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Conserved domains on  [gi|392895268|ref|NP_001254936|]
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Very-long-chain 3-oxooacyl-coA reductase let-767 [Caenorhabditis elegans]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143247)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to very-long-chain 3-oxoacyl-CoA reductase that catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation; 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
47-289 3.82e-117

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: 337.27  E-value: 3.82e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  47 ASWAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSsIEVRTAAFDFTnAAPSAYKDLLATLNQVE 126
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYG-VETKTIAADFS-AGDDIYERIEKELEGLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IGVLINNVGMSYEYPDVLHKVDGgiERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATK 206
Cdd:cd05356   79 IGILVNNVGISHSIPEYFLETPE--DELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 207 KYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTSFFTPDGAVFAKSALNTVGNTSDTTGYITHQLQLELMDLIP 286
Cdd:cd05356  157 AFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKSSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARLVP 236

                 ...
gi 392895268 287 TFI 289
Cdd:cd05356  237 EWI 239
 
Name Accession Description Interval E-value
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
47-289 3.82e-117

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: 337.27  E-value: 3.82e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  47 ASWAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSsIEVRTAAFDFTnAAPSAYKDLLATLNQVE 126
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYG-VETKTIAADFS-AGDDIYERIEKELEGLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IGVLINNVGMSYEYPDVLHKVDGgiERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATK 206
Cdd:cd05356   79 IGILVNNVGISHSIPEYFLETPE--DELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 207 KYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTSFFTPDGAVFAKSALNTVGNTSDTTGYITHQLQLELMDLIP 286
Cdd:cd05356  157 AFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKSSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARLVP 236

                 ...
gi 392895268 287 TFI 289
Cdd:cd05356  237 EWI 239
PLN02780 PLN02780
ketoreductase/ oxidoreductase
25-312 6.23e-64

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 204.71  E-value: 6.23e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  25 IFSNILGPYV-LLSPIDLKKRAGaSWAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTA 103
Cdd:PLN02780  31 FFTILNWVYVyFLRPAKNLKKYG-SWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKTQIKTV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 104 AFDFTNAAPSAYKDLLATLNQVEIGVLINNVGMSYEYPDVLHKVDGGIerLANITTINTLPPTLLSAGILPQMVARKAGV 183
Cdd:PLN02780 110 VVDFSGDIDEGVKRIKETIEGLDVGVLINNVGVSYPYARFFHEVDEEL--LKNLIKVNVEGTTKVTQAVLPGMLKRKKGA 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 184 IVNVGSSAGA--NQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTSFFTPDGAVFAKSALN 261
Cdd:PLN02780 188 IINIGSGAAIviPSDPLYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMASIRRSSFLVPSSDGYARAALR 267
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392895268 262 TVGNTSDTTGYITHQLQLELMDLIPTFIRDKILTNMSVGTRAAALRKKERE 312
Cdd:PLN02780 268 WVGYEPRCTPYWPHSLIWGLISALPESAVDSWRLKFCLQIRKKGQQKDSRK 318
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
49-239 2.60e-40

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 141.16  E-value: 2.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  49 WAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKysSIEVRTAAFDFTN--AAPSAYKDLLATLNQVE 126
Cdd:COG0300    7 TVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAA--GARVEVVALDVTDpdAVAALAEAVLARFGPID 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 igVLINNVGMSYeyPDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATK 206
Cdd:COG0300   85 --VLVNNAGVGG--GGPFEELD--LEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASK 158
                        170       180       190
                 ....*....|....*....|....*....|...
gi 392895268 207 KYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:COG0300  159 AALEGFSESLRAELAPTGVRVTAVCPGPVDTPF 191
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
49-244 5.49e-37

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 130.81  E-value: 5.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268   49 WAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKysSIEVRTAAFDFTNAApsaykDLLATLNQVE-- 126
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAL--GGKALFIQGDVTDRA-----QVKALVEQAVer 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  127 ---IGVLINNVGMSYEYPDVLHKVDGgIERLANIttiNTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYS 203
Cdd:pfam00106  75 lgrLDILVNNAGITGLGPFSELSDED-WERVIDV---NLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYS 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 392895268  204 ATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKR 244
Cdd:pfam00106 151 ASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
50-246 1.81e-10

