Cdd:smart00822  81 PLTGVIHA--AGVlddGVLASLTPERFAAV 108
 
Name Accession Description Interval E-value
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 5-271 1.36e-163

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: 455.75  E-value: 1.36e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQK 83
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTiLPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  84 GRLDVLVNNAYAGVQAILNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNVPY 163
Cdd:cd09763  81 GRLDILVNNAYAAVQLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVAY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMakeDTPEDPLFKKMKPDFSSAESPEMSGKCVVALATDP 243
Cdd:cd09763 161 GVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMP---EDDEGSWHAKERDAFLNGETTEYSGRCVVALAADP 237

                       250       260
                ....*....|....*....|....*...
gi 31980844 244 NILNLSGKVLPSCDLARRYGLKDIDGRP 271
Cdd:cd09763 238 DLMELSGRVLITGELAREYGFTDVDGRQ 265
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 5-271 1.87e-94

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: 279.66  E-value: 1.87e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHL--------DTLRAT----AQEAQSLGGRCVPVVCDSSQESEVK 72
Cdd:cd05338   1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTAsegdngsaKSLPGTieetAEEIEAAGGQALPIVVDVRDEDQVR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  73 SLFEQVDREQkGRLDVLVNNAYAGVQAilnttnkSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSP 152
Cdd:cd05338  81 ALVEATVDQF-GRLDILVNNAGAIWLS-------LVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPP 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 153 GGLQHMF-NVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTemvkefmakedtpedplfkkmkpdfsSAESPEM 231
Cdd:cd05338 153 LSLRPARgDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIE--------------------------TPAATEL 206

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 31980844 232 SGKCVVALATDPNILNLSGKVLPSCDLARRYGLKDIDGRP 271
Cdd:cd05338 207 SGGSDPARARSPEILSDAVLAILSRPAAERTGLVVIDEEL 246
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 3-242 2.13e-59

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: 190.38  E-value: 2.13e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQ 82
Cdd:COG1028   2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAA-VAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  83 KGRLDVLVNNayAGVQAilnttNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN-V 161
Cdd:COG1028  81 FGRLDILVNN--AGITP-----PGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGqA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 162 PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDplFKKMKPdFSSAESPEMSGKCVVALAT 241
Cdd:COG1028 154 AYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREA--LAARIP-LGRLGTPEEVAAAVLFLAS 230


                .
gi 31980844 242 D 242
Cdd:COG1028 231 D 231
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 1-271 6.60e-58

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 188.28  E-value: 6.60e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHL----------DTLRATAQEAQSLGGRCVPVVCDSSQESE 70
Cdd:PRK08303   2 MMKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTrarrseydrpETIEETAELVTAAGGRGIAVQVDHLVPEQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   71 VKSLFEQVDREQkGRLDVLVNNAYAGvqAILNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVS 150
Cdd:PRK08303  82 VRALVERIDREQ-GRLDILVNDIWGG--EKLFEWGKPVWEHSLDKGLRMLRLAIDTHLITSHFALPLLIRRPGGLVVEIT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  151 SpGGLQH-----MFNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKE-FMAKEDTPEDPLFKkmKPDFS 224
Cdd:PRK08303 159 D-GTAEYnathyRLSVFYDLAKTSVNRLAFSLAHELAPHGATAVALTPGWLRSEMMLDaFGVTEENWRDALAK--EPHFA 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 31980844  225 SAESPEMSGKCVVALATDPNILNLSGKVLPSCDLARRYGLKDIDG-RP 271
Cdd:PRK08303 236 ISETPRYVGRAVAALAADPDVARWNGQSLSSGQLARVYGFTDLDGsRP 283
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 4-243 3.34e-50

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: 166.51  E-value: 3.34e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqsLGGRCVPVVCDSSQESEVKSLFEQVdREQK 83
Cdd:COG4221   2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAE---LGGRALAVPLDVTDEAAVEAAVAAA-VAEF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  84 GRLDVLVNNayAGVQAIlnttnKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHM-FNVP 162
Cdd:COG4221  78 GRLDVLVNN--AGVALL-----GPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYpGGAV 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 163 YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDPLFKKMKPdfssaESPEMSGKCVVALATD 242
Cdd:COG4221 151 YAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEP-----LTPEDVAEAVLFALTQ 225


                .
gi 31980844 243 P 243
Cdd:COG4221 226 P 226
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 10-238 3.39e-48

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: 161.30  E-value: 3.39e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  10 CVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAqEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRLDVL 89
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELA-AIEALGGNAVAVQADVSDEEDVEALVEEA-LEEFGRLDIL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  90 VNNayAGVQailntTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN-VPYGVGKA 168
Cdd:cd05233  79 VNN--AGIA-----RPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGqAAYAASKA 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 169 ACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPED----PLFKKMKPD--------FSSAESPEMSGKCV 236
Cdd:cd05233 152 ALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELaaaiPLGRLGTPEevaeavvfLASDEASYITGQVI 231


                ..
gi 31980844 237 VA 238
Cdd:cd05233 232 PV 233
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
5-213 8.97e-48

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 160.42  E-value: 8.97e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:COG0300   3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAV-LARFG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHM-FNVPY 163
Cdd:COG0300  82 PIDVLVNN--AGV-----GGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLpGMAAY 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 31980844 164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKED----TPED 213
Cdd:COG0300 155 AASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGrpllSPEE 208
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 8-209 1.09e-46

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 155.85  E-value: 1.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844     8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRLD 87
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQA-VERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    88 VLVNNayAGVQAilnttNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNVP-YGVG 166
Cdd:pfam00106  80 ILVNN--AGITG-----LGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSaYSAS 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 31980844   167 KAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKED 209
Cdd:pfam00106 153 KAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
5-222 1.92e-40

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 141.45  E-value: 1.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDrEQKG 84
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAV-EAFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN-VPY 163
Cdd:PRK05653  82 ALDILVNN--AGI-----TRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGqTNY 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31980844  164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVK---EFMAKEDTPEDPLFKKMKPD 222
Cdd:PRK05653 155 SAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDMTEglpEEVKAEILKEIPLGRLGQPE 216
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-212 1.25e-36

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 131.50  E-value: 1.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITG-RHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQkG 84
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYdINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKF-G 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAyagvqAILNTtnKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN-VPY 163
Cdd:PRK05565  83 KIDILVNNA-----GISNF--GLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCeVLY 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 31980844  164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKeFMAKEDTPE 212
Cdd:PRK05565 156 SASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWS-SFSEEDKEG 203
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 5-202 1.77e-35

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 128.39  E-value: 1.77e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTL-RATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQK 83
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGaEALVAEIGALGGKALAVQGDVSDAESVERAVDEA-KAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   84 GRLDVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN-VP 162
Cdd:PRK05557  82 GGVDILVNN--AGI-----TRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGqAN 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 31980844  163 YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVK 202
Cdd:PRK05557 155 YAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDMTD 194
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
4-213 5.09e-35

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 127.53  E-value: 5.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDrEQ 82
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQID-EE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   83 KGRLDVLVNNAYAGVqailnttNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNVP 162
Cdd:PRK08063  80 FGRLDVFVNNAASGV-------LRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYT 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 31980844  163 Y-GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPED 213
Cdd:PRK08063 153 TvGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPNREELLED 204
FabG-like PRK07231
SDR family oxidoreductase;
7-213 1.60e-34

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 126.10  E-value: 1.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSlGGRCVPVVCDSSQESEVKSLFEQVdREQKGRL 86
Cdd:PRK07231   5 GKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILA-GGRAIAVAADVSDEADVEAAVAAA-LERFGSV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   87 DVLVNNayAGVqailNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN-VPYGV 165
Cdd:PRK07231  83 DILVNN--AGT----THRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGlGWYNA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 31980844  166 GKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMaKEDTPED 213
Cdd:PRK07231 157 SKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFM-GEPTPEN 203
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 12-254 2.14e-34

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: 125.54  E-value: 2.14e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  12 VTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRLDVLV 90
Cdd:cd05359   3 VTGGSRGIGKAIALRLAERGADVVINYRKsKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAV-KERFGRLDVLV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  91 NNAYAGVQailnttnKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN-VPYGVGKAA 169
Cdd:cd05359  82 SNAAAGAF-------RPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNyLAVGTAKAA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 170 CDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPED-----PLFKKMKPDfssaespEMSGkcVVALATDPN 244
Cdd:cd05359 155 LEALVRYLAVELGPRGIRVNAVSPGVIDTDALAHFPNREDLLEAaaantPAGRVGTPQ-------DVAD--AVGFLCSDA 225

                       250
                ....*....|
gi 31980844 245 ILNLSGKVLP 254
Cdd:cd05359 226 ARMITGQTLV 235
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 5-242 5.51e-34

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: 124.75  E-value: 5.51e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQE-AQSLGGRCVPVVCDSSQESEVKSLFEQVDREQk 83
Cdd:cd05352   6 LKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEElAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDF- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  84 GRLDVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGlqHMFNVP- 162
Cdd:cd05352  85 GKIDILIAN--AGI-----TVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSG--TIVNRPq 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 163 ----YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVkefmakedtpeDPLFKKMKPDFSS-------AESPEM 231
Cdd:cd05352 156 pqaaYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLT-----------DFVDKELRKKWESyiplkriALPEEL 224

                       250
                ....*....|.
gi 31980844 232 SGKCVVaLATD 242
Cdd:cd05352 225 VGAYLY-LASD 234
PRK07035 PRK07035
SDR family oxidoreductase;
5-242 9.67e-34

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 123.97  E-value: 9.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHI-RERHG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAYAGVQ--AILNTtnksfwevPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSS-----PGGLQH 157
Cdd:PRK07035  85 RLDILVNNAAANPYfgHILDT--------DLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASvngvsPGDFQG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  158 MfnvpYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDPLfkKMKPDFSSAESPEMSGkCVV 237
Cdd:PRK07035 157 I----YSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKNDAILKQAL--AHIPLRRHAEPSEMAG-AVL 229


                 ....*
gi 31980844  238 ALATD 242
Cdd:PRK07035 230 YLASD 234
PRK05867 PRK05867
SDR family oxidoreductase;
5-237 1.50e-33

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 123.61  E-value: 1.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQKG 84
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 rLDVLVNNA-YAGVQAILnttnksfwEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGK-GLIVIVSSPGGlqHMFNVP 162
Cdd:PRK05867  87 -IDIAVCNAgIITVTPML--------DMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQgGVIINTASMSG--HIINVP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  163 YGVG-----KAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVK---EFMAKEDtPEDPLFKKMKPD--------FSSA 226
Cdd:PRK05867 156 QQVShycasKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEpytEYQPLWE-PKIPLGRLGRPEelaglylyLASE 234

                        250
                 ....*....|.
gi 31980844  227 ESPEMSGKCVV 237
Cdd:PRK05867 235 ASSYMTGSDIV 245
PRK12826 PRK12826
SDR family oxidoreductase;
3-203 1.98e-33

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 123.10  E-value: 1.98e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDrEQ 82
Cdd:PRK12826   2 RDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGV-ED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   83 KGRLDVLVNNA-YAGVQAilnttnksFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMF-- 159
Cdd:PRK12826  81 FGRLDILVANAgIFPLTP--------FAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRVGYpg 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 31980844  160 NVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKE 203
Cdd:PRK12826 153 LAHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGN 196
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 5-242 2.32e-33

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: 123.26  E-value: 2.32e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGR-HLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDrEQK 83
Cdd:cd05358   1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRsKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAI-KEF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  84 GRLDVLVNNayAGVQAilnttNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMV-PAGKGLIVIVSS-------PGgl 155
Cdd:cd05358  80 GTLDILVNN--AGLQG-----DASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRkSKIKGKIINMSSvhekipwPG-- 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 156 qhmfNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDPLfkKMKPdFSSAESPEMSGKC 235
Cdd:cd05358 151 ----HVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQRADLL--SLIP-MGRIGEPEEIAAA 223


                ....*..
gi 31980844 236 VVALATD 242
Cdd:cd05358 224 AAWLASD 230
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 5-219 6.39e-33

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: 121.70  E-value: 6.39e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQkG 84
Cdd:cd05347   3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDF-G 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNayAGVQAIlnttnKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNVP-Y 163
Cdd:cd05347  82 KIDILVNN--AGIIRR-----HPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPaY 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 31980844 164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDPLFKKM 219
Cdd:cd05347 155 AASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVVADPEFNDDILKRIP 210
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 5-220 2.30e-32

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: 120.59  E-value: 2.30e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVP---VVCDSSQESEVKSLFEQVdRE 81
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSEKKillVVADLTEEEGQDRIISTT-LA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  82 QKGRLDVLVNNAYAGVQAILNTTNKSFwevpasiWDDINNVGLRGHYLCSvygaRLMVP---AGKGLIVIVSS-PGGLQH 157
Cdd:cd05364  80 KFGRLDILVNNAGILAKGGGEDQDIEE-------YDKVMNLNLRAVIYLT----KLAVPhliKTKGEIVNVSSvAGGRSF 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980844 158 MFNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEfMAKEDTPEDPLFKKMK 220
Cdd:cd05364 149 PGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRR-MGMPEEQYIKFLSRAK 210
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 17-202 3.21e-31

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: 116.76  E-value: 3.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    17 RGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPvvCDSSQESEVKSLFEQVdREQKGRLDVLVNNAyag 96
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEELGAAVLP--CDVTDEEQVEALVAAA-VEKFGRLDILVNNA--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    97 vqAILNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKglIVIVSSPGGLQHMFNV-PYGVGKAACDRLAA 175
Cdd:pfam13561  80 --GFAPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGGS--IVNLSSIGAERVVPNYnAYGAAKAALEALTR 155

                         170       180
                  ....*....|....*....|....*....
gi 31980844   176 DCAHELRRHG--VSYVSlwPGLVQTEMVK 202
Cdd:pfam13561 156 YLAVELGPRGirVNAIS--PGPIKTLAAS 182
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 8-203 4.71e-31

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: 116.49  E-value: 4.71e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQkGRLD 87
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEF-GPVD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  88 VLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN-VPYGVG 166
Cdd:cd05333  80 ILVNN--AGI-----TRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGqANYAAS 152

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 31980844 167 KAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKE 203
Cdd:cd05333 153 KAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDA 189
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-222 6.15e-31

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 116.51  E-value: 6.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGR-HLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQvDREQ 82
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAA-AVER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   83 KGRLDVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHYlcsvYGARLMVP----AGKGLIVIVSSPGGLQ-H 157
Cdd:PRK12825  82 FGRIDILVNN--AGI-----FEDKPLADMSDDEWDEVIDVNLSGVF----HLLRAVVPpmrkQRGGRIVNISSVAGLPgW 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31980844  158 MFNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMV-KEFMAKEDTPED--PLFKKMKPD 222
Cdd:PRK12825 151 PGRSNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKeATIEEAREAKDAetPLGRSGTPE 218
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 1-200 1.54e-30

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 115.45  E-value: 1.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdR 80
Cdd:PRK12939   1 MASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAA-A 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   81 EQKGRLDVLVNNAyagvqAIlnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN 160
Cdd:PRK12939  80 AALGGLDGLVNNA-----GI--TNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPK 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 31980844  161 VP-YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:PRK12939 153 LGaYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEA 193
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 5-242 2.14e-29

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: 112.58  E-value: 2.14e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDtlrATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQKG 84
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGG---AAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 rLDVLVNNAyagvqAILNTTNkSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQhmfNVP-- 162
Cdd:cd08944  78 -LDLLVNNA-----GAMHLTP-AIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQS---GDPgy 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 163 --YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDPLFKKMKPDFSSAE--SPEMSGKCVVA 238
Cdd:cd08944 148 gaYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEGALGPGGFHLLIHQLQGRlgRPEDVAAAVVF 227


                ....
gi 31980844 239 LATD 242
Cdd:cd08944 228 LLSD 231
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 11-244 3.30e-29

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: 111.94  E-value: 3.30e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  11 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRAtAQEAQSLGGRCVPVvcDSSQESEVKSLFEQVdREQKGRLDVLV 90
Cdd:cd05374   4 LITGCSSGIGLALALALAAQGYRVIATARNPDKLES-LGELLNDNLEVLEL--DVTDEESIKAAVKEV-IERFGRIDVLV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  91 NNA---YAGvqailnttnkSFWEVPAsiwDDINNVglrghYLCSVYG--------ARLMVPAGKGLIVIVSSPGGLQHM- 158
Cdd:cd05374  80 NNAgygLFG----------PLEETSI---EEVREL-----FEVNVFGplrvtrafLPLMRKQGSGRIVNVSSVAGLVPTp 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 159 FNVPYGVGKAACDRLaADC-AHELRRHGVSYVSLWPGLVQTEMVKEFMAK-----EDTPEDPLFKKMKPDFSSAE----S 228
Cdd:cd05374 142 FLGPYCASKAALEAL-SESlRLELAPFGIKVTIIEPGPVRTGFADNAAGSaledpEISPYAPERKEIKENAAGVGsnpgD 220

                       250
                ....*....|....*.
gi 31980844 229 PEMSGKCVVALATDPN 244
Cdd:cd05374 221 PEKVADVIVKALTSES 236
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 5-243 8.43e-29

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 111.13  E-value: 8.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDReQKG 84
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVE-TFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNayAGVQAILNTTnksfwEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQ-HMFNVPY 163
Cdd:PRK12429  81 GVDILVNN--AGIQHVAPIE-----DFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVgSAGKAAY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMV----KEFMAKEDTPEDPLFKK-MKPDFSSAE--SPEMSGKCV 236
Cdd:PRK12429 154 VSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTPLVrkqiPDLAKERGISEEEVLEDvLLPLVPQKRftTVEEIADYA 233


                 ....*..
gi 31980844  237 VALATDP 243
Cdd:PRK12429 234 LFLASFA 240
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-222 1.09e-28

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 110.16  E-value: 1.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdR 80
Cdd:PRK07666   1 MAQSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQL-K 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   81 EQKGRLDVLVNNayAGVQAIlnttnKSFWEVPASIWDDINNVGLRGHYlcsvYGARLMVPA----GKGLIVIVSSPGGLQ 156
Cdd:PRK07666  80 NELGSIDILINN--AGISKF-----GKFLELDPAEWEKIIQVNLMGVY----YATRAVLPSmierQSGDIINISSTAGQK 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980844  157 HMFNV-PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEdplfKKMKPD 222
Cdd:PRK07666 149 GAAVTsAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGLTDGNPD----KVMQPE 211
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 5-211 1.29e-28

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 110.81  E-value: 1.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:PRK08213  10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEET-LERFG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAYA--GVQAIlnttnksfwEVPASIWDDINNVGLRGHYLCS-VYGARLMVPAGKGLIVIVSSPGGLQ----- 156
Cdd:PRK08213  89 HVDILVNNAGAtwGAPAE---------DHPVEAWDKVMNLNVRGLFLLSqAVAKRSMIPRGYGRIINVASVAGLGgnppe 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31980844  157 HMFNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM-------VKEFMAkEDTP 211
Cdd:PRK08213 160 VMDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMtrgtlerLGEDLL-AHTP 220
PRK06172 PRK06172
SDR family oxidoreductase;
1-209 1.87e-28

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 110.23  E-value: 1.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdR 80
Cdd:PRK06172   1 MSMTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQT-I 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   81 EQKGRLDVLVNNAYAGVQailnttNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN 160
Cdd:PRK06172  80 AAYGRLDYAFNNAGIEIE------QGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPK 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 31980844  161 VP-YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKED 209
Cdd:PRK06172 154 MSiYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYEADP 203
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 6-221 8.43e-28

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: 108.13  E-value: 8.43e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   6 KGQVCVVTGASRGIGRGIALQLCKAGATV---YITGRhlDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDrEQ 82
Cdd:cd05362   2 AGKVALVTGASRGIGRAIAKRLARDGASVvvnYASSK--AAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAE-KA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  83 KGRLDVLVNNayAGV---QAILNTTNKSFwevpasiwDDINNVGLRGHYLCSVYGARLMVPAGKgLIVIVSSPGGLQHMF 159
Cdd:cd05362  79 FGGVDILVNN--AGVmlkKPIAETSEEEF--------DRMFTVNTKGAFFVLQEAAKRLRDGGR-IINISSSLTAAYTPN 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980844 160 NVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMvkeFMAKEdTPEDP-LFKKMKP 221
Cdd:cd05362 148 YGAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDM---FYAGK-TEEAVeGYAKMSP 206
PRK06181 PRK06181
SDR family oxidoreductase;
7-202 1.98e-27

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 107.76  E-value: 1.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRL 86
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAA-VARFGGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   87 DVLVNNayAGVqailnTTNKSFWEVPA-SIWDDINNVglrgHYLCSVYGARLMVP---AGKGLIVIVSSPGGLQhmfNVP 162
Cdd:PRK06181  80 DILVNN--AGI-----TMWSRFDELTDlSVFERVMRV----NYLGAVYCTHAALPhlkASRGQIVVVSSLAGLT---GVP 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 31980844  163 YGVGKAA--------CDRLAAdcahELRRHGVSYVSLWPGLVQTEMVK 202
Cdd:PRK06181 146 TRSGYAAskhalhgfFDSLRI----ELADDGVAVTVVCPGFVATDIRK 189
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 5-199 9.05e-27

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: 105.36  E-value: 9.05e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSL-GGRCVPVVCDSSQESEVKSLFEQVDREQk 83
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSAtGGRAHPIQCDVRDPEAVEAAVDETLKEF- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  84 GRLDVLVNNAyAGvQAILNTTNKSF--WEvpASIwdDINNVGlrGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHM-FN 160
Cdd:cd05369  80 GKIDILINNA-AG-NFLAPAESLSPngFK--TVI--DIDLNG--TFNTTKAVGKRLIEAKHGGSILNISATYAYTGSpFQ 151

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 31980844 161 VPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTE 199
Cdd:cd05369 152 VHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTT 190
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 7-242 1.00e-26

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: 105.54  E-value: 1.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLD-TLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGR 85
Cdd:cd05366   2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEeAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQA-VEKFGS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  86 LDVLVNNayAGVQAIlnttnKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAG-KGLIVIVSSPGGLQHMFNVP-Y 163
Cdd:cd05366  81 FDVMVNN--AGIAPI-----TPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAGVQGFPNLGaY 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM---VKEFMAKED-TPEDPLFKkmkpDFSS------AESPEMSG 233
Cdd:cd05366 154 SASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMwdyIDEEVGEIAgKPEGEGFA----EFSSsiplgrLSEPEDVA 229