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: 60.31  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268   50 AVVTGATDGIGKAYAFELARR----GFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAPSA--YKDLLATL- 122
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAERSGLRVVRVSLDLGAEAGLEqlLKALRELPr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  123 -NQVEIGVLINNVGMSYEypdvLHKVDGGIERLANITTINTLppTLLSAGILPQMVARK-------AGVIVNVGSSAGAN 194
Cdd:TIGR01500  83 pKGLQRLLLINNAGTLGD----VSKGFVDLSDSTQVQNYWAL--NLTSMLCLTSSVLKAfkdspglNRTVVNISSLCAIQ 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392895268  195 QMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM-SKVKRTS 246
Cdd:TIGR01500 157 PFKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMqQQVREES 209
 
Name Accession Description Interval E-value
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
47-289 3.82e-117

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: 337.27  E-value: 3.82e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  47 ASWAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSsIEVRTAAFDFTnAAPSAYKDLLATLNQVE 126
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYG-VETKTIAADFS-AGDDIYERIEKELEGLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IGVLINNVGMSYEYPDVLHKVDGgiERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATK 206
Cdd:cd05356   79 IGILVNNVGISHSIPEYFLETPE--DELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 207 KYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTSFFTPDGAVFAKSALNTVGNTSDTTGYITHQLQLELMDLIP 286
Cdd:cd05356  157 AFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKSSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARLVP 236

                 ...
gi 392895268 287 TFI 289
Cdd:cd05356  237 EWI 239
PLN02780 PLN02780
ketoreductase/ oxidoreductase
25-312 6.23e-64

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 204.71  E-value: 6.23e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  25 IFSNILGPYV-LLSPIDLKKRAGaSWAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTA 103
Cdd:PLN02780  31 FFTILNWVYVyFLRPAKNLKKYG-SWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKTQIKTV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 104 AFDFTNAAPSAYKDLLATLNQVEIGVLINNVGMSYEYPDVLHKVDGGIerLANITTINTLPPTLLSAGILPQMVARKAGV 183
Cdd:PLN02780 110 VVDFSGDIDEGVKRIKETIEGLDVGVLINNVGVSYPYARFFHEVDEEL--LKNLIKVNVEGTTKVTQAVLPGMLKRKKGA 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 184 IVNVGSSAGA--NQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTSFFTPDGAVFAKSALN 261
Cdd:PLN02780 188 IINIGSGAAIviPSDPLYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMASIRRSSFLVPSSDGYARAALR 267
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392895268 262 TVGNTSDTTGYITHQLQLELMDLIPTFIRDKILTNMSVGTRAAALRKKERE 312
Cdd:PLN02780 268 WVGYEPRCTPYWPHSLIWGLISALPESAVDSWRLKFCLQIRKKGQQKDSRK 318
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
49-239 2.60e-40

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 141.16  E-value: 2.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  49 WAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKysSIEVRTAAFDFTN--AAPSAYKDLLATLNQVE 126
Cdd:COG0300    7 TVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAA--GARVEVVALDVTDpdAVAALAEAVLARFGPID 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 igVLINNVGMSYeyPDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATK 206
Cdd:COG0300   85 --VLVNNAGVGG--GGPFEELD--LEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASK 158
                        170       180       190
                 ....*....|....*....|....*....|...
gi 392895268 207 KYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:COG0300  159 AALEGFSESLRAELAPTGVRVTAVCPGPVDTPF 191
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
49-244 5.49e-37

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 130.81  E-value: 5.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268   49 WAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKysSIEVRTAAFDFTNAApsaykDLLATLNQVE-- 126
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAL--GGKALFIQGDVTDRA-----QVKALVEQAVer 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  127 ---IGVLINNVGMSYEYPDVLHKVDGgIERLANIttiNTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYS 203
Cdd:pfam00106  75 lgrLDILVNNAGITGLGPFSELSDED-WERVIDV---NLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYS 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 392895268  204 ATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKR 244
Cdd:pfam00106 151 ASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
50-240 4.37e-32

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: 119.52  E-value: 4.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlekysSIEVRTAAFDFTNAA--PSAYKDLLATLNQVEi 127
Cdd:COG4221    8 ALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAEL-----GGRALAVPLDVTDEAavEAAVAAAVAEFGRLD- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gVLINNVGMSyeYPDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:COG4221   82 -VLVNNAGVA--LLGPLEELD--PEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKA 156
                        170       180       190
                 ....*....|....*....|....*....|...
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVATKMS 240
Cdd:COG4221  157 AVRGLSESLRAELRPTGIRVTVIEPGAVDTEFL 189
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
50-239 2.30e-31

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: 117.58  E-value: 2.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKysSIEVRTAAFDFTNAApsAYKDLLATLNQV--EI 127
Cdd:COG1028    9 ALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAA--GGRALAVAADVTDEA--AVEALVAAAVAAfgRL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYeyPDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:COG1028   85 DILVNNAGITP--PGPLEELT--EEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKA 160
                        170       180       190
                 ....*....|....*....|....*....|..
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:COG1028  161 AVVGLTRSLALELAPRGIRVNAVAPGPIDTPM 192
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
50-241 1.42e-29

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: 112.76  E-value: 1.42e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTaafDFTNAApsaykDLLATLNQVE--- 126
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALGGNAVAVQA---DVSDEE-----DVEALVEEALeef 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 --IGVLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSA 204
Cdd:cd05233   73 grLDILVNNAGIARPGP----LEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAA 148
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 392895268 205 TKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:cd05233  149 SKAALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLA 185
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
50-243 1.75e-28

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: 110.06  E-value: 1.75e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSiEVRTAAFDFTNAA--PSAYKDLLATLNQVEI 127
Cdd:cd05346    3 VLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPV-KVLPLQLDVSDREsiEAALENLPEEFRDIDI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gvLINNVGMS--------YEYPDVLHKVDGGIERLANITTIntlpptllsagILPQMVARKAGVIVNVGSSAGANQMALW 199
Cdd:cd05346   82 --LVNNAGLAlgldpaqeADLEDWETMIDTNVKGLLNVTRL-----------ILPIMIARNQGHIINLGSIAGRYPYAGG 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 392895268 200 AVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVK 243
Cdd:cd05346  149 NVYCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFSLVR 192
PRK07454 PRK07454
SDR family oxidoreductase;
50-251 3.28e-28

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 109.28  E-value: 3.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKysSIEVRTAAFDFTN--AAPSAYKDLLAtlNQVEI 127
Cdd:PRK07454   9 ALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRST--GVKAAAYSIDLSNpeAIAPGIAELLE--QFGCP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:PRK07454  85 DVLINNAGMAYTGP----LLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVATKM-------SKVKRTSFFTPD 251
Cdd:PRK07454 161 ALAAFTKCLAEEERSHGIRVCTITLGAVNTPLwdtetvqADFDRSAMLSPE 211
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
50-241 5.46e-26

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 103.23  E-value: 5.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlEKYSsIEVRTAAFDFTNAAP--SAYKDLLATLNQVEI 127
Cdd:PRK07666  10 ALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEV-EAYG-VKVVIATADVSDYEEvtAAIEQLKNELGSIDI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gvLINNVGMSyEYPDVLhkvDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:PRK07666  88 --LINNAGIS-KFGKFL---ELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKF 161
                        170       180       190
                 ....*....|....*....|....*....|....
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:PRK07666 162 GVLGLTESLMQEVRKHNIRVTALTPSTVATDMAV 195
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
51-240 7.18e-25

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: 100.74  E-value: 7.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEkYSSIEVRTAAFDFTN--AAPSAYKDLLATLNQVEIg 128
Cdd:cd05332    7 IITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLE-LGAPSPHVVPLDMSDleDAEQVVEEALKLFGGLDI- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 vLINNVGMSyeYPDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKY 208
Cdd:cd05332   85 -LINNAGIS--MRSLFHDTS--IDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHA 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 392895268 209 VSWLTAILRKEYEHQGITVQTIAPMMVATKMS 240
Cdd:cd05332  160 LQGFFDSLRAELSEPNISVTVVCPGLIDTNIA 191
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
50-239 1.58e-24

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: 98.92  E-value: 1.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlekySSIEVRTAafDFTNAA--PSAYKDLLAtlNQVEI 127
Cdd:cd05370    8 VLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKEL----PNIHTIVL--DVGDAEsvEALAEALLS--EYPNL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYEY-----PDVLHKVDGGIErlanittINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVY 202
Cdd:cd05370   80 DILINNAGIQRPIdlrdpASDLDKADTEID-------TNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVY 152
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 392895268 203 SATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:cd05370  153 CATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTEL 189
PRK05866 PRK05866
SDR family oxidoreductase;
34-239 1.21e-23