                ....*....
gi 31980844 234 KCVVALATD 242
Cdd:cd05366 230 GLVSFLASE 238
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 5-242 1.63e-26

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: 104.77  E-value: 1.63e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqsLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:cd05341   3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAE---LGDAARFFHLDVTDEDGWTAVVDTA-REAFG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNAyagvqAILntTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNVP-Y 163
Cdd:cd05341  79 RLDVLVNNA-----GIL--TGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAaY 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 164 GVGKAACDRLAADCAHELRRH--GVSYVSLWPGLVQTEMVKEFMAKEDTPEDPlfkKMKPDFSSAESPEMSGkCVVALAT 241
Cdd:cd05341 152 NASKGAVRGLTKSAALECATQgyGIRVNSVHPGYIYTPMTDELLIAQGEMGNY---PNTPMGRAGEPDEIAY-AVVYLAS 227


                .
gi 31980844 242 D 242
Cdd:cd05341 228 D 228
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 1-242 8.72e-26

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 103.21  E-value: 8.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQslGGRCVPVVCDSSQESEVKSLFEQVdR 80
Cdd:PRK12829   5 LLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLP--GAKVTATVADVADPAQVERVFDTA-V 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   81 EQKGRLDVLVNNA-YAGVQAILNttnksfwEVPASIWDDINNVGLRGHYlcsvYGARLMVPAGK-----GLIVIVSSPGG 154
Cdd:PRK12829  82 ERFGGLDVLVNNAgIAGPTGGID-------EITPEQWEQTLAVNLNGQF----YFARAAVPLLKasghgGVIIALSSVAG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  155 LQHM-FNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDPLFKKM------KPDFSSAE 227
Cdd:PRK12829 151 RLGYpGRTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARAQQLGIGLDEMeqeyleKISLGRMV 230

                        250
                 ....*....|....*
gi 31980844  228 SPEMSGKCVVALATD 242
Cdd:PRK12829 231 EPEDIAATALFLASP 245
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-202 1.75e-25

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 101.96  E-value: 1.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:PRK08217   3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQI-AEDFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAyagvqAILN------------TTNKSFWEvpasiWDDINNVGLRGHYLCSVYGARLMVPAG-KGLIVIVSS 151
Cdd:PRK08217  82 QLNGLINNA-----GILRdgllvkakdgkvTSKMSLEQ-----FQSVIDVNLTGVFLCGREAAAKMIESGsKGVIINISS 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 31980844  152 PGGLQHMFNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVK 202
Cdd:PRK08217 152 IARAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTA 202
PRK06138 PRK06138
SDR family oxidoreductase;
5-212 2.13e-25

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 101.77  E-value: 2.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSlGGRCVPVVCDSSQESEVKSLFEQVDREqKG 84
Cdd:PRK06138   3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAA-GGRAFARQGDVGSAEAVEALVDFVAAR-WG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAYAGVQAILNTTNksfwevPASiWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHM-FNVPY 163
Cdd:PRK06138  81 RLDVLVNNAGFGCGGTVVTTD------EAD-WDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGrGRAAY 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 31980844  164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPE 212
Cdd:PRK06138 154 VASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFARHADPE 202
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 7-207 2.38e-25

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: 101.58  E-value: 2.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRL 86
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKA-GDAFGRV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  87 DVLVNNAYAGVQAilnttnkSFWEVPASIWDDinnvGLRGHYLCSVYGARLMVPA----GKGLIVIVSSPGGLQHMFN-V 161
Cdd:cd05344  80 DILVNNAGGPPPG-------PFAELTDEDWLE----AFDLKLLSVIRIVRAVLPGmkerGWGRIVNISSLTVKEPEPNlV 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 31980844 162 PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAK 207
Cdd:cd05344 149 LSNVARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTERVRRLLEA 194
PRK12743 PRK12743
SDR family oxidoreductase;
8-214 4.76e-25

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 100.88  E-value: 4.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRL 86
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIGITWHSdEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKL-IQRLGRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   87 DVLVNNAYAGvqailntTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKG--LIVIVS------SPGGlqhm 158
Cdd:PRK12743  82 DVLVNNAGAM-------TKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQGgrIINITSvhehtpLPGA---- 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 31980844  159 fnVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKefMAKEDTPEDP 214
Cdd:PRK12743 151 --SAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMNG--MDDSDVKPDS 202
PRK07774 PRK07774
SDR family oxidoreductase;
6-213 9.06e-25

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 100.20  E-value: 9.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGR 85
Cdd:PRK07774   5 DDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADAT-VSAFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   86 LDVLVNNA--YAGVQAILNTTnksfweVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLqhMFNVPY 163
Cdd:PRK07774  84 IDYLVNNAaiYGGMKLDLLIT------VPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAW--LYSNFY 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31980844  164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTE---------MVKEFMA-----KEDTPED 213
Cdd:PRK07774 156 GLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEatrtvtpkeFVADMVKgiplsRMGTPED 219
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 7-213 1.12e-24

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: 99.77  E-value: 1.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQsLGGRCVPVVCDSSQESEVKSLFEQVDREQKGrL 86
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQ-GGPRALGVQCDVTSEAQVQSAFEQAVLEFGG-L 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  87 DVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKG--LIVIVS------SPGglqhm 158
Cdd:cd08943  79 DIVVSN--AGI-----ATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGgnIVFNASknavapGPN----- 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980844 159 fNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWP-----GLVQTEMVKEF---MAKEDTPED 213
Cdd:cd08943 147 -AAAYSAAKAAEAHLARCLALEGGEDGIRVNTVNPdavfrGSKIWEGVWRAaraKAYGLLEEE 208
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 9-200 1.55e-24

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: 99.46  E-value: 1.55e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   9 VCVVTGASRGIGRGIALQLCKAGATVYIT-GRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRLD 87
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAARGFDIAINdLPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQA-WEDFGRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  88 VLVNNayAGVQA-----ILNTTNKSFwevpasiwDDINNVGLRGHYLCSVYGARLMVPAGK------GLIVIVSS-PGGL 155
Cdd:cd05337  82 CLVNN--AGIAVrprgdLLDLTEDSF--------DRLIAINLRGPFFLTQAVARRMVEQPDrfdgphRSIIFVTSiNAYL 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 31980844 156 QHMFNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:cd05337 152 VSPNRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDM 196
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 5-208 1.61e-24

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: 99.48  E-value: 1.61e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLgGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:cd08942   4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAY-GECIAIPADLSSEEGIEALVARV-AERSD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNAYAGVQAilnttnkSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGK----GLIVIVSSPGGLQHMF- 159
Cdd:cd08942  82 RLDVLVNNAGATWGA-------PLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaenpARVINIGSIAGIVVSGl 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 31980844 160 -NVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVkEFMAKE 208
Cdd:cd08942 155 eNYSYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMT-AFLLND 203
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 7-230 1.86e-24

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: 98.86  E-value: 1.86e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQE----AQSLGGRCVPVVCDSSQESEVKSLFEQVDrEQ 82
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEieaeANASGQKVSYISADLSDYEEVEQAFAQAV-EK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  83 KGRLDVLVNNAYAGVQailnttnKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN-V 161
Cdd:cd08939  80 GGPPDLVVNCAGISIP-------GLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGyS 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31980844 162 PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEfmakEDTPEDPLFKKMKpDFSSAESPE 230
Cdd:cd08939 153 AYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFEE----ENKTKPEETKAIE-GSSGPITPE 216
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 5-200 2.51e-24

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: 98.76  E-value: 2.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERT-VEALG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNAYAGVQAILNTTNKSFWEVPAsiwdDINNVGLrghylcsVYGAR----LMVPAGKGLIVIVSSPGGLQHMFN 160
Cdd:cd08934  80 RLDILVNNAGIMLLGPVEDADTTDWTRMI----DTNLLGL-------MYTTHaalpHHLLRNKGTIVNISSVAGRVAVRN 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 31980844 161 -VPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:cd08934 149 sAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTEL 189
PRK07814 PRK07814
SDR family oxidoreductase;
7-253 2.77e-24

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 99.08  E-value: 2.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRL 86
Cdd:PRK07814  10 DQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQA-VEAFGRL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   87 DVLVNN-AYAGVQAILNTTNKSFWEVPASiwddinNVGlRGHYLcSVYGARLMV-PAGKGLIV-IVSSPGGLQHMFNVPY 163
Cdd:PRK07814  89 DIVVNNvGGTMPNPLLSTSTKDLADAFTF------NVA-TAHAL-TVAAVPLMLeHSGGGSVInISSTMGRLAGRGFAAY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  164 GVGKAACD---RLAA-DCAHELRRHGVSyvslwPGLVQTEMVkEFMAKEDTPEDPLFKKMKpdFSSAESPEMSGKCVVAL 239
Cdd:PRK07814 161 GTAKAALAhytRLAAlDLCPRIRVNAIA-----PGSILTSAL-EVVAANDELRAPMEKATP--LRRLGDPEDIAAAAVYL 232

                        250
                 ....*....|....
gi 31980844  240 ATdPNILNLSGKVL 253
Cdd:PRK07814 233 AS-PAGSYLTGKTL 245
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 1-243 3.52e-24

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 98.81  E-value: 3.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdR 80
Cdd:PRK13394   1 MMSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKV-A 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   81 EQKGRLDVLVNNayAGVQAILNTTNKSFwevpaSIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVI--------VSSP 152
Cdd:PRK13394  80 ERFGSVDILVSN--AGIQIVNPIENYSF-----ADWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIymgsvhshEASP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  153 GglqhmfNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFM---AKED--TPEDPLFKKMKPDFSSAE 227
Cdd:PRK13394 153 L------KSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIpeqAKELgiSEEEVVKKVMLGKTVDGV 226

                        250
                 ....*....|....*...
gi 31980844  228 --SPEMSGKCVVALATDP 243
Cdd:PRK13394 227 ftTVEDVAQTVLFLSSFP 244
PRK08589 PRK08589
SDR family oxidoreductase;
5-242 4.04e-24

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 99.08  E-value: 4.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVyITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYV-LAVDIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEI-KEQFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAyaGVqailNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNVPYG 164
Cdd:PRK08589  82 RVDVLFNNA--GV----DNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAADLYRSGYN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  165 VGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDPLFKK----MKPdFSSAESPEMSGKCVVALA 240
Cdd:PRK08589 156 AAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTGTSEDEAGKTFREnqkwMTP-LGRLGKPEEVAKLVVFLA 234


                 ..
gi 31980844  241 TD 242
Cdd:PRK08589 235 SD 236
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
4-186 6.07e-24

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 101.85  E-value: 6.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSlGGRCVPVVCDSSQESEVKSLFEQVDREQK 83
Cdd:PRK08324 419 PLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGG-PDRALGVACDVTDEAAVQAAFEEAALAFG 497

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   84 GrLDVLVNNAYAGVQAILNttnksfwEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKG--LIVIVS------SPGgl 155
Cdd:PRK08324 498 G-VDIVVSNAGIAISGPIE-------ETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLGgsIVFIASknavnpGPN-- 567

                        170       180       190
                 ....*....|....*....|....*....|.
gi 31980844  156 qhmfNVPYGVGKAACDRLAADCAHELRRHGV 186
Cdd:PRK08324 568 ----FGAYGAAKAAELHLVRQLALELGPDGI 594
PRK08278 PRK08278
SDR family oxidoreductase;
3-243 7.26e-24

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 98.05  E-value: 7.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGR----HLD---TLRATAQEAQSLGGRCVPVVCDSSQESEVKslf 75
Cdd:PRK08278   2 MSLSGKTLFITGASRGIGLAIALRAARDGANIVIAAKtaepHPKlpgTIHTAAEEIEAAGGQALPLVGDVRDEDQVA--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   76 EQVDR--EQKGRLDVLVNNAYAgvqaiLNTTNksFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPG 153
Cdd:PRK08278  79 AAVAKavERFGGIDICVNNASA-----INLTG--TEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSPPL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  154 GL-QHMF--NVPYGVGKAACDRLAADCAHELRRHGVSYVSLWP-GLVQTEMVKEFMAKEDTPEDplfkkmkpdfssAESP 229
Cdd:PRK08278 152 NLdPKWFapHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWPrTTIATAAVRNLLGGDEAMRR------------SRTP 219

                        250
                 ....*....|....
gi 31980844  230 EMSGKCVVALATDP 243
Cdd:PRK08278 220 EIMADAAYEILSRP 233
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 9-251 1.76e-23

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: 96.15  E-value: 1.76e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   9 VCVVTGASRGIGRGIALQLCKAGA-TVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRLD 87
Cdd:cd05324   2 VALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFV-EEKYGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  88 VLVNNayAGVQAILNTTNKSFWEVPASIWdDINnvglrghylcsVYGAR--------LMVPAGKGLIVIVSSpgGLQHMf 159
Cdd:cd05324  81 ILVNN--AGIAFKGFDDSTPTREQARETM-KTN-----------FFGTVdvtqallpLLKKSPAGRIVNVSS--GLGSL- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 160 NVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKedTPEDplfkkmkpdfsSAESPemsgkcvVAL 239
Cdd:cd05324 144 TSAYGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGGGKAPK--TPEE-----------GAETP-------VYL 203

                       250
                ....*....|..
gi 31980844 240 ATDPNILNLSGK 251
Cdd:cd05324 204 ALLPPDGEPTGK 215
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 5-242 1.77e-23

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: 96.76  E-value: 1.77e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITgrhlDTLRATAQE-AQSLGGRCVPVV-CDSSQESEVKSLF-EQVDRE 81
Cdd:cd05326   2 LDGKVAIITGGASGIGEATARLFAKHGARVVIA----DIDDDAGQAvAAELGDPDISFVhCDVTVEADVRAAVdTAVARF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  82 qkGRLDVLVNNAyagvqAILNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNV 161
Cdd:cd05326  78 --GRLDIMFNNA-----GVLGAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGP 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 162 -PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDPLFKKMKPDFSSAESPEMSGKCVVALA 240
Cdd:cd05326 151 hAYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFGVEDEAIEEAVRGAANLKGTALRPEDIAAAVLYLA 230


                ..
gi 31980844 241 TD 242
Cdd:cd05326 231 SD 232
PRK07326 PRK07326
SDR family oxidoreductase;
5-199 3.69e-23

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 95.46  E-value: 3.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSlGGRCVPVVCDSSQESEVKSLFEQVDREQkG 84
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNN-KGNVLGLAADVRDEADVQRAVDAIVAAF-G 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAYAGVQAilnttnkSFWEVPASIWDDINNVGLRGHYlcsvYGARLMVPA---GKGLIVIVSSPGGLQhmfnv 161
Cdd:PRK07326  82 GLDVLIANAGVGHFA-------PVEELTPEEWRLVIDTNLTGAF----YTIKAAVPAlkrGGGYIINISSLAGTN----- 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 31980844  162 PYGVGkaacdrlAADCAH-------------ELRRHGVSYVSLWPGLVQTE 199
Cdd:PRK07326 146 FFAGG-------AAYNASkfglvgfseaamlDLRQYGIKVSTIMPGSVATH 189
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 11-222 4.34e-23

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: 94.88  E-value: 4.34e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  11 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLratAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREqKGRLDVLV 90
Cdd:cd08929   4 LVTGASRGIGEATARLLHAEGYRVGICARDEARL---AAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEA-FGGLDALV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  91 NNAYAGVQAILNTTNKSFWevpasiWDDINNVgLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQhmfnvPYGVGKAAC 170
Cdd:cd08929  80 NNAGVGVMKPVEELTPEEW------RLVLDTN-LTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKN-----AFKGGAAYN 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 31980844 171 DR------LAADCAHELRRHGVSYVSLWPGLVQTEMvkefmakEDTPEDPlFKKMKPD 222
Cdd:cd08929 148 ASkfgllgLSEAAMLDLREANIRVVNVMPGSVDTGF-------AGSPEGQ-AWKLAPE 197
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 5-210 4.47e-23

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: 95.59  E-value: 4.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQKG 84
Cdd:cd05329   4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFGG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNAYAGV-QAILNTTNKSFwevpaSIWDDINnvgLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHM-FNVP 162
Cdd:cd05329  84 KLNILVNNAGTNIrKEAKDYTEEDY-----SLIMSTN---FEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVpSGAP 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 31980844 163 YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDT 210
Cdd:cd05329 156 YGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKEN 203
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 3-200 7.18e-23

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 94.81  E-value: 7.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdRE 81
Cdd:PRK12937   1 MTLSNKVAIVTGASRGIGAAIARRLAADGFAVAVNyAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAA-ET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   82 QKGRLDVLVNNayAGVQAILnttnkSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKgLIVIVSSPGGLQHMFNV 161
Cdd:PRK12937  80 AFGRIDVLVNN--AGVMPLG-----TIADFDLEDFDRTIATNLRGAFVVLREAARHLGQGGR-IINLSTSVIALPLPGYG 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 31980844  162 PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:PRK12937 152 PYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 7-203 7.54e-23

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 94.78  E-value: 7.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRhldTLRATAQEAQSLGgrCVPVVCDSSQESEVKSLFeqvdrEQKGRL 86
Cdd:PRK07060   9 GKSVLVTGASSGIGRACAVALAQRGARVVAAAR---NAAALDRLAGETG--CEPLRLDVGDDAAIRAAL-----AAAGAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   87 DVLVNNayAGVqAILnttnKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGK-GLIVIVSSPGGLQHM-FNVPYG 164
Cdd:PRK07060  79 DGLVNC--AGI-ASL----ESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRgGSIVNVSSQAALVGLpDHLAYC 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 31980844  165 VGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKE 203
Cdd:PRK07060 152 ASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAE 190
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 9-253 1.20e-22

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: 94.28  E-value: 1.20e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   9 VCVVTGASRGIGRGIALQLCKAGAT--VYITGRHLDTLRATAQEAQSlGGRCVPVVCDSSQESEVKSLFEQVdREQKGRL 86
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPsvVVLLARSEEPLQELKEELRP-GLRVTTVKADLSDAAGVEQLLEAI-RKLDGER 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  87 DVLVNNAyagvqAILNTTNKSFwevPASIwDDINNvglrgHYLCSVYGARLMVPA---------GKGLIVIVSSPGGLQH 157
Cdd:cd05367  79 DLLINNA-----GSLGPVSKIE---FIDL-DELQK-----YFDLNLTSPVCLTSTllrafkkrgLKKTVVNVSSGAAVNP 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 158 MFN-VPYGVGKAACDRLAADCAHELRrhGVSYVSLWPGLVQTEMVKEfmAKEDTPEDPL---FKKMKPDfSSAESPEMSG 233
Cdd:cd05367 145 FKGwGLYCSSKAARDMFFRVLAAEEP--DVRVLSYAPGVVDTDMQRE--IRETSADPETrsrFRSLKEK-GELLDPEQSA 219

                       250       260
                ....*....|....*....|
gi 31980844 234 KCVVALAtdPNILNLSGKVL 253
Cdd:cd05367 220 EKLANLL--EKDKFESGAHV 237
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 3-242 1.61e-22

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 94.02  E-value: 1.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRH----LDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQV 78
Cdd:PRK12827   2 ASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHpmrgRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   79 DREQkGRLDVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHY-LCSVYGARLMVPAGKGLIVIVSSPGGLQ- 156
Cdd:PRK12827  82 VEEF-GRLDILVNN--AGI-----ATDAAFAELSIEEWDDVIDVNLDGFFnVTQAALPPMIRARRGGRIVNIASVAGVRg 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  157 HMFNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEmvkefMAKEDTPEDPLFKKMkpDFSSAESPEMSGKCV 236
Cdd:PRK12827 154 NRGQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTP-----MADNAAPTEHLLNPV--PVQRLGEPDEVAALV 226


                 ....*.
gi 31980844  237 VALATD 242
Cdd:PRK12827 227 AFLVSD 232
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 9-257 3.13e-22

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: 93.13  E-value: 3.13e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   9 VCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCD-SSQESEVKsLFEQVdREQKGRLD 87
Cdd:cd05323   2 VAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELQAINPKVKATFVQCDvTSWEQLAA-AFKKA-IEKFGRVD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  88 VLVNNAyagvqAILNTTNKSFWEVPASIWDDINNVGLRGhylcSVYGARLMVPA-------GKGLIVIVSSPGGLQHMFN 160
Cdd:cd05323  80 ILINNA-----GILDEKSYLFAGKLPPPWEKTIDVNLTG----VINTTYLALHYmdknkggKGGVIVNIGSVAGLYPAPQ 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 161 VP-YGVGKAACDRLAADCAHEL-RRHGVSYVSLWPGLVQTEMVKEFMAKEDT--PEDPLfkkmkpdfssaESPEMSGKCV 236
Cdd:cd05323 151 FPvYSASKHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLLPDLVAKEAEmlPSAPT-----------QSPEVVAKAI 219

                       250       260
                ....*....|....*....|.
gi 31980844 237 VALATDPnilNLSGKVLPSCD 257
Cdd:cd05323 220 VYLIEDD---EKNGAIWIVDG 237
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 9-200 4.08e-22

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: 92.43  E-value: 4.08e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   9 VCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqslGGRCVPVVCDSSQESEVKSLFEQVdREQKGRLDV 88
Cdd:cd08932   2 VALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS----GGDVEAVPYDARDPEDARALVDAL-RDRFGRIDV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  89 LVNNAYAGVQAILNTTNKSFWEvpaSIWdDINnvglrghylcsVYGARLMV----PA----GKGLIVIVSS-PGGLQHMF 159
Cdd:cd08932  77 LVHNAGIGRPTTLREGSDAELE---AHF-SIN-----------VIAPAELTrallPAlreaGSGRVVFLNSlSGKRVLAG 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 31980844 160 NVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:cd08932 142 NAGYSASKFALRALAHALRQEGWDHGVRVSAVCPGFVDTPM 182
PRK06947 PRK06947
SDR family oxidoreductase;
8-200 8.68e-22

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 92.18  E-value: 8.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    8 QVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQkGRL 86
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVGINyARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAF-GRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   87 DVLVNNAyaGVQAilntTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPA---GKGLIVIVSSPG---GLQHMFn 160
Cdd:PRK06947  82 DALVNNA--GIVA----PSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDrggRGGAIVNVSSIAsrlGSPNEY- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 31980844  161 VPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:PRK06947 155 VDYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 5-254 1.40e-21