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 98.28  E-value: 1.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  34 VLLSPIDLK-KRAgaswaVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEkySSIEVRTAAFDFTNaaP 112
Cdd:PRK05866  31 PPRQPVDLTgKRI-----LLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITR--AGGDAMAVPCDLSD--L 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 113 SAYKDLLATLNQvEIG---VLINNVGMSYEYP-----DVLHKVdggiERlanITTINTLPPTLLSAGILPQMVARKAGVI 184
Cdd:PRK05866 102 DAVDALVADVEK-RIGgvdILINNAGRSIRRPlaeslDRWHDV----ER---TMVLNYYAPLRLIRGLAPGMLERGDGHI 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392895268 185 VNVGS-SAGANQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK05866 174 INVATwGVLSEASPLFSVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPM 229
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
50-274 1.23e-23

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: 96.28  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKkeiLEKYSSIEVRTAAFDFTNAapSAYKDLLATLNQvEIGV 129
Cdd:cd08932    3 ALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALS---ASGGDVEAVPYDARDPEDA--RALVDALRDRFG-RIDV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 LINNVGMSyEYPDVLHKVDGGIERLANIttiNTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKYV 209
Cdd:cd08932   77 LVHNAGIG-RPTTLREGSDAELEAHFSI---NVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFAL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392895268 210 SWLTAILRKEYEHQGITVQTIAPMMVATKM-SKVKRTSFFTPDGAVFAKSALNTVGNTSDTTGYIT 274
Cdd:cd08932  153 RALAHALRQEGWDHGVRVSAVCPGFVDTPMaQGLTLVGAFPPEEMIQPKDIANLVRMVIELPENIT 218
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
50-241 2.54e-23

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: 96.27  E-value: 2.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlEKYsSIEVRTAAFDFTNaaPSAYKDLLAtlnQVE--- 126
Cdd:cd05347    8 ALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLI-EKE-GVEATAFTCDVSD--EEAIKAAVE---AIEedf 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 --IGVLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSA 204
Cdd:cd05347   81 gkIDILVNNAGIIRRHP----AEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAA 156
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 392895268 205 TKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:cd05347  157 SKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTE 193
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
50-245 3.79e-22

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 92.92  E-value: 3.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEkySSIEVRTAAFDFTNAApsAYKDLLATLNQV--EI 127
Cdd:PRK05653   8 ALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRA--AGGEARVLVFDVSDEA--AVRALIEAAVEAfgAL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVG---------MSYE-YPDVLHkvdggierlANIT-TINTLPPTllsagiLPQMVARKAGVIVNVGSSAGANQM 196
Cdd:PRK05653  84 DILVNNAGitrdallprMSEEdWDRVID---------VNLTgTFNVVRAA------LPPMIKARYGRIVNISSVSGVTGN 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 392895268 197 ALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRT 245
Cdd:PRK05653 149 PGQTNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDMTEGLPE 197
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
52-241 2.75e-21

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: 90.61  E-value: 2.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  52 VTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILekyssiEVRTAAFDFTNAA--PSAYKDLLAT---LNqve 126
Cdd:COG3967   10 ITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANP------GLHTIVLDVADPAsiAALAEQVTAEfpdLN--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 igVLINNVGMSYEYpdvlhKVDGGIERLANIT---TINTLPPTLLSAGILPQMVARKAGVIVNVgSSAGANQ-MALWAVY 202
Cdd:COG3967   81 --VLINNAGIMRAE-----DLLDEAEDLADAEreiTTNLLGPIRLTAAFLPHLKAQPEAAIVNV-SSGLAFVpLAVTPTY 152
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 392895268 203 SATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:COG3967  153 SATKAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTG 191
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
50-293 4.57e-21

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: 89.70  E-value: 4.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVrtAAFDFTNAA--PSAYKDLLATLNQVEI 127
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEV--EILDVTDEErnQLVIAELEAELGGLDL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYEYPDVLHKVDGGIERLANITTINTLPPtllsagILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:cd05350   79 VIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEA------ALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTSFFTPDGAVFAKSALNTVgNTSDTTGYITHQL--QLELMDLI 285
Cdd:cd05350  153 ALSSLAESLRYDVKKRGIRVTVINPGFIDTPLTANMFTMPFLMSVEQAAKRIYKAI-KKGAAEPTFPWRLavPLRLLKLL 231

                 ....*...
gi 392895268 286 PTFIRDKI 293
Cdd:cd05350  232 PERLRRRL 239
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
50-239 5.44e-21