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: 91.81  E-value: 1.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLG--GRCVPVVCDSSQESEVKSlFEQVDREQ 82
Cdd:cd05330   1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIApdAEVLLIKADVSDEAQVEA-YVDATVEQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  83 KGRLDVLVNNayAGVQAILNTTnKSFwevPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN-V 161
Cdd:cd05330  80 FGRIDGFFNN--AGIEGKQNLT-EDF---GADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNqS 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 162 PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMaKEDTPEDPlfKKMKPDFSSAE------SPEMSGKC 235
Cdd:cd05330 154 GYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSL-KQLGPENP--EEAGEEFVSVNpmkrfgEPEEVAAV 230

                       250
                ....*....|....*....
gi 31980844 236 VVALATDPNILnLSGKVLP 254
Cdd:cd05330 231 VAFLLSDDAGY-VNAAVVP 248
PRK06484 PRK06484
short chain dehydrogenase; Validated
 6-203 1.55e-21

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 94.53  E-value: 1.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRataQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDReQKGR 85
Cdd:PRK06484   4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERAR---ERADSLGPDHHALAMDVSDEAQIREGFEQLHR-EFGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   86 LDVLVNNAyagvqAILNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGL-IVIVSSPGGLQHMFN-VPY 163
Cdd:PRK06484  80 IDVLVNNA-----GVTDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKrTAY 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 31980844  164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKE 203
Cdd:PRK06484 155 SASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAE 194
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 5-193 2.53e-21

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: 90.58  E-value: 2.53e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLD-------TLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQ 77
Cdd:cd09762   1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgTIYTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  78 VdREQKGRLDVLVNNAYAgvqaiLNTTNKSfwEVPASIWDDINNVGLRGHYLCSvygaRLMVPAGKGL----IVIVSSPG 153
Cdd:cd09762  81 A-VEKFGGIDILVNNASA-----ISLTGTL--DTPMKRYDLMMGVNTRGTYLCS----KACLPYLKKSknphILNLSPPL 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 31980844 154 GLQHMF---NVPYGVGKAACDRLAADCAHELRRHGVSYVSLWP 193
Cdd:cd09762 149 NLNPKWfknHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PRK06124 PRK06124
SDR family oxidoreductase;
7-209 3.86e-21

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 90.54  E-value: 3.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQkGRL 86
Cdd:PRK06124  11 GQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEH-GRL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   87 DVLVNNAYAgvqailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKG-LIVIVSSPGGLQHMFNVPYGV 165
Cdd:PRK06124  90 DILVNNVGA-------RDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGrIIAITSIAGQVARAGDAVYPA 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 31980844  166 GKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKED 209
Cdd:PRK06124 163 AKQGLTGLMRALAAEFGPHGITSNAIAPGYFATETNAAMAADPA 206
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 5-195 4.24e-21

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 90.46  E-value: 4.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYItgrhLDtLRATAQEAQSLggrcVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVN----AD-IHGGDGQHENY----QFVPTDVSSAEEVNHTVAEI-IEKFG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAYAGVQAIL--NTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGL-----QH 157
Cdd:PRK06171  77 RIDGLVNNAGINIPRLLvdEKDPAGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLegsegQS 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 31980844  158 MfnvpYGVGKAACDRLAADCAHELRRHGVSYVSLWPGL 195
Cdd:PRK06171 157 C----YAATKAALNSFTRSWAKELGKHNIRVVGVAPGI 190
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 5-230 5.00e-21

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: 89.95  E-value: 5.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVV-CDSSQESEVKSLFEQVdREQK 83
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVpLDMSDLEDAEQVVEEA-LKLF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  84 GRLDVLVNNayagvqAILNTTNKsFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLqhmFNVPY 163
Cdd:cd05332  80 GGLDILINN------AGISMRSL-FHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGK---IGVPF 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980844 164 GVGKAA----------CDRlaadcaHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEdplfKKMKPDFSSAESPE 230
Cdd:cd05332 150 RTAYAAskhalqgffdSLR------AELSEPNISVTVVCPGLIDTNIAMNALSGDGSMS----AKMDDTTANGMSPE 216
PRK07832 PRK07832
SDR family oxidoreductase;
10-238 5.24e-21

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 90.49  E-value: 5.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   10 CVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRcVP--VVCDSSQESEVKSLFEQVDREQkGRLD 87
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGT-VPehRALDISDYDAVAAFAADIHAAH-GSMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   88 VLVNNayAGVqAILNTTNKsfweVPASIWDDINNVGLRGhylcSVYGARLMVP----AGK-GLIVIVSSPGGLQHM-FNV 161
Cdd:PRK07832  81 VVMNI--AGI-SAWGTVDR----LTHEQWRRMVDVNLMG----PIHVIETFVPpmvaAGRgGHLVNVSSAAGLVALpWHA 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31980844  162 PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDPLFKKMKPDFSS-AESPEMSGKCVVA 238
Cdd:PRK07832 150 AYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVEIAGVDREDPRVQKWVDRFRGhAVTPEKAAEKILA 227
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-210 5.35e-21

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 90.02  E-value: 5.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    8 QVCVVTGASRGIGRGIALQLCKAGATVYITG-RHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRL 86
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDrPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAA-QAAWGRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   87 DVLVNNayAGVQA-----ILNTTNKSFwevpasiwDDINNVGLRGHYLCSVYGARLMV------PAGKGLIVIVSSPGGL 155
Cdd:PRK12745  82 DCLVNN--AGVGVkvrgdLLDLTPESF--------DRVLAINLRGPFFLTQAVAKRMLaqpepeELPHRSIVFVSSVNAI 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 31980844  156 QHMFN-VPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDT 210
Cdd:PRK12745 152 MVSPNrGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVTAKYDA 207
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 8-243 5.89e-21

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: 89.36  E-value: 5.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLfEQVDREQKGRLD 87
Cdd:cd05360   1 QVVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERA-ADTAVERFGRID 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  88 VLVNNAYAGVQAilnttnkSFWEVPASIWDDINNVGLRGHylcsVYGARLMVP----AGKGLIVIVSSPGGLQHM-FNVP 162
Cdd:cd05360  80 TWVNNAGVAVFG-------RFEDVTPEEFRRVFDVNYLGH----VYGTLAALPhlrrRGGGALINVGSLLGYRSApLQAA 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 163 YGVGKAAC----DRLAADCAHELRrhGVSYVSLWPGLVQT---EMVKEFMAKEDTPEDPLFKkmkpdfssaesPEMSGKC 235
Cdd:cd05360 149 YSASKHAVrgftESLRAELAHDGA--PISVTLVQPTAMNTpffGHARSYMGKKPKPPPPIYQ-----------PERVAEA 215


                ....*...
gi 31980844 236 VVALATDP 243
Cdd:cd05360 216 IVRAAEHP 223
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 6-202 1.23e-20

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 88.94  E-value: 1.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRC--VPVVCDSSQESEVKSLFEQVDrEQK 83
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEGmaYGFGADATSEQSVLALSRGVD-EIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   84 GRLDVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAG-KGLIV-IVSSPGGLQHMFNV 161
Cdd:PRK12384  80 GRVDLLVYN--AGI-----AKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIqINSKSGKVGSKHNS 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 31980844  162 PYGVGKAACDRLAADCAHELRRHGVSYVSLWPG-LVQTEMVK 202
Cdd:PRK12384 153 GYSAAKFGGVGLTQSLALDLAEYGITVHSLMLGnLLKSPMFQ 194
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 3-236 1.31e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 88.91  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    3 APMKGQVCVVTGASRGIGRGIALQLCKAGAT-VYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDRE 81
Cdd:PRK06198   2 GRLDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   82 QkGRLDVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAG-KGLIVIV---SSPGGlqH 157
Cdd:PRK06198  82 F-GRLDALVNA--AGL-----TDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKaEGTIVNIgsmSAHGG--Q 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  158 MFNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTE----MVKEFMAKEDTPED------PLFKKMKPD----- 222
Cdd:PRK06198 152 PFLAAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATEgedrIQREFHGAPDDWLEkaaatqPFGRLLDPDevara 231

                        250
                 ....*....|....*..
gi 31980844  223 ---FSSAESPEMSGKCV 236
Cdd:PRK06198 232 vafLLSDESGLMTGSVI 248
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 5-212 1.32e-20

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 89.14  E-value: 1.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFeQVDREQKG 84
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALA-DFALSKLG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAYAGvqailntTNKSFwEVPAS--IWDDINNVGLRGHyLCSVyGARLMVPAGKGLIVIVSSPGGLQHMFNV- 161
Cdd:PRK06113  88 KVDILVNNAGGG-------GPKPF-DMPMAdfRRAYELNVFSFFH-LSQL-VAPEMEKNGGGVILTITSMAAENKNINMt 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 31980844  162 PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMakedTPE 212
Cdd:PRK06113 158 SYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVI----TPE 204
PRK07454 PRK07454
SDR family oxidoreductase;
12-200 1.37e-20

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 88.48  E-value: 1.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   12 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRLDVLVN 91
Cdd:PRK07454  11 ITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAEL-LEQFGCPDVLIN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   92 NAYAGVQAILNTTnksfwevPASIWDDINNVGLRGHYLCsvygARLMVPA----GKGLIVIVSSPGGlqhmFNV-----P 162
Cdd:PRK07454  90 NAGMAYTGPLLEM-------PLSDWQWVIQLNLTSVFQC----CSAVLPGmrarGGGLIINVSSIAA----RNAfpqwgA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 31980844  163 YGVGKAAcdrLAA--DC-AHELRRHGVSYVSLWPGLVQTEM 200
Cdd:PRK07454 155 YCVSKAA---LAAftKClAEEERSHGIRVCTITLGAVNTPL 192
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 11-214 1.46e-20

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: 88.12  E-value: 1.46e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  11 VVTGASRGIGRGIALQLCKAG-ATVYITGRHldtlRATAQEAQSLGGRCVPVVC---DSSqeSEVKSLFEQVDREQKGR- 85
Cdd:cd05325   2 LITGASRGIGLELVRQLLARGnNTVIATCRD----PSAATELAALGASHSRLHIlelDVT--DEIAESAEAVAERLGDAg 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  86 LDVLVNNAyagvqAIL-NTTNKSfwEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGG---LQHMFNV 161
Cdd:cd05325  76 LDVLINNA-----GILhSYGPAS--EVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGsigDNTSGGW 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 31980844 162 -PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFmAKEDTPEDP 214
Cdd:cd05325 149 ySYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPF-AKNKGPITP 201
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 5-234 1.57e-20

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 89.35  E-value: 1.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYIT--GRHLDTLRATAQEAQSL-------GGRCVPVVCDSSQESEVKSLF 75
Cdd:PRK07791   4 LDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNdiGVGLDGSASGGSAAQAVvdeivaaGGEAVANGDDIADWDGAANLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   76 EQVdREQKGRLDVLVNNayAGV---QAILNTTNKSfwevpasiWDDINNVGLRGHYLCSVYGA---RLMVPAGKGL---I 146
Cdd:PRK07791  84 DAA-VETFGGLDVLVNN--AGIlrdRMIANMSEEE--------WDAVIAVHLKGHFATLRHAAaywRAESKAGRAVdarI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  147 VIVSSPGGLQHmfNV---PYGVGKAACDRLAADCAHELRRHGVSYVSLWPgLVQTEMVK----EFMAKedtPEDPLFKKM 219
Cdd:PRK07791 153 INTSSGAGLQG--SVgqgNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP-AARTRMTEtvfaEMMAK---PEEGEFDAM 226

                        250       260
                 ....*....|....*....|...
gi 31980844  220 KPD--------FSSAESPEMSGK 234
Cdd:PRK07791 227 APEnvsplvvwLGSAESRDVTGK 249
PRK09730 PRK09730
SDR family oxidoreductase;
9-200 2.42e-20

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 87.98  E-value: 2.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    9 VCVVTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDReQKGRLD 87
Cdd:PRK09730   3 IALVTGGSRGIGRATALLLAQEGYTVAVNYQQnLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQ-HDEPLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   88 VLVNNAyagvqAILnTTNKSFWEVPAsiwDDINNV---GLRGHYLCSVYGARLMV--PAGK-GLIVIVSS-------PGG 154
Cdd:PRK09730  82 ALVNNA-----GIL-FTQCTVENLTA---ERINRVlstNVTGYFLCCREAVKRMAlkHGGSgGAIVNVSSaasrlgaPGE 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 31980844  155 LqhmfnVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:PRK09730 153 Y-----VDYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEM 193
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 5-242 2.69e-20

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: 87.98  E-value: 2.69e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:cd08945   1 QDSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAA-VARYG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNA---YAGVQAilnttnksfwEVPASIWDDINNVGLRGHYLCS--VYGARLMVPAGKGLIVIVSSPGGLQH-M 158
Cdd:cd08945  80 PIDVLVNNAgrsGGGATA----------ELADELWLDVVETNLTGVFRVTkeVLKAGGMLERGTGRIINIASTGGKQGvV 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 159 FNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM---VKEFMAKE-DTPEDPLFKKM--KPDFSSAESPEMS 232
Cdd:cd08945 150 HAAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMaasVREHYADIwEVSTEEAFDRItaRVPLGRYVTPEEV 229

                       250
                ....*....|
gi 31980844 233 GKCVVALATD 242
Cdd:cd08945 230 AGMVAYLIGD 239
PRK05855 PRK05855
SDR family oxidoreductase;
4-202 3.13e-20

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 90.81  E-value: 3.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQK 83
Cdd:PRK05855 312 PFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWV-RAEH 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   84 GRLDVLVNNAYAGVQAilnttnkSFWEVPASIWDDINNVGLRGhylcSVYGARL----MVPAGK-GLIVIVSSPGGLQHM 158
Cdd:PRK05855 391 GVPDIVVNNAGIGMAG-------GFLDTSAEDWDRVLDVNLWG----VIHGCRLfgrqMVERGTgGHIVNVASAAAYAPS 459

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 31980844  159 FNVP-YGVGKAACDRLaADCAH-ELRRHGVSYVSLWPGLVQTEMVK 202
Cdd:PRK05855 460 RSLPaYATSKAAVLML-SECLRaELAAAGIGVTAICPGFVDTNIVA 504
PRK07074 PRK07074
SDR family oxidoreductase;
8-199 3.81e-20

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 87.90  E-value: 3.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqsLG-GRCVPVVCDSSQESEVKSLFEQVdREQKGRL 86
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADA---LGdARFVPVACDLTDAASLAAALANA-AAERGPV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   87 DVLVNNAYAGVQAILNTTNksfwevpASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLqHMFNVP-YGV 165
Cdd:PRK07074  79 DVLVANAGAARAASLHDTT-------PASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGM-AALGHPaYSA 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 31980844  166 GKAACDRLAADCAHELRRHGVSYVSLWPGLVQTE 199
Cdd:PRK07074 151 AKAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQ 184
PRK06123 PRK06123
SDR family oxidoreductase;
8-200 3.91e-20

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 87.53  E-value: 3.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQkGRL 86
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERGYAVCLNYLRnRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDREL-GRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   87 DVLVNNAyagvqAILNTTNKsFWEVPASIWDDINNVGLRGHYLCSVYGARLMVP--AGK-GLIVIVSS-------PGGLq 156
Cdd:PRK06123  82 DALVNNA-----GILEAQMR-LEQMDAARLTRIFATNVVGSFLCAREAVKRMSTrhGGRgGAIVNVSSmaarlgsPGEY- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 31980844  157 hmfnVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:PRK06123 155 ----IDYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEI 194
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
5-214 4.57e-20

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 87.55  E-value: 4.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHlDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEqVDREQKG 84
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANLILLDIS-PEIEKLADELCGRGHRCTAVVADVRDPASVAAAIK-RAKEKEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNayAGVQAILNttnksFWEVPASIWDDINNVGLRGHYlcSVYGARL--MVPAGKGLIVIVSSPGG--LQHMFN 160
Cdd:PRK08226  82 RIDILVNN--AGVCRLGS-----FLDMSDEDRDFHIDINIKGVW--NVTKAVLpeMIARKDGRIVMMSSVTGdmVADPGE 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 31980844  161 VPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVkEFMAKEDTPEDP 214
Cdd:PRK08226 153 TAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMA-ESIARQSNPEDP 205
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 9-222 5.02e-20

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: 86.91  E-value: 5.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   9 VCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRLDV 88
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKI-KKEVGDVTI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  89 LVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHYlcSVYGARL--MVPAGKGLIVIVSSPGGLqhmFNVP---- 162
Cdd:cd05339  80 LINN--AGV-----VSGKKLLELPDEEIEKTFEVNTLAHF--WTTKAFLpdMLERNHGHIVTIASVAGL---ISPAglad 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980844 163 YGVGKAACDRLAADCAHELRRH---GVSYVSLWPGLVQTEMvkefMAKEDTPEDPLFKKMKPD 222
Cdd:cd05339 148 YCASKAAAVGFHESLRLELKAYgkpGIKTTLVCPYFINTGM----FQGVKTPRPLLAPILEPE 206
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 4-242 5.22e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 87.41  E-value: 5.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqsLGGRCVPVVCDSSQESEVKSLFEQVdREQK 83
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQL---LGGNAKGLVCDVSDSQSVEAAVAAV-ISAF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   84 GRLDVLVNNayAGVqAILNTTNksfwEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGL----QHmf 159
Cdd:PRK06841  88 GRIDILVNS--AGV-ALLAPAE----DVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVvaleRH-- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  160 nVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEdTPEDplFKKMKPDFSSAESPEMSGkCVVAL 239
Cdd:PRK06841 159 -VAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGKKAWAGE-KGER--AKKLIPAGRFAYPEEIAA-AALFL 233


                 ...
gi 31980844  240 ATD 242
Cdd:PRK06841 234 ASD 236
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 6-194 5.57e-20

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: 87.00  E-value: 5.57e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGG-RCVPVVCDSSQESEVKSLFEQVDrEQKG 84
Cdd:cd08930   1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKnRVIALELDITSKESIKELIESYL-EKFG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNAYAGVQailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGL--------- 155
Cdd:cd08930  80 RIDILINNAYPSPK----VWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGViapdfriye 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 31980844 156 -QHMFN-VPYGVGKAACDRLAADCAHELRRHGVSYVSLWPG 194
Cdd:cd08930 156 nTQMYSpVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG 196
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 6-194 6.34e-20

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 87.31  E-value: 6.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHlDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGR 85
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRS-ELVHEVAAELRAAGGEALALTADLETYAGAQAAMAAA-VEAFGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   86 LDVLVNNAYAGVQAilnttnKSFWEV-PASIWDDINNVGLRGHYLCSvygARL--MVPAGKGLIVIVSS--PGGLQHmfn 160
Cdd:PRK12823  85 IDVLINNVGGTIWA------KPFEEYeEEQIEAEIRRSLFPTLWCCR---AVLphMLAQGGGAIVNVSSiaTRGINR--- 152

                        170       180       190
                 ....*....|....*....|....*....|....
gi 31980844  161 VPYGVGKAACDRLAADCAHELRRHGVSYVSLWPG 194
Cdd:PRK12823 153 VPYSAAKGGVNALTASLAFEYAEHGIRVNAVAPG 186
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 6-222 7.83e-20

(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: 86.61  E-value: 7.83e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYI---------TGRHLDTLRATAQEAQSLGGRCVPvvcDSSQESEVKSLFE 76
Cdd:cd05353   4 DGRVVLVTGAGGGLGRAYALAFAERGAKVVVndlggdrkgSGKSSSAADKVVDEIKAAGGKAVA---NYDSVEDGEKIVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  77 QVdREQKGRLDVLVNNAyagvqAILNttNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQ 156
Cdd:cd05353  81 TA-IDAFGRVDILVNNA-----GILR--DRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLY 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980844 157 HMF-NVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPgLVQTEMVKEFMakedtPEDpLFKKMKPD 222
Cdd:cd05353 153 GNFgQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAP-AAGSRMTETVM-----PED-LFDALKPE 212
PRK07063 PRK07063
SDR family oxidoreductase;
1-212 8.04e-20

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 87.03  E-value: 8.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQE--AQSLGGRCVPVVCDSSQESEVKSLFEQV 78
Cdd:PRK07063   1 MMNRLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAiaRDVAGARVLAVPADVTDAASVAAAVAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   79 DREQkGRLDVLVNNAYAGVQA-ILNTTNKSfwevpasiWDDINNVGLRGHYlcsvYGARL----MVPAGKGLIVIVSSpg 153
Cdd:PRK07063  81 EEAF-GPLDVLVNNAGINVFAdPLAMTDED--------WRRCFAVDLDGAW----NGCRAvlpgMVERGRGSIVNIAS-- 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31980844  154 glQHMFNV-----PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPE 212
Cdd:PRK07063 146 --THAFKIipgcfPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWWNAQPDPA 207
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 6-242 9.31e-20

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: 86.73  E-value: 9.31e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITG-RHLDTLRATAQEAQSL-GGRCVPVVCDSSQESEVKSLFEQVDReQK 83
Cdd:cd08940   1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGfGDAAEIEAVRAGLAAKhGVKVLYHGADLSKPAAIEDMVAYAQR-QF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  84 GRLDVLVNNayAGVQAILNTTnksfwEVPASIWDDINNVGLRGhylcSVYGARLMVPAGK----GLIVIVSSPGGL-QHM 158
Cdd:cd08940  80 GGVDILVNN--AGIQHVAPIE-----DFPTEKWDAIIALNLSA----VFHTTRLALPHMKkqgwGRIINIASVHGLvASA 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 159 FNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVK----EFMAKEDTPEDP----LFKKMKPDFSSAeSPE 230
Cdd:cd08940 149 NKSAYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVEkqisALAQKNGVPQEQaareLLLEKQPSKQFV-TPE 227

                       250
                ....*....|..
gi 31980844 231 MSGKCVVALATD 242
Cdd:cd08940 228 QLGDTAVFLASD 239
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 5-98 9.51e-20

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: 86.37  E-value: 9.51e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGrcvpVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:COG3967   3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPGLHT----IVLDVADPASIAALAEQV-TAEFP 77

                        90
                ....*....|....
gi 31980844  85 RLDVLVNNayAGVQ 98
Cdd:COG3967  78 DLNVLINN--AGIM 89
PRK07201 PRK07201
SDR family oxidoreductase;
4-201 1.27e-19

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 89.24  E-value: 1.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQk 83
Cdd:PRK07201 368 PLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEH- 446

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   84 GRLDVLVNNAYAGV-QAILNTTNKS--FWEVPAsiwddINnvglrghYlcsvYGA-RL-------MVPAGKGLIVIVSSP 152
Cdd:PRK07201 447 GHVDYLVNNAGRSIrRSVENSTDRFhdYERTMA-----VN-------Y----FGAvRLilgllphMRERRFGHVVNVSSI 510

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 31980844  153 GGLQhmfNVP----YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMV 201
Cdd:PRK07201 511 GVQT---NAPrfsaYVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTPMI 560
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 6-245 1.46e-19

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: 86.03  E-value: 1.46e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCV-PVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:cd05343   5 RGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLfPYQCDLSNEEQILSMFSAI-RTQHQ 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNAYAGVQAILNTTnksfwevPASIWDDINNVGLRGHYLCSVYGARLM--VPAGKGLIVIVSSPGG----LQHM 158
Cdd:cd05343  84 GVDVCINNAGLARPEPLLSG-------KTEGWKEMFDVNVLALSICTREAYQSMkeRNVDDGHIININSMSGhrvpPVSV 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 159 FNVpYGVGKAACDRLAADCAHELR--RHGVSYVSLWPGLVQTEMV-KEFMAKEDTPEDPL--FKKMKPDfssaespEMSG 233
Cdd:cd05343 157 FHF-YAATKHAVTALTEGLRQELReaKTHIRATSISPGLVETEFAfKLHDNDPEKAAATYesIPCLKPE-------DVAN 228

                       250
                ....*....|..
gi 31980844 234 KCVVALATDPNI 245
Cdd:cd05343 229 AVLYVLSTPPHV 240
PRK12746 PRK12746
SDR family oxidoreductase;
5-250 1.52e-19

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 85.86  E-value: 1.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYI-TGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQK 83
Cdd:PRK12746   4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNELQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   84 GR-----LDVLVNNAYAGVQAILNTTNKsfwevpaSIWDDINNVGLRGHYLCSVYGARLMVPAGKgLIVIVSSPGGLQHM 158
Cdd:PRK12746  84 IRvgtseIDILVNNAGIGTQGTIENTTE-------EIFDEIMAVNIKAPFFLIQQTLPLLRAEGR-VINISSAEVRLGFT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  159 FNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMakeDTPEDPLFKKMKPDFSSAESPEMSGKCVVA 238
Cdd:PRK12746 156 GSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLL---DDPEIRNFATNSSVFGRIGQVEDIADAVAF 232

                        250
                 ....*....|....*...
gi 31980844  239 LATDPN------ILNLSG 250
Cdd:PRK12746 233 LASSDSrwvtgqIIDVSG 250
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 7-202 1.55e-19

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: 85.73  E-value: 1.55e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVP-VVCDSSQESEVkslFEQVDREQKGr 85
Cdd:cd05356   1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKtIAADFSAGDDI---YERIEKELEG- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  86 LDV--LVNNAyagvqAILNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMfnvP- 162
Cdd:cd05356  77 LDIgiLVNNV-----GISHSIPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPT---Pl 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 31980844 163 ---YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVK 202
Cdd:cd05356 149 latYSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSK 191
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-215 1.97e-19

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 86.76  E-value: 1.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVyITGRHLDTLRA--TAQEAQSLGGRCVPVVCDSSQESEVKSLFEQV 78
Cdd:PRK07792   6 NTTDLSGKVAVVTGAAAGLGRAEALGLARLGATV-VVNDVASALDAsdVLDEIRAAGAKAVAVAGDISQRATADELVATA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   79 DreQKGRLDVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGA---RLMVPAGK----GLIVIVSS 151
Cdd:PRK07792  85 V--GLGGLDIVVNN--AGI-----TRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAaywRAKAKAAGgpvyGRIVNTSS 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31980844  152 PGGLQHMFNVP-YGVGKAACDRLAADCAHELRRHGVSYVSLWPgLVQTEMVKEFMAkeDTPE------DPL 215
Cdd:PRK07792 156 EAGLVGPVGQAnYGAAKAGITALTLSAARALGRYGVRANAICP-RARTAMTADVFG--DAPDveaggiDPL 223
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 7-251 2.13e-19

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: 85.74  E-value: 2.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQE--AQSLGGRCVPVVCD-SSQESeVKSLFEQVdREQK 83
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEikKETGNAKVEVIQLDlSSLAS-VRQFAEEF-LARF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  84 GRLDVLVNNayAGVQAILNTTNKsfwevpasiwDDIN-----NvglrghYLCSVYGARLMVPAGK----GLIVIVSSPGG 154
Cdd:cd05327  79 PRLDILINN--AGIMAPPRRLTK----------DGFElqfavN------YLGHFLLTNLLLPVLKasapSRIVNVSSIAH 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 155 ---------LQHMFNVPYGVGKAACD-RLAadC---AHELRRH----GVSYVSLWPGLVQTEMVKefmakedtpEDPLFK 217
Cdd:cd05327 141 ragpidfndLDLENNKEYSPYKAYGQsKLA--NilfTRELARRlegtGVTVNALHPGVVRTELLR---------RNGSFF 209

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 31980844 218 KMKPDFS--SAESPEMSGKCVVALATDPNILNLSGK 251
Cdd:cd05327 210 LLYKLLRpfLKKSPEQGAQTALYAATSPELEGVSGK 245
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 9-222 2.14e-19

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: 85.31  E-value: 2.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   9 VCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRLDV 88
Cdd:cd05365   1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKAT-VSQFGGITI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  89 LVNNAYAGvqailntTNKSFweVPASIWDDINNV---GLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNV-PYG 164
Cdd:cd05365  80 LVNNAGGG-------GPKPF--DMPMTEEDFEWAfklNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIaAYG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 31980844 165 VGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMakedTPEdpLFKKMKPD 222
Cdd:cd05365 151 SSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALASVL----TPE--IERAMLKH 202
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 9-186 2.27e-19

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: 85.13  E-value: 2.27e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   9 VCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATA-QEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREqKGRLD 87
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLvDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEE-IGPLE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  88 VLVNNAYAGVQ-AILNTTNKSF---WEVPASiwddinnvglrGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN-VP 162
Cdd:cd05373  80 VLVYNAGANVWfPILETTPRVFekvWEMAAF-----------GGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGfAA 148

                       170       180
                ....*....|....*....|....
gi 31980844 163 YGVGKAACDRLAADCAHELRRHGV 186
Cdd:cd05373 149 FAGAKFALRALAQSMARELGPKGI 172
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 12-200 2.39e-19

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: 85.07  E-value: 2.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  12 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQkGRLDVLVN 91
Cdd:cd05350   3 ITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAEL-GGLDLVII 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  92 NayAGVQAILNTTNKSFWEVPASIwdDINNVGlrghylcSVYGARLMVPA----GKGLIVIVSSPGGLQHMFNVP-YGVG 166
Cdd:cd05350  82 N--AGVGKGTSLGDLSFKAFRETI--DTNLLG-------AAAILEAALPQfrakGRGHLVLISSVAALRGLPGAAaYSAS 150

                       170       180       190
                ....*....|....*....|....*....|....
gi 31980844 167 KAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:cd05350 151 KAALSSLAESLRYDVKKRGIRVTVINPGFIDTPL 184
PRK09242 PRK09242
SDR family oxidoreductase;
5-210 2.56e-19

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 85.57  E-value: 2.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRA--TAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDrEQ 82
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQarDELAEEFPEREVHGLAADVSDDEDRRAILDWVE-DH 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   83 KGRLDVLVNNAYAGVQailnttnKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN-V 161
Cdd:PRK09242  86 WDGLHILVNNAGGNIR-------KAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSgA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 31980844  162 PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDT 210
Cdd:PRK09242 159 PYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDY 207
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 1-151 2.91e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 86.51  E-value: 2.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDR 80
Cdd:PRK07109   2 MLKPIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980844   81 EQkGRLDVLVNNAYAGVQAilnttnkSFWEVPAsiwDDINNVgLRGHYLCSVYGA----RLMVPAGKGLIVIVSS 151
Cdd:PRK07109  82 EL-GPIDTWVNNAMVTVFG-------PFEDVTP---EEFRRV-TEVTYLGVVHGTlaalRHMRPRDRGAIIQVGS 144
PRK06484 PRK06484
short chain dehydrogenase; Validated
 7-206 3.11e-19

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 87.98  E-value: 3.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATaqeAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRL 86
Cdd:PRK06484 269 PRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKL---AEALGDEHLSVQADITDEAAVESAFAQI-QARWGRL 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   87 DVLVNNayAGVQAILNTTNKSFWEVPASIWDdinnVGLRGHYLCSVYGARLMvpAGKGLIVIVSSPGGL-----QHmfnv 161
Cdd:PRK06484 345 DVLVNN--AGIAEVFKPSLEQSAEDFTRVYD----VNLSGAFACARAAARLM--SQGGVIVNLGSIASLlalppRN---- 412

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 31980844  162 PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMA 206
Cdd:PRK06484 413 AYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIETPAVLALKA 457
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 4-201 3.36e-19

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 85.38  E-value: 3.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAqslgGRCVPVVCDSSQESEVKSLFEQVDReQK 83
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAEL----GLVVGGPLDVTDPASFAAFLDAVEA-DL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   84 GRLDVLVNNayAGVQAIlnttnKSFWEVPASIWDDINNVGLRGhylcSVYGARL----MVPAGKGLIVIVSSPGGlqhMF 159
Cdd:PRK07825  77 GPIDVLVNN--AGVMPV-----GPFLDEPDAVTRRILDVNVYG----VILGSKLaaprMVPRGRGHVVNVASLAG---KI 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 31980844  160 NVP----YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMV 201
Cdd:PRK07825 143 PVPgmatYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELI 188
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 1-213 3.77e-19

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 84.46  E-value: 3.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVvcDSSQESEVKSLFEQVDR 80
Cdd:PRK12828   1 MEHSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGGI--DLVDPQAARRAVDEVNR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   81 eQKGRLDVLVNNAYAgvqailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQH-MF 159
Cdd:PRK12828  79 -QFGRLDALVNIAGA-------FVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAgPG 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 31980844  160 NVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKED-----TPED 213
Cdd:PRK12828 151 MGAYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNRADMPDADfsrwvTPEQ 209
PRK06114 PRK06114
SDR family oxidoreductase;
5-242 5.30e-19

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 84.45  E-value: 5.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDT-LRATAQEAQSLGGRCVPVVCDSSQESevkSLFEQVDREQK 83
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDgLAETAEHIEAAGRRAIQIAADVTSKA---DLRAAVARTEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   84 --GRLDVLVNNA-YAGVQAILnttnksfwEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGL---QH 157
Cdd:PRK06114  83 elGALTLAVNAAgIANANPAE--------EMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIivnRG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  158 MFNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEfmaKEDTPEDPLFKKMKPDFSSAESPEMSGKCVV 237
Cdd:PRK06114 155 LLQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTR---PEMVHQTKLFEEQTPMQRMAKVDEMVGPAVF 231


                 ....*
gi 31980844  238 aLATD 242
Cdd:PRK06114 232 -LLSD 235
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 5-244 7.24e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 84.57  E-value: 7.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRhlDTLRATAQEAQSLggrcvpVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:PRK06179   2 SNSKVALVTGASSGIGRATAEKLARAGYRVFGTSR--NPARAAPIPGVEL------LELDVTDDASVQAAVDEV-IARAG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNayAGVQAILNTTNKSFWEVPASIwdDINNVGLrghylcsVYGARLMVP----AGKGLIVIVSSPGGLQHM-F 159
Cdd:PRK06179  73 RIDVLVNN--AGVGLAGAAEESSIAQAQALF--DTNVFGI-------LRMTRAVLPhmraQGSGRIINISSVLGFLPApY 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  160 NVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMvKEFMAKEDTP-------EDPLFKKMKPDFSSAESPEMS 232
Cdd:PRK06179 142 MALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNF-DANAPEPDSPlaeydreRAVVSKAVAKAVKKADAPEVV 220

                        250
                 ....*....|..
gi 31980844  233 GKCVVALATDPN 244
Cdd:PRK06179 221 ADTVVKAALGPW 232
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 1-212 9.31e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 84.01  E-value: 9.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqsLGGRCVPVvcDSSQESEVKSLFEQVDr 80
Cdd:PRK06057   1 LSQRLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADE---VGGLFVPT--DVTDEDAVNALFDTAA- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   81 EQKGRLDVLVNNayAGVQ-----AILNTtnksfwEVPAsiWDDINNVGLRGHYLCSVYGARLMVPAGKGLIV----IVSS 151
Cdd:PRK06057  75 ETYGSVDIAFNN--AGISppeddSILNT------GLDA--WQRVQDVNLTSVYLCCKAALPHMVRQGKGSIIntasFVAV 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31980844  152 PGGLQHmfNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEdtPE 212
Cdd:PRK06057 145 MGSATS--QISYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELFAKD--PE 201
PRK08264 PRK08264
SDR family oxidoreductase;
5-213 9.74e-19

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 83.40  E-value: 9.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGAT-VYITGRHLDTlrataqeAQSLGGRCVPVVCDSSQESEVKSLFEQVdreqk 83
Cdd:PRK08264   4 IKGKVVLVTGANRGIGRAFVEQLLARGAAkVYAAARDPES-------VTDLGPRVVPLQLDVTDPASVAAAAEAA----- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   84 GRLDVLVNNayAGVqailNTTNKSFWEvpasiwDDInnVGLRGHYLCSVYG----ARLMVPA----GKGLIVIVSSPGGL 155
Cdd:PRK08264  72 SDVTILVNN--AGI----FRTGSLLLE------GDE--DALRAEMETNYFGplamARAFAPVlaanGGGAIVNVLSVLSW 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 31980844  156 QHM-FNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPED 213
Cdd:PRK08264 138 VNFpNLGTYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAGLDAPKASPAD 196
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 5-202 2.09e-18

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 82.88  E-value: 2.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREqKG 84
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKD-IG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNayAGVQailntTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIV-IVSSPGGLQHMFNVPY 163
Cdd:PRK08085  86 PIDVLINN--AGIQ-----RRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIInICSMQSELGRDTITPY 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 31980844  164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVK 202
Cdd:PRK08085 159 AASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTK 197
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 5-213 2.64e-18

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: 82.07  E-value: 2.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGAT-VYITGRHLDTLRATAQEAQSlggRCVPVVCDSSQESEVKSLFEQVDreqk 83
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAKkVYAAVRDPGSAAHLVAKYGD---KVVPLRLDVTDPESIKAAAAQAK---- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  84 gRLDVLVNNayAGVQAILNTTNKSFWEVpASIWDDINNVGLRGhyLCSVYgARLMVPAGKGLIVIVSSPGGLQhmfNVP- 162
Cdd:cd05354  74 -DVDVVINN--AGVLKPATLLEEGALEA-LKQEMDVNVFGLLR--LAQAF-APVLKANGGGAIVNLNSVASLK---NFPa 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 31980844 163 ---YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPED 213
Cdd:cd05354 144 mgtYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAGGPKESPET 197
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 4-199 2.86e-18

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: 82.58  E-value: 2.86e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHlDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQK 83
Cdd:cd08937   1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRS-ELVHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAA-VERF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  84 GRLDVLVNNAYAGVQA----------ILNTTNKSFWevPAsIWddinnvglrghylCSVYGARLMVPAGKGLIVIVSSPg 153
Cdd:cd08937  79 GRVDVLINNVGGTIWAkpyehyeeeqIEAEIRRSLF--PT-LW-------------CCRAVLPHMLERQQGVIVNVSSI- 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 31980844 154 GLQHMFNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTE 199
Cdd:cd08937 142 ATRGIYRIPYSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAP 187
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 6-209 3.42e-18

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 82.64  E-value: 3.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGR 85
Cdd:PRK08277   9 KGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQI-LEDFGP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   86 LDVLVNNA--------YAGVQAILNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQH 157
Cdd:PRK08277  88 CDILINGAggnhpkatTDNEFHELIEPTKTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAFTP 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 31980844  158 MFNVP-YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKED 209
Cdd:PRK08277 168 LTKVPaYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRALLFNED 220
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 11-201 5.72e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 82.16  E-value: 5.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   11 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQE--AQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRLDV 88
Cdd:PRK05875  11 LVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEieALKGAGAVRYEPADVTDEDQVARAVDAA-TAWHGRLHG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   89 LVNNAyAGVQAILNTTnksfwEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQ-HMFNVPYGVGK 167
Cdd:PRK05875  90 VVHCA-GGSETIGPIT-----QIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNtHRWFGAYGVTK 163

                        170       180       190
                 ....*....|....*....|....*....|....
gi 31980844  168 AACDRLAADCAHELRRHGVSYVSLWPGLVQTEMV 201
Cdd:PRK05875 164 SAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLV 197
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 7-213 6.91e-18

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: 81.09  E-value: 6.91e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITgrHLDTLRAtAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRL 86
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFA--DIDEERG-ADFAEAEGPNLFFVHGDVADETLVKFVVYAM-LEKLGRI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  87 DVLVNNAyagvqAILNTtnKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVpAGKGLIVIVSSPGGLQHMFNV-PYGV 165
Cdd:cd09761  77 DVLVNNA-----ARGSK--GILSSLLLEEWDRILSVNLTGPYELSRYCRDELI-KNKGRIINIASTRAFQSEPDSeAYAA 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 31980844 166 GKAACDRLAADCAHELRRHgVSYVSLWPGLVQTEMVKEFMAKEDTPED 213
Cdd:cd09761 149 SKGGLVALTHALAMSLGPD-IRVNCISPGWINTTEQQEFTAAPLTQED 195
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 7-218 7.70e-18

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: 80.98  E-value: 7.70e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLggrcVPVVCDSSQESEVKSLFEQVdreqkGRL 86
Cdd:cd05351   7 GKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPGI----EPVCVDLSDWDATEEALGSV-----GPV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  87 DVLVNNA-YAGVQAILNTTNKSFwevpasiwDDINNVGLRGHYLCSVYGARLMVPAG-KGLIVIVSSPGGLQHMFN-VPY 163
Cdd:cd05351  78 DLLVNNAaVAILQPFLEVTKEAF--------DRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNhTVY 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 31980844 164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKefmakeDTPEDPLFKK 218
Cdd:cd05351 150 CSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGR------DNWSDPEKAK 198
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
8-201 9.45e-18

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 80.97  E-value: 9.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRhldTLRATAQEAQSLGG------RCVPV-VCDSSQESEVKSLFEqvdr 80
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYF---SGNDCAKDWFEEYGftedqvRLKELdVTDTEECAEALAEIE---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   81 EQKGRLDVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGlrghyLCSVYG-ARLMVPA----GKGLIVIVSSPGGL 155
Cdd:PRK12824  76 EEEGPVDILVNN--AGI-----TRDSVFKRMSHQEWNDVINTN-----LNSVFNvTQPLFAAmceqGYGRIINISSVNGL 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 31980844  156 QHMFNVP-YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMV 201
Cdd:PRK12824 144 KGQFGQTnYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMV 190
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 6-244 1.31e-17

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: 80.66  E-value: 1.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLG-GRCVPVVCDSSQESEVKSLFEqVDREQKG 84
Cdd:cd08933   8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGpGSCKFVPCDVTKEEDIKTLIS-VTVERFG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNA--YAGVQAILNTTNKSFwevpasiwDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNVP 162
Cdd:cd08933  87 RIDCLVNNAgwHPPHQTTDETSAQEF--------RDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGQKQAAP 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 163 YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDPLFKKMKPD-FSSAESPEMSGKCVVALAT 241
Cdd:cd08933 159 YVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAQTPDTLATIKEGELAQlLGRMGTEAESGLAALFLAA 238


                ...
gi 31980844 242 DPN 244
Cdd:cd08933 239 EAT 241
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 6-242 1.66e-17

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: 80.21  E-value: 1.66e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   6 KGQVCVVTGASRGIGRGIALQLCKAGATVyitgrHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDreqkgR 85
Cdd:cd05368   1 DGKVALITAAAQGIGRAIALAFAREGANV-----IATDINEEKLKELERGPGITTRVLDVTDKEQVAALAKEEG-----R 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  86 LDVLVNNA-YAGVQAILNTTNKSfwevpasiWDDINNVGLRGHYLcsVYGARL--MVPAGKGLIVIVSSPGGlqHMFNVP 162
Cdd:cd05368  71 IDVLFNCAgFVHHGSILDCEDDD--------WDFAMNLNVRSMYL--MIKAVLpkMLARKDGSIINMSSVAS--SIKGVP 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 163 ----YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDPL--FKKMKPDFSSAeSPEMSGKCV 236
Cdd:cd05368 139 nrfvYSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERIQAQPDPEEALkaFAARQPLGRLA-TPEEVAALA 217


                ....*.
gi 31980844 237 VALATD 242
Cdd:cd05368 218 VYLASD 223
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 4-219 1.80e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 80.78  E-value: 1.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqsLGG--RCVPVVCDSSQESEVKSLFEQVdRE 81
Cdd:PRK05872   6 SLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAE---LGGddRVLTVVADVTDLAAMQAAAEEA-VE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   82 QKGRLDVLVNNayAGVqailnTTNKSFWEVPASIWD---DINNVGlrghylcSVYGARLMVPA---GKGLIVIVSS---- 151
Cdd:PRK05872  82 RFGGIDVVVAN--AGI-----ASGGSVAQVDPDAFRrviDVNLLG-------VFHTVRATLPAlieRRGYVLQVSSlaaf 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31980844  152 ---PGGlqhmfnVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEfmAKEDtpeDPLFKKM 219
Cdd:PRK05872 148 aaaPGM------AAYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVRD--ADAD---LPAFREL 207
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 5-210 2.15e-17

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: 79.66  E-value: 2.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHldtlRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQKg 84
Cdd:cd05370   3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRR----EERLAEAKKELPNIHTIVLDVGDAESVEALAEALLSEYP- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNayAGVQAILNTTNksfwevPASIWDDIN---NVGLRGhylcSVYGARLMVP----AGKGLIVIVSSPGGLQH 157
Cdd:cd05370  78 NLDILINN--AGIQRPIDLRD------PASDLDKADteiDTNLIG----PIRLIKAFLPhlkkQPEATIVNVSSGLAFVP 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 31980844 158 MFNVP-YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDT 210
Cdd:cd05370 146 MAANPvYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGG 199
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
6-203 2.65e-17