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: 89.62  E-value: 5.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKY--SSIEVRTAAFDFTNaapsaYKDLLATLNQVE- 126
Cdd:cd08939    4 VLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEAnaSGQKVSYISADLSD-----YEEVEQAFAQAVe 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 ----IGVLINNVGMSyeYPDVLHKVDGG-IERLANI---TTINtlpptlLSAGILPQMVARKAGVIVNVGSSAGANQMAL 198
Cdd:cd08939   79 kggpPDLVVNCAGIS--IPGLFEDLTAEeFERGMDVnyfGSLN------VAHAVLPLMKEQRPGHIVFVSSQAALVGIYG 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392895268 199 WAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:cd08939  151 YSAYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTPG 191
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
50-239 6.22e-21

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 89.82  E-value: 6.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSkldETKKEILEKY--SSIEVRTAAFDFTNAApsAYKDLLATLNQVE- 126
Cdd:PRK12824   5 ALVTGAKRGIGSAIARELLNDGYRVIATYFSGN---DCAKDWFEEYgfTEDQVRLKELDVTDTE--ECAEALAEIEEEEg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 -IGVLINNVGMSYEypDVLHKVdgGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSAT 205
Cdd:PRK12824  80 pVDILVNNAGITRD--SVFKRM--SHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAA 155
                        170       180       190
                 ....*....|....*....|....*....|....
gi 392895268 206 KKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK12824 156 KAGMIGFTKALASEGARYGITVNCIAPGYIATPM 189
PRK09291 PRK09291
SDR family oxidoreductase;
52-232 1.05e-20

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 89.29  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  52 VTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVR----TAAFDFTNAApsaykdllatlnQVEI 127
Cdd:PRK09291   7 ITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRGLALRVEkldlTDAIDRAQAA------------EWDV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:PRK09291  75 DVLLNNAGIGEAGA----VVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKH 150
                        170       180
                 ....*....|....*....|....*
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:PRK09291 151 ALEAIAEAMHAELKPFGIQVATVNP 175
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
50-246 1.33e-20

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: 89.12  E-value: 1.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLdETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLATLNQVEIgv 129
Cdd:cd08937    7 VVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVH-EVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDV-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 LINNVGMSYEYPDVLHKVDGGIERlaniTTINTLPPTL-LSAGILPQMVARKAGVIVNVGSSAGANqmALWAVYSATKKY 208
Cdd:cd08937   84 LINNVGGTIWAKPYEHYEEEQIEA----EIRRSLFPTLwCCRAVLPHMLERQQGVIVNVSSIATRG--IYRIPYSAAKGG 157
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895268 209 VSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTS 246
Cdd:cd08937  158 VNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPRNA 195
PRK09072 PRK09072
SDR family oxidoreductase;
51-239 2.83e-20

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 88.07  E-value: 2.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIleKYSSiEVRTAAFDFTnaAPSAYKDLLATLNQVE-IGV 129
Cdd:PRK09072   9 LLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARL--PYPG-RHRWVVADLT--SEAGREAVLARAREMGgINV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 LINNVGMSYEypDVL-HKVDGGIERL--ANITTintlpPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATK 206
Cdd:PRK09072  84 LINNAGVNHF--ALLeDQDPEAIERLlaLNLTA-----PMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASK 156
                        170       180       190
                 ....*....|....*....|....*....|...
gi 392895268 207 KYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK09072 157 FALRGFSEALRRELADTGVRVLYLAPRATRTAM 189
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
50-232 4.47e-20

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: 87.29  E-value: 4.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVrtaafDFTNaaPSAYKDLLATLNQVE--I 127
Cdd:cd05374    3 VLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLEL-----DVTD--EESIKAAVKEVIERFgrI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYEYPdVLhkvDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:cd05374   76 DVLVNNAGYGLFGP-LE---ETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKA 151
                        170       180
                 ....*....|....*....|....*
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:cd05374  152 ALEALSESLRLELAPFGIKVTIIEP 176
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
50-242 2.10e-19

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: 85.29  E-value: 2.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIleKYSSIEVRTAAFDFTN--AAPSAYKDLLATLNQVEI 127
Cdd:cd05333    3 ALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEI--KALGGNAAALEADVSDreAVEALVEKVEAEFGPVDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gvLINNVG---------MSYE-YPDVLHkvdggierlANITTIntlppTLLSAGILPQMVARKAGVIVNVGSSAG----A 193
Cdd:cd05333   81 --LVNNAGitrdnllmrMSEEdWDAVIN---------VNLTGV-----FNVTQAVIRAMIKRRSGRIINISSVVGlignP 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 392895268 194 NQmalwAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKV 242
Cdd:cd05333  145 GQ----ANYAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDA 189
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
49-242 2.33e-19