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 79.77  E-value: 2.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGR 85
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQV-VDTFGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   86 LDVLVNNAYAGVQAILNTtnksfweVPASIWDDINNVGLRGhylcSVYGARLMVPAGK-----GLIVIVSSPGGlqHMFN 160
Cdd:PRK08643  80 LNVVVNNAGVAPTTPIET-------ITEEQFDKVYNINVGG----VIWGIQAAQEAFKklghgGKIINATSQAG--VVGN 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 31980844  161 vP----YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKE 203
Cdd:PRK08643 147 -PelavYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPMMFD 192
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 5-199 3.00e-17

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: 79.81  E-value: 3.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDrEQKG 84
Cdd:cd08935   3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIV-AQFG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVN-------NAYAGVQAILNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQH 157
Cdd:cd08935  82 TVDILINgaggnhpDATTDPEHYEPETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSP 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 31980844 158 MFNVP-YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTE 199
Cdd:cd08935 162 LTKVPaYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTP 204
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 11-199 3.45e-17

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: 79.25  E-value: 3.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  11 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQE-AQSLGGRCVPVVCDSSQESEVKSLFEQVDREQKgRLDVL 89
Cdd:cd05346   4 LITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADElGAKFPVKVLPLQLDVSDRESIEAALENLPEEFR-DIDIL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  90 VNNayAGVQAILNttnkSFWEVPASIWD---DINNVGLrghylcsVYGARLMVPA----GKGLIVIVSS-------PGGl 155
Cdd:cd05346  83 VNN--AGLALGLD----PAQEADLEDWEtmiDTNVKGL-------LNVTRLILPImiarNQGHIINLGSiagrypyAGG- 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 31980844 156 qhmfNVpYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTE 199
Cdd:cd05346 149 ----NV-YCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETE 187
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 6-208 3.81e-17

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: 79.25  E-value: 3.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYItgrhLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGR 85
Cdd:cd05371   1 KGLVAVVTGGASGLGLATVERLLAQGAKVVI----LDLPNSPGETVAKLGDNCRFVPVDVTSEKDVKAALALA-KAKFGR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  86 LDVLVNNAYAGVqAILNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMV---P---AGKGLIVIVSSPGGLQ-HM 158
Cdd:cd05371  76 LDIVVNCAGIAV-AAKTYNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGknePdqgGERGVIINTASVAAFEgQI 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 31980844 159 FNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM-------VKEFMAKE 208
Cdd:cd05371 155 GQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLlaglpekVRDFLAKQ 211
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-200 6.86e-17

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 78.61  E-value: 6.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITG-RHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFeQVDREQK 83
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAkKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLA-KATIDRY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   84 GRLDVLVNNAYAGVQAIlnttnksFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKglIVIVSSPGGLQHMFNVP- 162
Cdd:PRK06077  83 GVADILVNNAGLGLFSP-------FLNVDDKLIDKHISTDFKSVIYCSQELAKEMREGGA--IVNIASVAGIRPAYGLSi 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 31980844  163 YGVGKAA----CDRLAADCAHELRRHGVSyvslwPGLVQTEM 200
Cdd:PRK06077 154 YGAMKAAvinlTKYLALELAPKIRVNAIA-----PGFVKTKL 190
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 5-212 6.96e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 78.43  E-value: 6.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:PRK07478   4 LNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALA-VERFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAyAGVQAILNTTnksfwEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGlqHMFNVP-- 162
Cdd:PRK07478  83 GLDIAFNNA-GTLGEMGPVA-----EMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVG--HTAGFPgm 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 31980844  163 --YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMakeDTPE 212
Cdd:PRK07478 155 aaYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMG---DTPE 203
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-209 1.37e-16

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 77.64  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATvyITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGAD--IVGVGVAEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQA-VEVMG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNayAGV---QAILNTTNKSfwevpasiWDDINNVGLRGHYLCSVYGARLMVPAGK-GLIVIVSSPGGLQHMFN 160
Cdd:PRK12481  83 HIDILINN--AGIirrQDLLEFGNKD--------WDDVININQKTVFFLSQAVAKQFVKQGNgGKIINIASMLSFQGGIR 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 31980844  161 VP-YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKED 209
Cdd:PRK12481 153 VPsYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALRADTA 202
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 5-212 1.55e-16

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: 77.43  E-value: 1.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqsLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:cd05345   3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAAD---IGEAAIAIQADVTKRADVEAMVEAA-LSKFG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNayAGVqailNTTNKSFWEVPASIWDDINNVGLRGHYLcsvyGARLMVP----AGKGLIVIVSSPGGLQHMFN 160
Cdd:cd05345  79 RLDILVNN--AGI----THRNKPMLEVDEEEFDRVFAVNVKSIYL----SAQALVPhmeeQGGGVIINIASTAGLRPRPG 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 31980844 161 -VPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAkEDTPE 212
Cdd:cd05345 149 lTWYNASKGWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFMG-EDTPE 200
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 5-242 1.73e-16

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 77.35  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQK 83
Cdd:PRK12935   4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVINyNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEA-VNHF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   84 GRLDVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMF-NVP 162
Cdd:PRK12935  83 GKVDILVNN--AGI-----TRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFgQTN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  163 YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEfmAKEDTPEDPLFKKMKPDFSSAEspEMSgKCVVALATD 242
Cdd:PRK12935 156 YSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAE--VPEEVRQKIVAKIPKKRFGQAD--EIA-KGVVYLCRD 230
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-199 1.81e-16

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 77.47  E-value: 1.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITgRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIIT-THGTNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEA-LEEFG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNayAGV---QAILNTTNKSfwevpasiWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSS----PGGlqh 157
Cdd:PRK06935  91 KIDILVNN--AGTirrAPLLEYKDED--------WNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASmlsfQGG--- 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 31980844  158 MFNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTE 199
Cdd:PRK06935 158 KFVPAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTA 199
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 5-208 2.06e-16

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 77.31  E-value: 2.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALA-LERFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAYAgVQAILNTTNKSFWEVPASIwdDINnvglrghylcsVYGA----RLMVPA---GKGLIVIVSSpGGLQH 157
Cdd:PRK07890  82 RVDALVNNAFR-VPSMKPLADADFAHWRAVI--ELN-----------VLGTlrltQAFTPAlaeSGGSIVMINS-MVLRH 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 31980844  158 MfNVPYG---VGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVK---EFMAKE 208
Cdd:PRK07890 147 S-QPKYGaykMAKGALLAASQSLATELGPQGIRVNSVAPGYIWGDPLKgyfRHQAGK 202
PRK06949 PRK06949
SDR family oxidoreductase;
5-200 2.74e-16

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 77.11  E-value: 2.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQkG 84
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEA-G 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGL--------IVIVSSPGGLQ 156
Cdd:PRK06949  86 TIDILVNN--SGV-----STTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGAgntkpggrIINIASVAGLR 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 31980844  157 HMFNV-PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:PRK06949 159 VLPQIgLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEI 203
PRK05650 PRK05650
SDR family oxidoreductase;
11-204 2.89e-16

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 77.00  E-value: 2.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   11 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSlFEQVDREQKGRLDVLV 90
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTA-LAQACEEKWGGIDVIV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   91 NNayAGVqailnTTNKSFWEVPASIWD---DINNVGLrghylcsVYGARLMVPA----GKGLIVIVSSPGGLQH---MFN 160
Cdd:PRK05650  83 NN--AGV-----ASGGFFEELSLEDWDwqiAINLMGV-------VKGCKAFLPLfkrqKSGRIVNIASMAGLMQgpaMSS 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 31980844  161 vpYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEF 204
Cdd:PRK05650 149 --YNVAKAGVVALSETLLVELADDEIGVHVVCPSFFQTNLLDSF 190
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 5-212 2.98e-16

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 76.85  E-value: 2.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVyiTGRHLDTLRATaqeaqslGGRCVPVVCDSSQESEVKSLFEQVDREQkG 84
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKV--IGFDQAFLTQE-------DYPFATFVLDVSDAAAVAQVCQRLLAET-G 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNayAGVQAILNTTnksfwEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGlqhmfNVP-- 162
Cdd:PRK08220  76 PLDVLVNA--AGILRMGATD-----SLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAA-----HVPri 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 31980844  163 ----YGVGKAACDRLAADCAHELRRHGV--SYVSlwPGLVQTEMVKEFMAKEDTPE 212
Cdd:PRK08220 144 gmaaYGASKAALTSLAKCVGLELAPYGVrcNVVS--PGSTDTDMQRTLWVDEDGEQ 197
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-242 3.21e-16

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 76.75  E-value: 3.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTlraTAQEAQSLGGrcVPVVCDSSQESEVKSLFEQVdR 80
Cdd:PRK06463   1 YSMRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAEN---EAKELREKGV--FTIKCDVGNRDQVKKSKEVV-E 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   81 EQKGRLDVLVNNayAGVQAILnttnkSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGL----- 155
Cdd:PRK06463  75 KEFGRVDVLVNN--AGIMYLM-----PFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgtaae 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  156 QHMFnvpYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTpedplfKKMKPDFSSAESPEMSGK- 234
Cdd:PRK06463 148 GTTF---YAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQEEA------EKLRELFRNKTVLKTTGKp 218

                        250
                 ....*....|...
gi 31980844  235 -----CVVALATD 242
Cdd:PRK06463 219 edianIVLFLASD 231
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 5-225 3.80e-16

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 76.65  E-value: 3.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYI-TGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQK 83
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIhYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNELQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   84 GR-----LDVLVNNAYAGVQAILNTTNKSFWevpasiwDDINNVGLRGHYLCsVYGARLMVPAGKGLIVIVSSPGGLQHM 158
Cdd:PRK12747  82 NRtgstkFDILINNAGIGPGAFIEETTEQFF-------DRMVSVNAKAPFFI-IQQALSRLRDNSRIINISSAATRISLP 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980844  159 FNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAkedtpeDPLFKKMKPDFSS 225
Cdd:PRK12747 154 DFIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLS------DPMMKQYATTISA 214
PRK09072 PRK09072
SDR family oxidoreductase;
6-93 4.29e-16

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 76.52  E-value: 4.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaQSLGGRCVPVVCDSSQESEVKSLFEQVdrEQKGR 85
Cdd:PRK09072   4 KDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAAR-LPYPGRHRWVVADLTSEAGREAVLARA--REMGG 80


                 ....*...
gi 31980844   86 LDVLVNNA 93
Cdd:PRK09072  81 INVLINNA 88
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 1-151 5.44e-16

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 76.30  E-value: 5.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGR-HLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVD 79
Cdd:PRK08936   1 MYSDLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980844   80 REqKGRLDVLVNNayAGVQAILNTTnksfwEVPASIWDDINNVGLRGHYLCSVYGARLMVPAG-KGLIVIVSS 151
Cdd:PRK08936  81 KE-FGTLDVMINN--AGIENAVPSH-----EMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDiKGNIINMSS 145
PRK06182 PRK06182
short chain dehydrogenase; Validated
 5-199 1.12e-15

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 75.38  E-value: 1.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAqeaqSLGGRCVPVvcDSSQESEVKSLFEQVDREQkG 84
Cdd:PRK06182   1 MQKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLA----SLGVHPLSL--DVTDEASIKAAVDTIIAEE-G 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAYAGVQAILNttnksfwEVP---ASIWDDINNVGLrghylcsvygARL-------MVPAGKGLIVIVSSPGG 154
Cdd:PRK06182  74 RIDVLVNNAGYGSYGAIE-------DVPideARRQFEVNLFGA----------ARLtqlvlphMRAQRSGRIINISSMGG 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 31980844  155 LQH-MFNVPYGVGKAACDRLaADCAH-ELRRHGVSYVSLWPGLVQTE 199
Cdd:PRK06182 137 KIYtPLGAWYHATKFALEGF-SDALRlEVAPFGIDVVVIEPGGIKTE 182
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 7-258 1.27e-15

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: 75.58  E-value: 1.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQE--AQSLGGRCVPVVCDSSQESEVKSLFEQVDREQKg 84
Cdd:cd09807   1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEirRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEED- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNayAGVQAILNTTNKSFWEVPASiwddINNVglrGHYLCSVYGARLMVPAGKGLIVIVSSpggLQHM------ 158
Cdd:cd09807  80 RLDVLINN--AGVMRCPYSKTEDGFEMQFG----VNHL---GHFLLTNLLLDLLKKSAPSRIVNVSS---LAHKagkinf 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 159 ----FNVPYGVGKAAC-DRLA-----ADCAHELRRHGVSYVSLWPGLVQTEMVKeFMAKEDTPEDPLFKKMKPDFssAES 228
Cdd:cd09807 148 ddlnSEKSYNTGFAYCqSKLAnvlftRELARRLQGTGVTVNALHPGVVRTELGR-HTGIHHLFLSTLLNPLFWPF--VKT 224

                       250       260       270
                ....*....|....*....|....*....|
gi 31980844 229 PEMSGKCVVALATDPNILNLSGKVLPSCDL 258
Cdd:cd09807 225 PREGAQTSIYLALAEELEGVSGKYFSDCKL 254
PRK07856 PRK07856
SDR family oxidoreductase;
6-199 1.57e-15

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 74.58  E-value: 1.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRhldtlrataQEAQSLGGRCVPVV-CDSSQESEVKSLFEQVdREQKG 84
Cdd:PRK07856   5 TGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGR---------RAPETVDGRPAEFHaADVRDPDQVAALVDAI-VERHG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAYAGVQAILNTTNKSFWEvpasiwdDINNVGLRGHYLCSVYGARLMVP-AGKGLIVIVSS-------PGglq 156
Cdd:PRK07856  75 RLDVLVNNAGGSPYALAAEASPRFHE-------KIVELNLLAPLLVAQAANAVMQQqPGGGSIVNIGSvsgrrpsPG--- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 31980844  157 hmfNVPYGVGKAACDRLAADCAHELRRHgVSYVSLWPGLVQTE 199
Cdd:PRK07856 145 ---TAAYGAAKAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTE 183
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 7-96 1.88e-15

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 74.71  E-value: 1.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDrEQKGRL 86
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQID-EKFGRI 79

                         90
                 ....*....|
gi 31980844   87 DVLVNNAyAG 96
Cdd:PRK07677  80 DALINNA-AG 88
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
5-207 2.65e-15

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 74.29  E-value: 2.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqsLGGRCVPVVCDSSQESEVKSLFEQVDrEQKG 84
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALE---IGPAAIAVSLDVTRQDSIDRIVAAAV-ERFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAYA-GVQAILNTTNKSFwevpasiwDDINNVGLRGHYLCSVYGARLMVPAGKG--LIVIVSSPGGLQHMFNV 161
Cdd:PRK07067  80 GIDILFNNAALfDMAPILDISRDSY--------DRLFAVNVKGLFFLMQAVARHMVEQGRGgkIINMASQAGRRGEALVS 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 31980844  162 PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM---VKEFMAK 207
Cdd:PRK07067 152 HYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMwdqVDALFAR 200
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 5-200 3.37e-15

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: 73.81  E-value: 3.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqsLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAE---IGPAACAISLDVTDQASIDRCVAAL-VDRWG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNAYA-GVQAILNTTNKSFwevpasiwDDINNVGLRGHYLCSVYGARLMVPAGKG--LIVIVSSPGGLQHMFNV 161
Cdd:cd05363  77 SIDILVNNAALfDLAPIVDITRESY--------DRLFAINVSGTLFMMQAVARAMIAQGRGgkIINMASQAGRRGEALVG 148

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 31980844 162 PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:cd05363 149 VYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEH 187
PRK06398 PRK06398
aldose dehydrogenase; Validated
 5-214 3.95e-15

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 73.71  E-value: 3.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQeaqslggrcvpVVCDSSQESEVKSLFEQVDReQKG 84
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYNDVDY-----------FKVDVSNKEQVIKGIDYVIS-KYG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNA----YAGVQAIlnttnksfwevPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFN 160
Cdd:PRK06398  72 RIDILVNNAgiesYGAIHAV-----------EEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRN 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 31980844  161 V-PYGVGKAA----CDRLAADCAHELRRHGVSyvslwPGLVQTEMVkEFMAKEDTPEDP 214
Cdd:PRK06398 141 AaAYVTSKHAvlglTRSIAVDYAPTIRCVAVC-----PGSIRTPLL-EWAAELEVGKDP 193
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 5-213 5.10e-15

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: 72.99  E-value: 5.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGR---CVPVVCDSSQESEVKSLFEQVDRE 81
Cdd:cd05340   2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRqpqWFILDLLTCTSENCQQLAQRIAVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  82 QkGRLDVLVNNAyagvqAILNTTNkSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNV 161
Cdd:cd05340  82 Y-PRLDGVLHNA-----GLLGDVC-PLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANW 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 31980844 162 -PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKED-----TPED 213
Cdd:cd05340 155 gAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAFPTEDpqklkTPAD 212
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-209 9.34e-15

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 72.60  E-value: 9.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATvyITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQkG 84
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCD--IVGINIVEPTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEF-G 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNayAGVqaILNTTNKSFWEvpaSIWDDINNVGLRGHYLCSVYGARLMVPAGK-GLIVIVSSPGGLQHMFNVP- 162
Cdd:PRK08993  85 HIDILVNN--AGL--IRREDAIEFSE---KDWDDVMNLNIKSVFFMSQAAAKHFIAQGNgGKIINIASMLSFQGGIRVPs 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 31980844  163 YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKED 209
Cdd:PRK08993 158 YTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQ 204
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 5-242 2.06e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 71.72  E-value: 2.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSlfeQVDR--EQ 82
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRA---AIDAfeAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   83 KGRLDVLVNNAYAGVQAILNttnksfwEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIV-IVSSPGGLQHMFNV 161
Cdd:PRK07523  85 IGPIDILVNNAGMQFRTPLE-------DFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIInIASVQSALARPGIA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  162 PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAkedtpeDPLF----KKMKPDFSSAESPEMSGKCVV 237
Cdd:PRK07523 158 PYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAALVA------DPEFsawlEKRTPAGRWGKVEELVGACVF 231


                 ....*
gi 31980844  238 aLATD 242
Cdd:PRK07523 232 -LASD 235
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 7-185 3.17e-14

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 73.03  E-value: 3.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQE--AQSLGGRCVPVVCDSSQESEVKSLFEQVDREQKG 84
Cdd:COG3347 425 GRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAElgGGYGADAVDATDVDVTAEAAVAAAFGFAGLDIGG 504

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNAYAGVqailnttnKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKG-LIVIVSSPGGLqhmfNVPY 163
Cdd:COG3347 505 SDIGVANAGIASS--------SPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGLGgSSVFAVSKNAA----AAAY 572

                       170       180
                ....*....|....*....|..
gi 31980844 164 GVGKAACDRLAAdcAHELRRHG 185
Cdd:COG3347 573 GAAAAATAKAAA--QHLLRALA 592
PRK09134 PRK09134
SDR family oxidoreductase;
12-93 3.70e-14

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 71.11  E-value: 3.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   12 VTGASRGIGRGIALQLCKAGATVYI-TGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRLDVLV 90
Cdd:PRK09134  14 VTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALAAEIRALGRRAVALQADLADEAEVRALVARA-SAALGPITLLV 92


                 ...
gi 31980844   91 NNA 93
Cdd:PRK09134  93 NNA 95
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 6-213 3.97e-14

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: 70.96  E-value: 3.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQS-LGGRCVPVVCDSSQESEVKSLFEQVDREQKg 84
Cdd:cd05322   1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAeYGEKAYGFGADATNEQSVIALSKGVDEIFK- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNAYAGVQAILNttnkSFwevPASIWDDINNVGLRGHYLCSVYGARLMVPAG-KGLIV-IVSSPGGLQHMFNVP 162
Cdd:cd05322  80 RVDLLVYSAGIAKSAKIT----DF---ELGDFDRSLQVNLVGYFLCAREFSKLMIRDGiQGRIIqINSKSGKVGSKHNSG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 31980844 163 YGVGKAACDRLAADCAHELRRHGVSYVSLWPG-LVQTEM----VKEFMAKEDTPED 213
Cdd:cd05322 153 YSAAKFGGVGLTQSLALDLAEHGITVNSLMLGnLLKSPMfqslLPQYAKKLGIKES 208
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 8-199 4.27e-14

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: 70.56  E-value: 4.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   8 QVCVVTGASRGIGRGIALQLCKAGATVyITGRHLDTLRATAQeAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRLD 87
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARV-VVNYYRSTESAEAV-AAEAGERAIAIQADVRDRDQVQAMIEEA-KNHFGPVD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  88 VLVNNAYAGvQAILNTTNKSFWEVPasiWDDINN---VGLRGHYLCSVYGARLMVPAGKGLIVIVSSpgGLQHMFNVPYG 164
Cdd:cd05349  78 TIVNNALID-FPFDPDQRKTFDTID---WEDYQQqleGAVKGALNLLQAVLPDFKERGSGRVINIGT--NLFQNPVVPYH 151

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 31980844 165 ---VGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTE 199
Cdd:cd05349 152 dytTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVT 189
PRK07831 PRK07831
SDR family oxidoreductase;
5-147 7.53e-14

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 70.06  E-value: 7.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGAS-RGIGRGIALQLCKAGATVYITGRHLDTLRATAQE--AQSLGGRCVPVVCDSSQESEVKSLFEQVDrE 81
Cdd:PRK07831  15 LAGKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADElaAELGLGRVEAVVCDVTSEAQVDALIDAAV-E 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31980844   82 QKGRLDVLVNNAYAGVQA-ILNTTNKSfwevpasiWDDINNVGLRGHYLCSVYGARLMVPAG-KGLIV 147
Cdd:PRK07831  94 RLGRLDVLVNNAGLGGQTpVVDMTDDE--------WSRVLDVTLTGTFRATRAALRYMRARGhGGVIV 153
PRK05866 PRK05866
SDR family oxidoreductase;
3-202 7.69e-14

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 70.54  E-value: 7.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDrEQ 82
Cdd:PRK05866  36 VDLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVE-KR 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   83 KGRLDVLVNNAyagVQAILNTTNKSFwevpaSIWDDINNVGLRGHY--LCSVYG-ARLMVPAGKGLIVIVSS---PGGLQ 156
Cdd:PRK05866 115 IGGVDILINNA---GRSIRRPLAESL-----DRWHDVERTMVLNYYapLRLIRGlAPGMLERGDGHIINVATwgvLSEAS 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 31980844  157 HMFNVpYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVK 202
Cdd:PRK05866 187 PLFSV-YNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPMIA 231
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 5-209 9.20e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 70.09  E-value: 9.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQkG 84
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEV-G 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAyagvqAILNTTnkSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIV-IVSSPGGLQHMFNVPY 163
Cdd:PRK07097  87 VIDILVNNA-----GIIKRI--PMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIInICSMMSELGRETVSAY 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 31980844  164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLV---QTEMVKEFMAKED 209
Cdd:PRK07097 160 AAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIatpQTAPLRELQADGS 208
PRK08219 PRK08219
SDR family oxidoreductase;
9-214 1.02e-13

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 69.19  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    9 VCVVTGASRGIGRGIALQLCKAgATVYITGRHLDTLRATAQEAQSLggrcVPVVCDSSQESEVKSLFEQVDreqkgRLDV 88
Cdd:PRK08219   5 TALITGASRGIGAAIARELAPT-HTLLLGGRPAERLDELAAELPGA----TPFPVDLTDPEAIAAAVEQLG-----RLDV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   89 LVNNayAGVqailnTTNKSFWEVPASIWddinnvglRGHYLCSVYGA----RLMVP---AGKGLIVIVSSPGGLQ-HMFN 160
Cdd:PRK08219  75 LVHN--AGV-----ADLGPVAESTVDEW--------RATLEVNVVAPaeltRLLLPalrAAHGHVVFINSGAGLRaNPGW 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 31980844  161 VPYGVGK----AACDRLAADCAHELRrhgVSyvSLWPGLVQTEMVKEFMAKEDTPEDP 214
Cdd:PRK08219 140 GSYAASKfalrALADALREEEPGNVR---VT--SVHPGRTDTDMQRGLVAQEGGEYDP 192
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-213 1.08e-13

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 69.43  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASR--GIGRGIALQLCKAGATVYIT-----------GRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEV 71
Cdd:PRK12859   4 LKNKVAVVTGVSRldGIGAAICKELAEAGADIFFTywtaydkempwGVDQDEQIQLQEELLKNGVKVSSMELDLTQNDAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   72 KSLFEQVdREQKGRLDVLVNNAyagvqaiLNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSS 151
Cdd:PRK12859  84 KELLNKV-TEQLGYPHILVNNA-------AYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTS 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980844  152 PGGLQHM-FNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQT----EMVKEF------MAKEDTPED 213
Cdd:PRK12859 156 GQFQGPMvGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTgwmtEEIKQGllpmfpFGRIGEPKD 228
PRK09291 PRK09291
SDR family oxidoreductase;
12-198 1.42e-13

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 69.26  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   12 VTGASRGIGRGIALQLCKAG----ATVYITGRhLDTLRATAQEaqslggrcvpvvCDSSQESEVKSLFEQVDREQKGRL- 86
Cdd:PRK09291   7 ITGAGSGFGREVALRLARKGhnviAGVQIAPQ-VTALRAEAAR------------RGLALRVEKLDLTDAIDRAQAAEWd 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   87 -DVLVNNAYAGvqailntTNKSFWEVPASIwddinnvgLRGHYLCSVYG--------ARLMVPAGKGLIVIVSSPGGLqh 157
Cdd:PRK09291  74 vDVLLNNAGIG-------EAGAVVDIPVEL--------VRELFETNVFGpleltqgfVRKMVARGKGKVVFTSSMAGL-- 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 31980844  158 mFNVP----YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQT 198
Cdd:PRK09291 137 -ITGPftgaYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLT 180
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 5-216 1.43e-13

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 69.13  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVV-CD--SSQESEVKSLFEQVDrE 81
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIpLDllTATPQNYQQLADTIE-E 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   82 QKGRLDVLVNNAyagvqAILNTTNkSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQ-HMFN 160
Cdd:PRK08945  89 QFGRLDGVLHNA-----GLLGELG-PMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQgRANW 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31980844  161 VPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM-VKEFMAkED-----TPED--PLF 216
Cdd:PRK08945 163 GAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAMrASAFPG-EDpqklkTPEDimPLY 225
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 12-222 1.56e-13

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: 68.63  E-value: 1.56e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  12 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAqeAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQKGRLDVLVN 91
Cdd:cd08931   5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALA--AELGAENVVAGALDVTDRAAWAAALADFAAATGGRLDALFN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  92 NAYAGvqailntTNKSFWEVPASIWDDINNVGLRGhylcSVYGARLMVPAGK----GLIVIVSSPGGLQHMFN-VPYGVG 166
Cdd:cd08931  83 NAGVG-------RGGPFEDVPLAAHDRMVDINVKG----VLNGAYAALPYLKatpgARVINTASSSAIYGQPDlAVYSAT 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 31980844 167 KAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDtPEDPLFKKMKPD 222
Cdd:cd08931 152 KFAVRGLTEALDVEWARHGIRVADVWPWFVDTPILTKGETGAA-PKKGLGRVLPVS 206
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 7-203 1.56e-13

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. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 69.27  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844     7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGR-----HLDTLRATAQE----AQSLGGRCVPVVCDSSQESEVKSLFEQ 77
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVDLcaddpAVGYPLATRAEldavAAACPDQVLPVIADVRDPAALAAAVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    78 VdREQKGRLDVLVnnAYAGVQAilntTNKSFWEVPASIWDDINNVGLRGhylcsVYG-ARLMVPA-------GKGLIVIV 149
Cdd:TIGR04504  81 A-VERWGRLDAAV--AAAGVIA----GGRPLWETTDAELDLLLDVNLRG-----VWNlARAAVPAmlarpdpRGGRFVAV 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 31980844   150 SSPGGLQHMFNVP-YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKE 203
Cdd:TIGR04504 149 ASAAATRGLPHLAaYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLAA 203
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 12-222 1.72e-13

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: 68.65  E-value: 1.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  12 VTGASRGIGRGIALQLCKAGATVYitgrhldtlrATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDR--EQKGRLDVL 89
Cdd:cd05331   3 VTGAAQGIGRAVARHLLQAGATVI----------ALDLPFVLLLEYGDPLRLTPLDVADAAAVREVCSRllAEHGPIDAL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  90 VNnaYAGVQAILNTTnksfwEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGlqhmfNVP------Y 163
Cdd:cd05331  73 VN--CAGVLRPGATD-----PLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAA-----HVPrismaaY 140

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31980844 164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKED--------TPED-----PLFKKMKPD 222
Cdd:cd05331 141 GASKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAMQRTLWHDEDgaaqviagVPEQfrlgiPLGKIAQPA 212
PLN02253 PLN02253
xanthoxin dehydrogenase
 7-215 1.75e-13

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 69.47  E-value: 1.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDtlrATAQEAQSLGGR--CVPVVCDSSQESEVKslfEQVD--REQ 82
Cdd:PLN02253  18 GKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDD---LGQNVCDSLGGEpnVCFFHCDVTVEDDVS---RAVDftVDK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   83 KGRLDVLVNNAYAGVQAILNTTNKSFWEVPASIwdDINnvgLRGHYLCSVYGARLMVPAGKGLIV----IVSSPGGL-QH 157
Cdd:PLN02253  92 FGTLDIMVNNAGLTGPPCPDIRNVELSEFEKVF--DVN---VKGVFLGMKHAARIMIPLKKGSIVslcsVASAIGGLgPH 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 31980844  158 mfnvPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDPL 215
Cdd:PLN02253 167 ----AYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAHLPEDERTEDAL 220
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 4-198 2.02e-13

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: 68.72  E-value: 2.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQK 83
Cdd:cd08936   7 PLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATA-VNLH 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  84 GRLDVLVNNAyagvqailntTNKSFW----EVPASIWDDINNVGLRGHYLCSvygaRLMVPA----GKGLIVIVSSPGGL 155
Cdd:cd08936  86 GGVDILVSNA----------AVNPFFgnilDSTEEVWDKILDVNVKATALMT----KAVVPEmekrGGGSVVIVSSVAAF 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 31980844 156 QHMFNV-PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQT 198
Cdd:cd08936 152 HPFPGLgPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKT 195
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
11-252 2.22e-13

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 68.56  E-value: 2.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   11 VVTGASRGIGRGIALQLCKAGATVY-ITGRHLDTLRATAQEAqslGGRCVPVVCDSSQESEVKSLFEQVDR--EQKGRLD 87
Cdd:PRK06924   5 IITGTSQGLGEAIANQLLEKGTHVIsISRTENKELTKLAEQY---NSNLTFHSLDLQDVHELETNFNEILSsiQEDNVSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   88 V-LVNNAyagvqAILNttnksfwevPASIWDDINNVGLRGHY---------LCSVYGARLMVPAGKGLIVIVSSPGGLQH 157
Cdd:PRK06924  82 IhLINNA-----GMVA---------PIKPIEKAESEELITNVhlnllapmiLTSTFMKHTKDWKVDKRVINISSGAAKNP 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  158 MFN-VPYGVGKAACDrLAADCAH---ELRRHGVSYVSLWPGLVQTEMVKEF--MAKEDTPEDPLFKKMKpDFSSAESPEM 231
Cdd:PRK06924 148 YFGwSAYCSSKAGLD-MFTQTVAteqEEEEYPVKIVAFSPGVMDTNMQAQIrsSSKEDFTNLDRFITLK-EEGKLLSPEY 225

                        250       260
                 ....*....|....*....|.
gi 31980844  232 SGKCVVALATDPNILNlsGKV 252
Cdd:PRK06924 226 VAKALRNLLETEDFPN--GEV 244
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 3-93 8.67e-13

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 66.96  E-value: 8.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDtlrATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQ 82
Cdd:PRK08265   2 IGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDAD---NGAAVAASLGERARFIATDITDDAAIERAVATV-VAR 77

                         90
                 ....*....|.
gi 31980844   83 KGRLDVLVNNA 93
Cdd:PRK08265  78 FGRVDILVNLA 88
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 12-198 9.10e-13

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: 66.01  E-value: 9.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  12 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGgrcvpVVCDSSQESEVKSLFEQVdreqkGRLDVLVn 91
Cdd:cd11730   3 ILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALA-----RPADVAAELEVWALAQEL-----GPLDLLV- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  92 naYAgVQAILnttNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVivsspGGLQHMFNVP----YGVGK 167
Cdd:cd11730  72 --YA-AGAIL---GKPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFL-----GAYPELVMLPglsaYAAAK 140

                       170       180       190
                ....*....|....*....|....*....|.
gi 31980844 168 AACDRLAADCAHELRrhGVSYVSLWPGLVQT 198
Cdd:cd11730 141 AALEAYVEVARKEVR--GLRLTLVRPPAVDT 169
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 5-93 9.18e-13

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: 66.93  E-value: 9.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYIT--GRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQ 82
Cdd:cd05355  24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINylPEEEDDAEETKKLIEEEGRKCLLIPGDLGDESFCRDLVKEV-VKE 102

                        90
                ....*....|.
gi 31980844  83 KGRLDVLVNNA 93
Cdd:cd05355 103 FGKLDILVNNA 113
PRK07062 PRK07062
SDR family oxidoreductase;
1-213 1.59e-12

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 66.22  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQE--AQSLGGRCVPVVCDSSQESEVKSLFEQV 78
Cdd:PRK07062   2 MQIQLEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARlrEKFPGARLLAARCDVLDEADVAAFAAAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   79 drEQK-GRLDVLVNNAYAGVQAILNTTNKSFW--EVPASIWDDINNVglrghylcsvygaRLMVPA----GKGLIVIVSS 151
Cdd:PRK07062  82 --EARfGGVDMLVNNAGQGRVSTFADTTDDAWrdELELKYFSVINPT-------------RAFLPLlrasAAASIVCVNS 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31980844  152 PGGLQ---HMfnVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQT-EMVKEFMAKEDTPED 213
Cdd:PRK07062 147 LLALQpepHM--VATSAARAGLLNLVKSLATELAPKGVRVNSILLGLVESgQWRRRYEARADPGQS 210
PRK08267 PRK08267
SDR family oxidoreductase;
12-211 1.96e-12

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 66.11  E-value: 1.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   12 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqsLG-GRCVPVVCDSSQESEVKSLFEQVDREQKGRLDVLV 90
Cdd:PRK08267   6 ITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAE---LGaGNAWTGALDVTDRAAWDAALADFAAATGGRLDVLF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   91 NNA---YAGvqailnttnkSFWEVPASIWD---DINNVGLrghylcsVYGARLMVPAGKGlivivsSPGGlqHMFNVP-- 162
Cdd:PRK08267  83 NNAgilRGG----------PFEDIPLEAHDrviDINVKGV-------LNGAHAALPYLKA------TPGA--RVINTSsa 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980844  163 ---YGVGkaacdRLAADCAH-------------ELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTP 211
Cdd:PRK08267 138 saiYGQP-----GLAVYSATkfavrgltealdlEWRRHGIRVADVMPLFVDTAMLDGTSNEVDAG 197
PRK05693 PRK05693
SDR family oxidoreductase;
9-215 2.05e-12

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 66.35  E-value: 2.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    9 VCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSlggrcvPVVCDSSQESEVKSLFEQVDrEQKGRLDV 88
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAAAGFT------AVQLDVNDGAALARLAEELE-AEHGGLDV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   89 LVNNA-YAGVQAILnttnksfwevpasiwdDINNVGLRGHYLCSVYG----ARLMVPA---GKGLIVIVSSPGG-LQHMF 159
Cdd:PRK05693  76 LINNAgYGAMGPLL----------------DGGVEAMRRQFETNVFAvvgvTRALFPLlrrSRGLVVNIGSVSGvLVTPF 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31980844  160 NVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVK------EFMAKEDTPEDPL 215
Cdd:PRK05693 140 AGAYCASKAAVHALSDALRLELAPFGVQVMEVQPGAIASQFASnasreaEQLLAEQSPWWPL 201
PRK06139 PRK06139
SDR family oxidoreductase;
1-154 2.53e-12

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 66.28  E-value: 2.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdR 80
Cdd:PRK06139   1 MMGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQA-A 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31980844   81 EQKGRLDVLVNNayAGVQAILNttnksFWEVPASIWDDINNVGLRGHylcsVYGARLMVP----AGKGLIVIVSSPGG 154
Cdd:PRK06139  80 SFGGRIDVWVNN--VGVGAVGR-----FEETPIEAHEQVIQTNLIGY----MRDAHAALPifkkQGHGIFINMISLGG 146
PRK06194 PRK06194
hypothetical protein; Provisional
 6-169 4.88e-12

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 65.04  E-value: 4.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGR 85
Cdd:PRK06194   5 AGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAA-LERFGA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   86 LDVLVNNAYAGVQAILnttnksfWEVPASIWDDINNVGLRGhylcSVYGARLMVP----------AGKGLIVIVSSPGGL 155
Cdd:PRK06194  84 VHLLFNNAGVGAGGLV-------WENSLADWEWVLGVNLWG----VIHGVRAFTPlmlaaaekdpAYEGHIVNTASMAGL 152

                        170
                 ....*....|....*...
gi 31980844  156 qhmFNVP----YGVGKAA 169
Cdd:PRK06194 153 ---LAPPamgiYNVSKHA 167
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-237 5.09e-12

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 64.73  E-value: 5.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTlrATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQKGRLD 87
Cdd:PRK08642   6 QTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSED--AAEALADELGDRAIALQADVTDREQVQAMFATATEHFGKPIT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   88 VLVNNAYAGVQaiLNTTNKSFWEVPAsiWDDINNvGLRGhylcSVYGARL--------MVPAGKGLIVIVSSpgglqHMF 159
Cdd:PRK08642  84 TVVNNALADFS--FDGDARKKADDIT--WEDFQQ-QLEG----SVKGALNtiqaalpgMREQGFGRIINIGT-----NLF 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  160 NVP------YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQT--------EMVKEFMA------KEDTPEDplFKKM 219
Cdd:PRK08642 150 QNPvvpyhdYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTtdasaatpDEVFDLIAattplrKVTTPQE--FADA 227

                        250
                 ....*....|....*...
gi 31980844  220 KPDFSSAESPEMSGKCVV 237
Cdd:PRK08642 228 VLFFASPWARAVTGQNLV 245
PRK08628 PRK08628
SDR family oxidoreductase;
5-215 9.77e-12

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 63.82  E-value: 9.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHlDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDrEQKG 84
Cdd:PRK08628   5 LKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRS-APDDEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTV-AKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAYAGVQAILNTTNKSFwevPASIwdDINNVglrgHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNVP-Y 163
Cdd:PRK08628  83 RIDGLVNNAGVNDGVGLEAGREAF---VASL--ERNLI----HYYVMAHYCLPHLKASRGAIVNISSKTALTGQGGTSgY 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 31980844  164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDPL 215
Cdd:PRK08628 154 AAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMTPLYENWIATFDDPEAKL 205
PRK06500 PRK06500
SDR family oxidoreductase;
5-198 1.16e-11

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 63.44  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqsLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAE---LGESALVIRADAGDVAAQKALAQAL-AEAFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHYLcsVYGARLMVPAGKGLIVIVSSPGGLQHMFNVP-Y 163
Cdd:PRK06500  80 RLDAVFIN--AGV-----AKFAPLEDWDEAMFDRSFNTNVKGPYF--LIQALLPLLANPASIVLNGSINAHIGMPNSSvY 150

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 31980844  164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQT 198
Cdd:PRK06500 151 AASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQT 185
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-200 1.80e-11

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 64.47  E-value: 1.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYI-----TGRHLDTLrataqeAQSLGGRCVPvvCDSSQESEVKSLFEQV 78
Cdd:PRK08261 207 PLAGKVALVTGAARGIGAAIAEVLARDGAHVVCldvpaAGEALAAV------ANRVGGTALA--LDITAPDAPARIAEHL 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   79 dREQKGRLDVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRG-----HYLcsvYGARLMVPAGKglIVIVSSPG 153
Cdd:PRK08261 279 -AERHGGLDIVVHN--AGI-----TRDKTLANMDEARWDSVLAVNLLAplritEAL---LAAGALGDGGR--IVGVSSIS 345

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 31980844  154 GL-----QHmfNvpYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:PRK08261 346 GIagnrgQT--N--YAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQM 393
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-214 2.54e-11

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 62.78  E-value: 2.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    4 PMKGQVCVVTGASR--GIGRGIALQLCKAGATVYIT-----------GRHLDTLRATAQEAQSLGGRCVPVVCDSSQESE 70
Cdd:PRK12748   2 PLMKKIALVTGASRlnGIGAAVCRRLAAKGIDIFFTywspydktmpwGMHDKEPVLLKEEIESYGVRCEHMEIDLSQPYA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   71 VKSLFEQVdREQKGRLDVLVNNAyagvqaiLNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVS 150
Cdd:PRK12748  82 PNRVFYAV-SERLGDPSILINNA-------AYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLT 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980844  151 SPGGLQHMFN-VPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQT---------EMVKEF-MAKEDTPEDP 214
Cdd:PRK12748 154 SGQSLGPMPDeLAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTgwiteelkhHLVPKFpQGRVGEPVDA 228
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 5-194 2.84e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 63.01  E-value: 2.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAqslGGRCVPVVCDSSQESEVKSLFEQVDREQkG 84
Cdd:PRK06180   2 SSMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALH---PDRALARLLDVTDFDAIDAVVADAEATF-G 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAYAGVQAILNTTNKSfwEVPASIwdDINnvglrghylcsVYGARLMVPA--------GKGLIVIVSSPGGLQ 156
Cdd:PRK06180  78 PIDVLVNNAGYGHEGAIEESPLA--EMRRQF--EVN-----------VFGAVAMTKAvlpgmrarRRGHIVNITSMGGLI 142

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 31980844  157 HMFNVPYGVG-KAACDRLAADCAHELRRHGVSYVSLWPG 194
Cdd:PRK06180 143 TMPGIGYYCGsKFALEGISESLAKEVAPFGIHVTAVEPG 181
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 5-244 3.30e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 62.75  E-value: 3.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLratAQEAQSLGGRCVPVVCDSSQESEVkslFEQVDR--EQ 82
Cdd:PRK08263   1 MMEKVWFITGASRGFGRAWTEAALERGDRVVATARDTATL---ADLAEKYGDRLLPLALDVTDRAAV---FAAVETavEH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   83 KGRLDVLVNNA-YAGVQAILNTTNKSfwevpasiwddinnvgLRGHYLCSVYGARLMVPA--------GKGLIVIVSSPG 153
Cdd:PRK08263  75 FGRLDIVVNNAgYGLFGMIEEVTESE----------------ARAQIDTNFFGALWVTQAvlpylreqRSGHIIQISSIG 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  154 GLQHMFNVP-YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFM--AKEDTPEDPLFKKM---KPDFSSAE 227
Cdd:PRK08263 139 GISAFPMSGiYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWAGTSAkrATPLDAYDTLREELaeqWSERSVDG 218

                        250
                 ....*....|....*..
gi 31980844  228 SPEMSGKCVVALATDPN 244
Cdd:PRK08263 219 DPEAAAEALLKLVDAEN 235
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 5-208 3.45e-11

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 62.24  E-value: 3.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqsLGGRCVPVVCDSSQESEVKSLFEQVDREQKG 84
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAE---LGERVKIFPANLSDRDEVKALGQKAEADLEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 rLDVLVNNayAGVqailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQ-HMFNVPY 163
Cdd:PRK12936  81 -VDILVNN--AGI-----TKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTgNPGQANY 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 31980844  164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKE 208
Cdd:PRK12936 153 CASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQ 197
PRK07806 PRK07806
SDR family oxidoreductase;
7-99 4.16e-11

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 62.04  E-value: 4.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHlDTLRAT--AQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:PRK07806   6 GKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQ-KAPRANkvVAEIEAAGGRASAVGADLTDEESVAALMDTA-REEFG 83

                         90
                 ....*....|....*
gi 31980844   85 RLDVLVNNAYAGVQA 99
Cdd:PRK07806  84 GLDALVLNASGGMES 98
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 5-93 5.55e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 61.97  E-value: 5.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITgrHLDT---LRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDRE 81
Cdd:PRK06701  44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIV--YLDEhedANETKQRVEKEGVKCLLIPGDVSDEAFCKDAVEETVRE 121

                         90
                 ....*....|..
gi 31980844   82 QkGRLDVLVNNA 93
Cdd:PRK06701 122 L-GRLDILVNNA 132
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 5-208 9.70e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 61.21  E-value: 9.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPV-VCDSSQESEVKSLFEQVdreqk 83
Cdd:PRK06125   5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVDVAVhALDLSSPEAREQLAAEA----- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   84 GRLDVLVNNAYAgvqailnttnksfweVPASIWDDINNVGLRGHYLCSVYG----ARLMVPA----GKGLIVIVSSPGGL 155
Cdd:PRK06125  80 GDIDILVNNAGA---------------IPGGGLDDVDDAAWRAGWELKVFGyidlTRLAYPRmkarGSGVIVNVIGAAGE 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 31980844  156 QHMFNvpYGVGKAACDRLAA-DCA--HELRRHGVSYVSLWPGLVQTEMVKEFMAKE 208
Cdd:PRK06125 145 NPDAD--YICGSAGNAALMAfTRAlgGKSLDDGVRVVGVNPGPVATDRMLTLLKGR 198
PRK08703 PRK08703
SDR family oxidoreductase;
4-236 1.85e-10

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 59.95  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    4 PMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGG---RCVPVVCDSSQESEVKSLFEQVDR 80
Cdd:PRK08703   3 TLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHpepFAIRFDLMSAEEKEFEQFAATIAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   81 EQKGRLDVLVNNAyAGVQAILNTTNKSFWEvpasiWDD---INNVGLRGHylcsvygARLMVP----AGKGLIVIVSSPG 153
Cdd:PRK08703  83 ATQGKLDGIVHCA-GYFYALSPLDFQTVAE-----WVNqyrINTVAPMGL-------TRALFPllkqSPDASVIFVGESH 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  154 GLQhmfNVPY----GVGKAACDRLAADCAHELRRHGVSYVS-LWPGLVQTEMVKEFMAKEDTPEDPLFKKMKPDF---SS 225
Cdd:PRK08703 150 GET---PKAYwggfGASKAALNYLCKVAADEWERFGNLRANvLVPGPINSPQRIKSHPGEAKSERKSYGDVLPAFvwwAS 226

                        250
                 ....*....|.
gi 31980844  226 AESPEMSGKCV 236
Cdd:PRK08703 227 AESKGRSGEIV 237
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
5-202 1.98e-10

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 60.03  E-value: 1.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVyITGRHLDTLRATA--QEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQ 82
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKV-VAGCGPNSPRRVKwlEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   83 kGRLDVLVNNAyaGVqailnTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMF-NV 161
Cdd:PRK12938  80 -GEIDVLVNNA--GI-----TRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFgQT 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 31980844  162 PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVK 202
Cdd:PRK12938 152 NYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVK 192
PRK06196 PRK06196
oxidoreductase; Provisional
 5-275 2.28e-10

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 60.47  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQslggRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGID----GVEVVMLDLADLESVRAFAERF-LDSGR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNayAGVQAILNTTNKSFWEVPASiwddINNVglrGHYLCSVYGARLMVPAGKGLIVIVSSPGglQHM------ 158
Cdd:PRK06196  99 RIDILINN--AGVMACPETRVGDGWEAQFA----TNHL---GHFALVNLLWPALAAGAGARVVALSSAG--HRRspirwd 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  159 ---FNVP------YGVGKAA-------CDRLAADcahelrrHGVSYVSLWPGLVQT---------EMV-KEFMAKEDTPE 212
Cdd:PRK06196 168 dphFTRGydkwlaYGQSKTAnalfavhLDKLGKD-------QGVRAFSVHPGGILTplqrhlpreEQVaLGWVDEHGNPI 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980844  213 DPLFKkmkpdfssaeSPEMSGKCVVALATDPNILNLSGKVLPSCDLARRYGlKDIDGRPVKDY 275
Cdd:PRK06196 241 DPGFK----------TPAQGAATQVWAATSPQLAGMGGLYCEDCDIAEPTP-KDAPWSGVRPH 292
PRK12742 PRK12742
SDR family oxidoreductase;
3-200 2.80e-10

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 59.39  E-value: 2.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITgrHLDTLRATAQEAQSLGGRCVPVvcDSSQESEVKSLFeqvdrEQ 82
Cdd:PRK12742   2 GAFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFT--YAGSKDAAERLAQETGATAVQT--DSADRDAVIDVV-----RK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   83 KGRLDVLVNNAYAGVQAILNTTNKsfwevpasiwDDIN---NVGLRGHYLCSVYGARLMVPAGKglIVIVSSPGGLQHMF 159
Cdd:PRK12742  73 SGALDILVVNAGIAVFGDALELDA----------DDIDrlfKINIHAPYHASVEAARQMPEGGR--IIIIGSVNGDRMPV 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 31980844  160 N--VPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:PRK12742 141 AgmAAYAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDA 183
PRK08416 PRK08416
enoyl-ACP reductase;
5-204 2.94e-10

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 59.78  E-value: 2.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHLDTLRATAQEAQSLGG---RCVPVvcDSSQESEVKSLFEQVDr 80
Cdd:PRK08416   6 MKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTyNSNVEEANKIAEDLEQKYGikaKAYPL--NILEPETYKELFKKID- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   81 EQKGRLDVLVNNAYAGVQAILNTTNKSFWEVPASiwddINNVglrghYLCSVY--------GARLMVPAGKGLIVIVSSP 152
Cdd:PRK08416  83 EDFDRVDFFISNAIISGRAVVGGYTKFMRLKPKG----LNNI-----YTATVNafvvgaqeAAKRMEKVGGGSIISLSST 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 31980844  153 GGLQHMFNVP-YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEF 204
Cdd:PRK08416 154 GNLVYIENYAgHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAF 206
PRK07069 PRK07069
short chain dehydrogenase; Validated
 12-219 4.00e-10

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 59.34  E-value: 4.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   12 VTGASRGIGRGIALQLCKAGATVYITG-RHLDTLRATAQEAQSLGGRCV--PVVCDSSQESEVKSLFEQVDREQKGrLDV 88
Cdd:PRK07069   4 ITGAAGGLGRAIARRMAEQGAKVFLTDiNDAAGLDAFAAEINAAHGEGVafAAVQDVTDEAQWQALLAQAADAMGG-LSV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   89 LVNNayAGVQAILNTTNKSFWEvpasiWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNVP-YGVGK 167
Cdd:PRK07069  83 LVNN--AGVGSFGAIEQIELDE-----WRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTaYNASK 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 31980844  168 AACDRL----AADCAHelRRHGVSYVSLWPGLVQTEMVkefmakedtpeDPLFKKM 219
Cdd:PRK07069 156 AAVASLtksiALDCAR--RGLDVRCNSIHPTFIRTGIV-----------DPIFQRL 198
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 9-214 4.68e-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: 59.01  E-value: 4.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   9 VCVVTGASRGIGRGIALQLCKAGAT---VYITGRHL---DTLRATAQEA--QSLggRCVPV-VCDSsqesevKSLFEQVD 79
Cdd:cd09806   2 VVLITGCSSGIGLHLAVRLASDPSKrfkVYATMRDLkkkGRLWEAAGALagGTL--ETLQLdVCDS------KSVAAAVE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  80 REQKGRLDVLVNNAYAGVQAILNTTnkSFWEVPASIwdDINNVGLrghylcsvygARLM---VPAGK----GLIVIVSSP 152
Cdd:cd09806  74 RVTERHVDVLVCNAGVGLLGPLEAL--SEDAMASVF--DVNVFGT----------VRMLqafLPDMKrrgsGRILVTSSV 139

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980844 153 GGLQHM-FNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDP 214
Cdd:cd09806 140 GGLQGLpFNDVYCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEEVLDR 202
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 6-199 7.72e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 58.38  E-value: 7.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    6 KGQVCVVTGASRGIGRGIALQLCKAGATVYITGRhldtlraTAQEAQSLGGRCVPVvcDSSQESEVKSLFEQVdREQKGR 85
Cdd:PRK06523   8 AGKRALVTGGTKGIGAATVARLLEAGARVVTTAR-------SRPDDLPEGVEFVAA--DLTTAEGCAAVARAV-LERLGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   86 LDVLVNNAYA------GVQAIlnttnksfwevPASIWDDINNVGLrghyLCSVYGARLMVPA----GKGLIVIVSS---- 151
Cdd:PRK06523  78 VDILVHVLGGssapagGFAAL-----------TDEEWQDELNLNL----LAAVRLDRALLPGmiarGSGVIIHVTSiqrr 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 31980844  152 ---PGGLQHmfnvpYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTE 199
Cdd:PRK06523 143 lplPESTTA-----YAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETE 188
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 7-96 1.12e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 58.04  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKGRL 86
Cdd:PRK07576   9 GKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQI-ADEFGPI 87

                         90
                 ....*....|
gi 31980844   87 DVLVNNAyAG 96
Cdd:PRK07576  88 DVLVSGA-AG 96
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 11-196 1.88e-09

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: 56.90  E-value: 1.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  11 VVTGASRGIGRGIALQLCKAGATVYItgrHLDTLRATAQEAQ----SLGGRCVPVVCDSSQ----ESEVKSLFEQVdreq 82
Cdd:cd05357   4 LVTGAAKRIGRAIAEALAAEGYRVVV---HYNRSEAEAQRLKdelnALRNSAVLVQADLSDfaacADLVAAAFRAF---- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  83 kGRLDVLVNNAYAGVQailnttnKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIV----IVSSPGGLQHm 158
Cdd:cd05357  77 -GRCDVLVNNASAFYP-------TPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIIniidAMTDRPLTGY- 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 31980844 159 fnVPYGVGKAACDRL----AADCAHELRRHGVSyvslwPGLV 196
Cdd:cd05357 148 --FAYCMSKAALEGLtrsaALELAPNIRVNGIA-----PGLI 182
PRK08862 PRK08862
SDR family oxidoreductase;
5-92 2.14e-09

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 56.66  E-value: 2.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPV-VCDSSQESeVKSLFEQVDREQK 83
Cdd:PRK08862   3 IKSSIILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCSALTDNVYSFqLKDFSQES-IRHLFDAIEQQFN 81


                 ....*....
gi 31980844   84 GRLDVLVNN 92
Cdd:PRK08862  82 RAPDVLVNN 90
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 7-201 2.63e-09

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 56.89  E-value: 2.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDReQKGRL 86
Cdd:PRK05876   6 GRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFR-LLGHV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   87 DVLVNNAYAGVQA-ILNTTNKSF-WEVPASIWDDINNVglrghylcSVYGARLMVPAGKGLIVIVSSPGGLqhmfnVP-- 162
Cdd:PRK05876  85 DVVFSNAGIVVGGpIVEMTHDDWrWVIDVDLWGSIHTV--------EAFLPRLLEQGTGGHVVFTASFAGL-----VPna 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 31980844  163 ----YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMV 201
Cdd:PRK05876 152 glgaYGVAKYGVVGLAETLAREVTADGIGVSVLCPMVVETNLV 194
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-242 2.86e-09

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 56.69  E-value: 2.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVpVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYGNIHY-VVGDVSSTESARNVIEKA-AKVLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   85 RLDVLVNNAYAGVQAILnttnksfwEVPASIWDDINNvGLRGHYLCSVYGARLMVPAGKglIVIVSSPGGLQHMF--NVP 162
Cdd:PRK05786  81 AIDGLVVTVGGYVEDTV--------EEFSGLEEMLTN-HIKIPLYAVNASLRFLKEGSS--IVLVSSMSGIYKASpdQLS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  163 YGVGKAACDRLAADCAHELRRHGVSYVSLWPGlvqtemvkeFMAKEDTPEDPlFKKMKPDFSSAESPEMSGKCVVALATD 242
Cdd:PRK05786 150 YAVAKAGLAKAVEILASELLGRGIRVNGIAPT---------TISGDFEPERN-WKKLRKLGDDMAPPEDFAKVIIWLLTD 219
PRK05717 PRK05717
SDR family oxidoreductase;
3-151 3.06e-09

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 56.82  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    3 APMKGQVCVVTGASRGIGRGIALQLCKAGATVYITgrHLDTLRAtAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDReQ 82
Cdd:PRK05717   6 PGHNGRVALVTGAARGIGLGIAAWLIAEGWQVVLA--DLDRERG-SKVAKALGENAWFIAMDVADEAQVAAGVAEVLG-Q 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980844   83 KGRLDVLVNNAyagvqAILNTTNKSFWEVPASIWDDINNVGLRGHYL----CSVYgarlmVPAGKGLIVIVSS 151
Cdd:PRK05717  82 FGRLDALVCNA-----AIADPHNTTLESLSLAHWNRVLAVNLTGPMLlakhCAPY-----LRAHNGAIVNLAS 144
PRK07024 PRK07024
SDR family oxidoreductase;
11-200 3.22e-09

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 56.48  E-value: 3.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   11 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGG-RCVPV-VCDSSQESEVKSLFEQvdreQKGRLDV 88
Cdd:PRK07024   6 FITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAARvSVYAAdVRDADALAAAAADFIA----AHGLPDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   89 LVNNayAGVQAILNTTNKSFWEVPASIWdDINNVGLRGHYLCSVYGarlMVPAGKGLIVIVSSPGGLQHMfnvP----YG 164
Cdd:PRK07024  82 VIAN--AGISVGTLTEEREDLAVFREVM-DTNYFGMVATFQPFIAP---MRAARRGTLVGIASVAGVRGL---PgagaYS 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 31980844  165 VGKAA----CDRLAAdcahELRRHGVSYVSLWPGLVQTEM 200
Cdd:PRK07024 153 ASKAAaikyLESLRV----ELRPAGVRVVTIAPGYIRTPM 188
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 6-250 6.47e-09

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: 55.99  E-value: 6.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   6 KGQVcVVTGASRGIGRGIALQLCKAGA-TVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:cd09810   1 KGTV-VITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVGMPKDSYSVLHCDLASLDSVRQFVDNF-RRTGR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  85 RLDVLVNNayAGVQAILNttnksfwEVPASIWDDIN-NVGLR--GHYLCSvygaRLMV------PAGKGLIVIVSS---- 151
Cdd:cd09810  79 PLDALVCN--AAVYLPTA-------KEPRFTADGFElTVGVNhlGHFLLT----NLLLedlqrsENASPRIVIVGSithn 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 152 --------------------PGGLQHmFNVPYGVGKAACDRLAAD---C----AHELRRH-----GVSYVSLWPGLV-QT 198
Cdd:cd09810 146 pntlagnvppratlgdleglAGGLKG-FNSMIDGGEFEGAKAYKDskvCnmltTYELHRRlheetGITFNSLYPGCIaET 224

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 31980844 199 EMVKEFMakedtpedPLFKKMKPDF-----SSAESPEMSGKCVVALATDPNiLNLSG 250
Cdd:cd09810 225 GLFREHY--------PLFRTLFPPFqkyitKGYVSEEEAGERLAAVIADPS-LGVSG 272
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 5-90 7.82e-09

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: 55.41  E-value: 7.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGA--SRGIGRGIALQLCKAGATVYITGRHlDTLRATAQE-AQSLGGRCVpVVCDSSQESEVKSLFEQVdRE 81
Cdd:COG0623   3 LKGKRGLITGVanDRSIAWGIAKALHEEGAELAFTYQG-EALKKRVEPlAEELGSALV-LPCDVTDDEQIDALFDEI-KE 79


                ....*....
gi 31980844  82 QKGRLDVLV 90
Cdd:COG0623  80 KWGKLDFLV 88
PRK06914 PRK06914
SDR family oxidoreductase;
5-219 9.49e-09

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 55.41  E-value: 9.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLD---TLRATAQEAqSLGGRCVPVVCDSSQESEVKSlFEQVDRE 81
Cdd:PRK06914   1 MNKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEkqeNLLSQATQL-NLQQNIKVQQLDVTDQNSIHN-FQLVLKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   82 QkGRLDVLVNNAyagvqailNTTNKSFWEvpasiwdDINNVGLRGHYLCSVYGA----RLMVP----AGKGLIVIVSSPG 153
Cdd:PRK06914  79 I-GRIDLLVNNA--------GYANGGFVE-------EIPVEEYRKQFETNVFGAisvtQAVLPymrkQKSGKIINISSIS 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980844  154 GLQHMFNV-PYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM------VKEFMAKEDTPEDPLFKKM 219
Cdd:PRK06914 143 GRVGFPGLsPYVSSKYALEGFSESLRLELKPFGIDVALIEPGSYNTNIwevgkqLAENQSETTSPYKEYMKKI 215
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 7-90 9.50e-09

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: 54.90  E-value: 9.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   7 GQVCVVTGAS--RGIGRGIALQLCKAGATVYITGRHlDTLRATAQE-AQSLGGRCVPVVCDSSQESEVKSLFEQVdREQK 83
Cdd:cd05372   1 GKRILITGIAndRSIAWGIAKALHEAGAELAFTYQP-EALRKRVEKlAERLGESALVLPCDVSNDEEIKELFAEV-KKDW 78


                ....*..
gi 31980844  84 GRLDVLV 90
Cdd:cd05372  79 GKLDGLV 85
PRK09135 PRK09135
pteridine reductase; Provisional
 2-193 1.49e-08

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 54.55  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    2 VAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRATAQEAQSLGGRCVPVVC-DSSQESEVKSLFEQVD 79
Cdd:PRK09135   1 MMTDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADALAAELNALRPGSAAALQaDLLDPDALPELVAACV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   80 ReQKGRLDVLVNNAyagvqailnttnKSFW-----EVPASIWDDINNVGLRGHYLCSVYGARLMVPAgKGLIVIVSSPGG 154
Cdd:PRK09135  81 A-AFGRLDALVNNA------------SSFYptplgSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQ-RGAIVNITDIHA 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 31980844  155 LQHMFNVP-YGVGKAACDRLAADCAHEL----RRHGVSY-VSLWP 193
Cdd:PRK09135 147 ERPLKGYPvYCAAKAALEMLTRSLALELapevRVNAVAPgAILWP 191
PRK06720 PRK06720
hypothetical protein; Provisional
 1-93 1.87e-08

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 53.05  E-value: 1.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    1 MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEqVDR 80
Cdd:PRK06720  10 MKMKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEITNLGGEALFVSYDMEKQGDWQRVIS-ITL 88

                         90
                 ....*....|...
gi 31980844   81 EQKGRLDVLVNNA 93
Cdd:PRK06720  89 NAFSRIDMLFQNA 101
PRK07041 PRK07041
SDR family oxidoreductase;
11-93 2.77e-08

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 53.50  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   11 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSlGGRCVPVVCDSSQESEVKSLFEQVdreqkGRLDVLV 90
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGG-GAPVRTAALDITDEAAVDAFFAEA-----GPFDHVV 74


                 ...
gi 31980844   91 NNA 93
Cdd:PRK07041  75 ITA 77
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 7-244 4.11e-08

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: 52.71  E-value: 4.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRhldtlrataQEAQSLGGRCVPVVCDSSQESEvKSLFEQVDReQKGRL 86
Cdd:cd05334   1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDL---------AENEEADASIIVLDSDSFTEQA-KQVVASVAR-LSGKV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  87 DVLVNNA--YAGVQAILNTTNKSfwevpasiWDDINNVGLRGHYLCSVYGARLMVPAgkGLIVIVSSPGGLQ-HMFNVPY 163
Cdd:cd05334  70 DALICVAggWAGGSAKSKSFVKN--------WDLMWKQNLWTSFIASHLATKHLLSG--GLLVLTGAKAALEpTPGMIGY 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 164 GVGKAACDRLAADCAHELR--RHGVSYVSLWPGLVQTEMVKEFMAKEdtpedplfkkmkpDFSSAESPEMSGKCVVALAT 241
Cdd:cd05334 140 GAAKAAVHQLTQSLAAENSglPAGSTANAILPVTLDTPANRKAMPDA-------------DFSSWTPLEFIAELILFWAS 206


                ...
gi 31980844 242 DPN 244
Cdd:cd05334 207 GAA 209
PRK07775 PRK07775
SDR family oxidoreductase;
11-200 9.38e-08

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 52.45  E-value: 9.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   11 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDrEQKGRLDVLV 90
Cdd:PRK07775  14 LVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAE-EALGEIEVLV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   91 nnAYAGvqailNTTNKSFWEVPASIWDDINNVGLRGHYlcSVYGARL--MVPAGKGLIVIVSSPGGLQ---HMfnVPYGV 165
Cdd:PRK07775  93 --SGAG-----DTYFGKLHEISTEQFESQVQIHLVGAN--RLATAVLpgMIERRRGDLIFVGSDVALRqrpHM--GAYGA 161

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 31980844  166 GKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:PRK07775 162 AKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGM 196
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 6-93 1.52e-07

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: 52.37  E-value: 1.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   6 KGQVCVVTGASRGIGRGIALQLCK-AGATVYITGRH-----LDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVd 79
Cdd:cd08953 204 PGGVYLVTGGAGGIGRALARALARrYGARLVLLGRSplppeEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKV- 282

                        90
                ....*....|....
gi 31980844  80 REQKGRLDVLVNNA 93
Cdd:cd08953 283 RERYGAIDGVIHAA 296
PRK09186 PRK09186
flagellin modification protein A; Provisional
 5-151 1.66e-07

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 51.53  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGR---CVpVVCDSSQESEVKSLFEQVdRE 81
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSkklSL-VELDITDQESLEEFLSKS-AE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980844   82 QKGRLDVLVNNAYAgvqailntTNKS----FWEVPasiWDDIN---NVGLRGHYLCSVYGARLMVPAGKGLIVIVSS 151
Cdd:PRK09186  80 KYGKIDGAVNCAYP--------RNKDygkkFFDVS---LDDFNenlSLHLGSSFLFSQQFAKYFKKQGGGNLVNISS 145
PRK08340 PRK08340
SDR family oxidoreductase;
11-93 3.35e-07

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 50.57  E-value: 3.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   11 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGrCVPVVCDSSQESEVKSLFEQVdREQKGRLDVLV 90
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYGE-VYAVKADLSDKDDLKNLVKEA-WELLGGIDALV 81


                 ...
gi 31980844   91 NNA 93
Cdd:PRK08340  82 WNA 84
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
11-196 3.36e-07

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 50.75  E-value: 3.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  11 VVTGASRGIGRGIALQLCKAGATVYITGRhldtlRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDreqkgrldVLV 90
Cdd:COG0451   3 LVTGGAGFIGSHLARRLLARGHEVVGLDR-----SPPGAANLAALPGVEFVRGDLRDPEALAAALAGVD--------AVV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  91 NNAyagvqAILNTTNKSfwevPASIWDdINNVGLR-----------GHYL----CSVYGARlmvpagkGLIVIVSSPGGL 155
Cdd:COG0451  70 HLA-----APAGVGEED----PDETLE-VNVEGTLnlleaaraagvKRFVyassSSVYGDG-------EGPIDEDTPLRP 132

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 31980844 156 QHmfnvPYGVGKAACDRLAADCAhelRRHGVSYVSLWPGLV 196
Cdd:COG0451 133 VS----PYGASKLAAELLARAYA---RRYGLPVTILRPGNV 166
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-222 3.60e-07

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 50.35  E-value: 3.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    6 KGQVCVVTGASRGIGRGIALQLCKAGATVYitgrHLDTlrataQEAQSLGGRCVPVVCDSSQesEVKSLFEQVdreqkGR 85
Cdd:PRK06550   4 MTKTVLITGAASGIGLAQARAFLAQGAQVY----GVDK-----QDKPDLSGNFHFLQLDLSD--DLEPLFDWV-----PS 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   86 LDVLVNNayAGV----QAILNTTnksfwevpASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHmfnv 161
Cdd:PRK06550  68 VDILCNT--AGIlddyKPLLDTS--------LEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVA---- 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980844  162 pyGVGKAA-----------CDRLAADCAhelrRHGVSYVSLWPGLVQTEM-VKEF----MAKEDTPEDPLFKKMKPD 222
Cdd:PRK06550 134 --GGGGAAytaskhalagfTKQLALDYA----KDGIQVFGIAPGAVKTPMtAADFepggLADWVARETPIKRWAEPE 204
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 5-187 1.19e-06

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 48.80  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAqslgGRCVPVVCD--SSQESEVKSLFEQVDReq 82
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRF----GDHVLVVEGdvTSYADNQRAVDQTVDA-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   83 KGRLDVLVNNayAGV----QAILNTTnksfWEVPASIWDDINNVGLRGHYLcsvyGARLMVPA---GKGLIVIVSS---- 151
Cdd:PRK06200  78 FGKLDCFVGN--AGIwdynTSLVDIP----AETLDTAFDEIFNVNVKGYLL----GAKAALPAlkaSGGSMIFTLSnssf 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 31980844  152 -PGGlqhmFNVPYGVGKAACDRLAADCAHEL----RRHGVS 187
Cdd:PRK06200 148 yPGG----GGPLYTASKHAVVGLVRQLAYELapkiRVNGVA 184
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 11-212 2.45e-06

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: 47.87  E-value: 2.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  11 VVTGASRGIGRGIALQLCKAGATVyitgrhldtLRATAQEAQslggrcvpVVCDSSQESEVKSLFEQVDREQKGRLDVLV 90
Cdd:cd05328   3 VITGAASGIGAATAELLEDAGHTV---------IGIDLREAD--------VIADLSTPEGRAAAIADVLARCSGVLDGLV 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  91 NNAYAGVQAILNTTNKsfwevpasiwddINNVGLRgHYLCSVygARLMVPAGKGLIVIVSSPGGLQ-------------- 156
Cdd:cd05328  66 NCAGVGGTTVAGLVLK------------VNYFGLR-ALMEAL--LPRLRKGHGPAAVVVSSIAGAGwaqdklelakalaa 130

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31980844 157 --------------HMFNVPYGVGKAACDRLAADCAHE-LRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPE 212
Cdd:cd05328 131 gtearavalaehagQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPILQAFLQDPRGGE 201
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 12-200 3.39e-06

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: 47.66  E-value: 3.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  12 VTGASRGIGRGIALQLCKAGATVYITgrhldTLRATAQEAQSLGGRCVP----VVCDSSQESEVKSLFEQVDREQKGR-L 86
Cdd:cd09805   5 ITGCDSGFGNLLAKKLDSLGFTVLAG-----CLTKNGPGAKELRRVCSDrlrtLQLDVTKPEQIKRAAQWVKEHVGEKgL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  87 DVLVNNAyaGVQAILNTTnksfWEVPASIWDDINNVGLRGhyLCSVYGARL-MVPAGKGLIVIVSSPGGlQHMFNV--PY 163
Cdd:cd09805  80 WGLVNNA--GILGFGGDE----ELLPMDDYRKCMEVNLFG--TVEVTKAFLpLLRRAKGRVVNVSSMGG-RVPFPAggAY 150

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 31980844 164 GVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:cd09805 151 CASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGI 187
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 9-93 3.82e-06

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: 47.21  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844     9 VCVVTGASRGIGRGIALQLCKA----GATVYITGRHLDTLRATAQE--AQSLGGRCVPVVCDSSQESEV----KSLFEQV 78
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEigAERSGLRVVRVSLDLGAEAGLeqllKALRELP 81

                          90
                  ....*....|....*
gi 31980844    79 DREQKGRLdVLVNNA 93
Cdd:TIGR01500  82 RPKGLQRL-LLINNA 95
PRK06482 PRK06482
SDR family oxidoreductase;
12-154 4.56e-06

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 47.42  E-value: 4.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   12 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqsLGGRCVPVVCDSSQESEVKSLFEQVDREQkGRLDVLVN 91
Cdd:PRK06482   7 ITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKAR---YGDRLWVLQLDVTDSAAVRAVVDRAFAAL-GRIDVVVS 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31980844   92 NA-YAGVQAILNTTNKsfwEVPASIwdDINNVGlrghylcSVYGARLMVP----AGKGLIVIVSSPGG 154
Cdd:PRK06482  83 NAgYGLFGAAEELSDA---QIRRQI--DTNLIG-------SIQVIRAALPhlrrQGGGRIVQVSSEGG 138
PRK07102 PRK07102
SDR family oxidoreductase;
12-200 5.05e-06

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 46.84  E-value: 5.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   12 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPV-VCDSSQESEVKSLFEQVdreqKGRLD-VL 89
Cdd:PRK07102   6 IIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAVAVSThELDILDTASHAAFLDSL----PALPDiVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   90 VNNAYAGVQA-----------ILNTTnksfWEVPASIWDDInnvglrghylcsvygARLMVPAGKGLIVIVSSPGGLQ-H 157
Cdd:PRK07102  82 IAVGTLGDQAaceadpalalrEFRTN----FEGPIALLTLL---------------ANRFEARGSGTIVGISSVAGDRgR 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 31980844  158 MFNVPYGVGKAAcdrLAADCA---HELRRHGVSYVSLWPGLVQTEM 200
Cdd:PRK07102 143 ASNYVYGSAKAA---LTAFLSglrNRLFKSGVHVLTVKPGFVRTPM 185
PRK05854 PRK05854
SDR family oxidoreductase;
7-97 6.03e-06

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 46.98  E-value: 6.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRH-------LDTLRATAQEAQ-SLGGrcvpvvCDSSQESEVKSLFEQV 78
Cdd:PRK05854  14 GKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNrakgeaaVAAIRTAVPDAKlSLRA------LDLSSLASVAALGEQL 87

                         90       100
                 ....*....|....*....|
gi 31980844   79 DREqkGR-LDVLVNNayAGV 97
Cdd:PRK05854  88 RAE--GRpIHLLINN--AGV 103
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 5-253 8.63e-06

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: 46.19  E-value: 8.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqsLGGRCVPVVCD-SSQESEVKSLFEQVDReqK 83
Cdd:cd05348   2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRAD---FGDAVVGVEGDvRSLADNERAVARCVER--F 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  84 GRLDVLVNNayAGV----QAILNTTnksfWEVPASIWDDINNVGLRGHYLcsvyGARLMVPA---GKGLIVIVSS----- 151
Cdd:cd05348  77 GKLDCFIGN--AGIwdysTSLVDIP----EEKLDEAFDELFHINVKGYIL----GAKAALPAlyaTEGSVIFTVSnagfy 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844 152 PGGlqhmFNVPYGVGKAACDRLAADCAHEL----RRHGVSyvslwPGLVQTEMV------KEFMAKEDTPEDPLFKKMKP 221
Cdd:cd05348 147 PGG----GGPLYTASKHAVVGLVKQLAYELaphiRVNGVA-----PGGMVTDLRgpaslgQGETSISTPPLDDMLKSILP 217

                       250       260       270
                ....*....|....*....|....*....|..
gi 31980844 222 dFSSAESPEMSGKCVVALATDPNILNLSGKVL 253
Cdd:cd05348 218 -LGFAPEPEDYTGAYVFLASRGDNRPATGTVI 248
PRK08251 PRK08251
SDR family oxidoreductase;
8-210 8.91e-06

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 46.08  E-value: 8.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    8 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQE--AQSLGGRCVPVVCDSSQESEVKSLFEQVDREQkGR 85
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAEllARYPGIKVAVAALDVNDHDQVFEVFAEFRDEL-GG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   86 LDVLVNNAYAGVQAILNTTNksFWEVPASIwdDINNVGLrghyLCSVYGA-RLMVPAGKGLIVIVSS-------PGGLqh 157
Cdd:PRK08251  82 LDRVIVNAGIGKGARLGTGK--FWANKATA--ETNFVAA----LAQCEAAmEIFREQGSGHLVLISSvsavrglPGVK-- 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 31980844  158 mfnVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM---VKE--FMAKEDT 210
Cdd:PRK08251 152 ---AAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMnakAKStpFMVDTET 206
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 12-196 9.11e-06

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 46.29  E-value: 9.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   12 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqsLGGRCVPVVCDSSQESEVKSLFEQVDREQKgRLDVLVN 91
Cdd:PRK10538   5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDE---LGDNLYIAQLDVRNRAAIEEMLASLPAEWR-NIDVLVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   92 NayAGVQAILNTTNKsfwevpASI--WD---DINNVGLrghylcsVYGARL----MVPAGKGLIVIVSSPGGlqhmfNVP 162
Cdd:PRK10538  81 N--AGLALGLEPAHK------ASVedWEtmiDTNNKGL-------VYMTRAvlpgMVERNHGHIINIGSTAG-----SWP 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 31980844  163 ------YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLV 196
Cdd:PRK10538 141 yaggnvYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLV 180
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 7-93 1.14e-05

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: 46.05  E-value: 1.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHldtlRATAQEAQS-----LGGRCVPV-VCDSSQESEVKSLFEQVDR 80
Cdd:cd09808   1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRN----QTRAEEARKeieteSGNQNIFLhIVDMSDPKQVWEFVEEFKE 76

                        90
                ....*....|...
gi 31980844  81 EQKgRLDVLVNNA 93
Cdd:cd09808  77 EGK-KLHVLINNA 88
PRK07985 PRK07985
SDR family oxidoreductase;
5-233 1.20e-05

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 46.14  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITgrHLDTLRATAQEAQSL----GGRCVPVVCDSSQESEVKSLFEQVdR 80
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAIS--YLPVEEEDAQDVKKIieecGRKAVLLPGDLSDEKFARSLVHEA-H 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   81 EQKGRLDV--LVNNAYAGVQAILNTTNKSFWEVPAsiwddINNVGLrgHYLCSvyGARLMVPAGKGlIVIVSSPGGLQ-- 156
Cdd:PRK07985 124 KALGGLDImaLVAGKQVAIPDIADLTSEQFQKTFA-----INVFAL--FWLTQ--EAIPLLPKGAS-IITTSSIQAYQps 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  157 -HMFNvpYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMvkefMAKEDTPED--PLFKKMKPDFSSAESPEMSG 233
Cdd:PRK07985 194 pHLLD--YAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAL----QISGGQTQDkiPQFGQQTPMKRAGQPAELAP 267
PRK06128 PRK06128
SDR family oxidoreductase;
5-93 1.47e-05

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 46.01  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    5 MKGQVCVVTGASRGIGRGIALQLCKAGATVYITgrHLDTLRATAQEAQSL----GGRCVPVVCDSSQESEVKSLFEQVdR 80
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFAREGADIALN--YLPEEEQDAAEVVQLiqaeGRKAVALPGDLKDEAFCRQLVERA-V 129

                         90
                 ....*....|...
gi 31980844   81 EQKGRLDVLVNNA 93
Cdd:PRK06128 130 KELGGLDILVNIA 142
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 2-97 1.98e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 45.40  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    2 VAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDT-LRATAQEAQSLGGRCVPVV-CDSSQESEVKSLFEQVd 79
Cdd:PRK06197  11 IPDQSGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKgKAAAARITAATPGADVTLQeLDLTSLASVRAAADAL- 89

                         90
                 ....*....|....*...
gi 31980844   80 REQKGRLDVLVNNayAGV 97
Cdd:PRK06197  90 RAAYPRIDLLINN--AGV 105
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 12-200 2.73e-05

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: 44.79  E-value: 2.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  12 VTGASRGIGRGIALQLCKAGATVYITGRhlDTLRATAQEAQSLGGRCVpVVCDSSQESEVKSLFEQVDreQKGRLDVLVN 91
Cdd:cd08951  12 ITGSSDGLGLAAARTLLHQGHEVVLHAR--SQKRAADAKAACPGAAGV-LIGDLSSLAETRKLADQVN--AIGRFDAVIH 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  92 NAyagvqAILNTTNKsfwEVPASIWDDINNVGLRGHYLCSvygARLMVPagKGLIVIVSS--PGGLQHM-----FNVPYG 164
Cdd:cd08951  87 NA-----GILSGPNR---KTPDTGIPAMVAVNVLAPYVLT---ALIRRP--KRLIYLSSGmhRGGNASLddidwFNRGEN 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 31980844 165 VGKAACDR------LAADCAHelRRHGVSYVSLWPGLVQTEM 200
Cdd:cd08951 154 DSPAYSDSklhvltLAAAVAR--RWKDVSSNAVHPGWVPTKM 193
PRK05993 PRK05993
SDR family oxidoreductase;
11-199 2.93e-05

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 44.63  E-value: 2.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   11 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEaqslGGRCVPVvcDSSQESEVKSLFEQVDREQKGRLDVLV 90
Cdd:PRK05993   8 LITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEAE----GLEAFQL--DYAEPESIAALVAQVLELSGGRLDALF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   91 NN-AYAGVQAIlnttnksfwevpasiwDDINNVGLRGHYLCSVYG----ARLMVPA----GKGLIVIVSSPGGLQHM-FN 160
Cdd:PRK05993  82 NNgAYGQPGAV----------------EDLPTEALRAQFEANFFGwhdlTRRVIPVmrkqGQGRIVQCSSILGLVPMkYR 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 31980844  161 VPYGVGKAACDRLAADCAHELRRHGVsYVSLW-PGLVQTE 199
Cdd:PRK05993 146 GAYNASKFAIEGLSLTLRMELQGSGI-HVSLIePGPIETR 184
PRK08177 PRK08177
SDR family oxidoreductase;
12-200 7.29e-05

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 43.09  E-value: 7.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   12 VTGASRGIGRGIALQLCKAGATVYITGRhlDTLRATAqeAQSLGGRCVPVVcDSSQESEVKSLFEQVDREqkgRLDVLVN 91
Cdd:PRK08177   6 IIGASRGLGLGLVDRLLERGWQVTATVR--GPQQDTA--LQALPGVHIEKL-DMNDPASLDQLLQRLQGQ---RFDLLFV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   92 NAyagvqAILNTTNKSFWEV-PASIWD--DINNVG-LRghylcsvyGARLMVP---AGKGLIVIVSS--------PGGlq 156
Cdd:PRK08177  78 NA-----GISGPAHQSAADAtAAEIGQlfLTNAIApIR--------LARRLLGqvrPGQGVLAFMSSqlgsvelpDGG-- 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 31980844  157 hmfNVP-YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEM 200
Cdd:PRK08177 143 ---EMPlYKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDM 184
PRK06953 PRK06953
SDR family oxidoreductase;
12-200 7.82e-05

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 43.14  E-value: 7.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   12 VTGASRGIGRGIALQLCKAGATVYITGRH---LDTLRATAQEAQSLggrcvpvvcDSSQESEVKSLFEQVDREqkgRLDV 88
Cdd:PRK06953   6 IVGASRGIGREFVRQYRADGWRVIATARDaaaLAALQALGAEALAL---------DVADPASVAGLAWKLDGE---ALDA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   89 LVNNayAGV-----QAILNTTNKSFWEVPASiwddinnvglrghylcSVYGARL-------MVPAGKGLIVIVSSP---- 152
Cdd:PRK06953  74 AVYV--AGVygprtEGVEPITREDFDAVMHT----------------NVLGPMQllpillpLVEAAGGVLAVLSSRmgsi 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 31980844  153 GGLQHMFNVPYGVGKAACDRLAADCAHELRRhgVSYVSLWPGLVQTEM 200
Cdd:PRK06953 136 GDATGTTGWLYRASKAALNDALRAASLQARH--ATCIALHPGWVRTDM 181
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 10-82 9.18e-05

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: 43.53  E-value: 9.18e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31980844  10 CVVTGASRGIGRGIALQLCKAGAT-VYITGRHLDTLRATAQEAQS--LGGRCVPVVCDSSQESEVKSLFEQVDREQ 82
Cdd:cd05274 153 YLITGGLGGLGLLVARWLAARGARhLVLLSRRGPAPRAAARAALLraGGARVSVVRCDVTDPAALAALLAELAAGG 228
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 11-93 1.64e-04

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: 41.80  E-value: 1.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  11 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRataqeaqslggrcvpvvCDSSQESEVKSLFEQVdreqkGRLDVLV 90
Cdd:cd11731   2 IVIGATGTIGLAVAQLLSAHGHEVITAGRSSGDYQ-----------------VDITDEASIKALFEKV-----GHFDAIV 59


                ...
gi 31980844  91 NNA 93
Cdd:cd11731  60 STA 62
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 9-111 2.03e-04

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: 41.31  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844      9 VCVVTGASRGIGRGIALQLCKAGA-TVYITGRH---LDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVdREQKG 84
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGArRLVLLSRSgpdAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAI-PAVEG 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 31980844     85 RLDVLVNNayAGV---QAILNTTNKSFWEV 111
Cdd:smart00822  81 PLTGVIHA--AGVlddGVLASLTPERFAAV 108
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 9-95 4.46e-04

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: 41.07  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844     9 VCVVTGASRGIGRGIALQLCKAGATVYITGRHldtlraTAQEAQSLGG-----RCVPVVCDSSQESEVKSLF----EQVD 79
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHR------SAAAASTLAAelnarRPNSAVTCQADLSNSATLFsrceAIID 76

                          90
                  ....*....|....*...
gi 31980844    80 REQK--GRLDVLVNNAYA 95
Cdd:TIGR02685  77 ACFRafGRCDVLVNNASA 94
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
7-96 5.47e-04

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 40.85  E-value: 5.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    7 GQVCVVTGAS--RGIGRGIALQLCKAGATVYIT------GRHLDTLRA-TAQEAQSLggrCVPvvCDSSQESEVKSLFEQ 77
Cdd:PRK07370   6 GKKALVTGIAnnRSIAWGIAQQLHAAGAELGITylpdekGRFEKKVRElTEPLNPSL---FLP--CDVQDDAQIEETFET 80

                         90       100
                 ....*....|....*....|
gi 31980844   78 VdREQKGRLDVLVNN-AYAG 96
Cdd:PRK07370  81 I-KQKWGKLDILVHClAFAG 99
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 11-199 6.05e-04

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: 40.64  E-value: 6.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  11 VVTGASRGIGRGIALQLCKAGATVYITgrhlDTLRATAQEAQSLGGRCVPVVCDSSQESEvkSLFEQVdREQKGRLDVLV 90
Cdd:cd05361   5 LVTHARHFAGPASAEALTEDGYTVVCH----DASFADAAERQAFESENPGTKALSEQKPE--ELVDAV-LQAGGAIDVLV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  91 NNAYagvqailnttnksfWEVPASIWDDINNVGLRGHYLCSVYGARLMVPA--------GKGLIVIVSSPGGLQHMFNVP 162
Cdd:cd05361  78 SNDY--------------IPRPMNPIDGTSEADIRQAFEALSIFPFALLQAaiaqmkkaGGGSIIFITSAVPKKPLAYNS 143

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 31980844 163 -YGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTE 199
Cdd:cd05361 144 lYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSP 181
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 11-81 9.54e-04

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: 39.47  E-value: 9.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980844    11 VVTGASRGIGRGIALQLCKAGA-TVYITGRH---LDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDRE 81
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGArHLVLLSRSaapRPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAE 78
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
 10-196 1.16e-03

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 39.58  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  10 CVVTGASRGIGRGIALQLCKAGATVYI--TGRHLDtlrataqeaqSLGGRCVPVVCDSSQESEVKSLFeqvdreqKGRL- 86
Cdd:cd05265   3 ILIIGGTRFIGKALVEELLAAGHDVTVfnRGRTKP----------DLPEGVEHIVGDRNDRDALEELL-------GGEDf 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844  87 DVLV-NNAYAgvqailnttnksfwevPASIWDDINNVGLR-GHYL----CSVYGARLMV-----PAGKGLIVIVSSPGgl 155
Cdd:cd05265  66 DVVVdTIAYT----------------PRQVERALDAFKGRvKQYIfissASVYLKPGRVitestPLREPDAVGLSDPW-- 127

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 31980844 156 qhmfnvPYGVGKAACDRLAAdcahelRRHGVSYVSLWPGLV 196
Cdd:cd05265 128 ------DYGRGKRAAEDVLI------EAAAFPYTIVRPPYI 156
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 7-202 2.32e-03

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 39.08  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844    7 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRC--VPVVCDSSQESE--VKSLFEQVDREQ 82
Cdd:PLN02780  53 GSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKTqiKTVVVDFSGDIDegVKRIKETIEGLD 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980844   83 KGrldVLVNNayAGVQAilnTTNKSFWEVPASIWDDINNVGLRGhyLCSVYGARL--MVPAGKGLIVIVSSPGGL---QH 157
Cdd:PLN02780 133 VG---VLINN--VGVSY---PYARFFHEVDEELLKNLIKVNVEG--TTKVTQAVLpgMLKRKKGAIINIGSGAAIvipSD 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 31980844  158 MFNVPYGVGKAACDRLAAdCAH-ELRRHGVSYVSLWPGLVQTEMVK 202
Cdd:PLN02780 203 PLYAVYAATKAYIDQFSR-CLYvEYKKSGIDVQCQVPLYVATKMAS 247
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 6-65 2.81e-03

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 38.98  E-value: 2.81e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31980844   6 KGQVCVVTGASRGIGrGIALQLCKA-GATVYITGR---HLDTLRA--------------TAQEAQSLGGRCVPVVCDS 65
Cdd:COG0604 139 PGETVLVHGAAGGVG-SAAVQLAKAlGARVIATASspeKAELLRAlgadhvidyreedfAERVRALTGGRGVDVVLDT 215
 
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