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 85.28  E-value: 2.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  49 WAVVTGATDGIGKAYAFELARRGFNVLL-VSRTQSKLDETKKEILEKYSSIEvrtaafdFTNAAPSAYKDLLATLNQVE- 126
Cdd:PRK05565   7 VAIVTGASGGIGRAIAELLAKEGAKVVIaYDINEEAAQELLEEIKEEGGDAI-------AVKADVSSEEDVENLVEQIVe 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 ----IGVLINNVGMSY-----EYPDvlhkvdggiERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVgSSAGANQMA 197
Cdd:PRK05565  80 kfgkIDILVNNAGISNfglvtDMTD---------EEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNI-SSIWGLIGA 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 392895268 198 -LWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKV 242
Cdd:PRK05565 150 sCEVLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSS 195
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
50-239 4.10e-19

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: 84.66  E-value: 4.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKldETKKEILEKYSSIEVRTAAFDFTNaapsaYKDLLATLNQV---- 125
Cdd:cd05323    3 AIITGGASGIGLATAKLLLKKGAKVAILDRNENP--GAAAELQAINPKVKATFVQCDVTS-----WEQLAAAFKKAiekf 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 -EIGVLINNVGMSYEYP-DVLHKVDGGIERLANIT---TINTlppTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWA 200
Cdd:cd05323   76 gRVDILINNAGILDEKSyLFAGKLPPPWEKTIDVNltgVINT---TYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFP 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 392895268 201 VYSATKKYVSWLTAILRKEYEHQ-GITVQTIAPMMVATKM 239
Cdd:cd05323  153 VYSASKHGVVGFTRSLADLLEYKtGVRVNAICPGFTNTPL 192
PRK07201 PRK07201
SDR family oxidoreductase;
51-239 4.17e-19

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 87.70  E-value: 4.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAafDFTNAAPSAY--KDLLATLNQVEIg 128
Cdd:PRK07201 375 LITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAYTC--DLTDSAAVDHtvKDILAEHGHVDY- 451
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 vLINNVGMS-----YEYPDVLHKvdggIERlanITTINTLPPTLLSAGILPQMVARKAGVIVNVgSSAG--ANQMALWAv 201
Cdd:PRK07201 452 -LVNNAGRSirrsvENSTDRFHD----YER---TMAVNYFGAVRLILGLLPHMRERRFGHVVNV-SSIGvqTNAPRFSA- 521
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895268 202 YSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK07201 522 YVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTPM 559
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
50-239 8.70e-19

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: 83.86  E-value: 8.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLL-VSRTQSKLDETKKEILEK----------YSSIEVRTAAFDFTNAAPSaykdl 118
Cdd:cd05362    6 ALVTGASRGIGRAIAKRLARDGASVVVnYASSKAAAEEVVAEIEAAggkaiavqadVSDPSQVARLFDAAEKAFG----- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 119 latlnqvEIGVLINNVGMSyeypDVLHKVDGGIERLANITTINTLPPTLLSAGILPQMvaRKAGVIVNVGSSAGANQMAL 198
Cdd:cd05362   81 -------GVDILVNNAGVM----LKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPN 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392895268 199 WAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:cd05362  148 YGAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDM 188
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
50-232 1.27e-18

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 83.46  E-value: 1.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRtqSKL-DETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLATLNQVEIg 128
Cdd:PRK12823  11 VVVTGAAQGIGRGVALRAAAEGARVVLVDR--SELvHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRIDV- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 vLINNVGMS-----YEYPDVlHKVDGGIERlanittinTLPPTLLSA-GILPQMVARKAGVIVNVGSSA--GANQMAlwa 200
Cdd:PRK12823  88 -LINNVGGTiwakpFEEYEE-EQIEAEIRR--------SLFPTLWCCrAVLPHMLAQGGGAIVNVSSIAtrGINRVP--- 154
                        170       180       190
                 ....*....|....*....|....*....|..
gi 392895268 201 vYSATKKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:PRK12823 155 -YSAAKGGVNALTASLAFEYAEHGIRVNAVAP 185
FabG-like PRK07231
SDR family oxidoreductase;
50-241 1.51e-18

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 83.34  E-value: 1.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDftnaaPSAYKDLLATLNQV--EI 127
Cdd:PRK07231   8 AIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGGRAIAVAADVSD-----EADVEAAVAAALERfgSV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYEYpDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:PRK07231  83 DILVNNAGTTHRN-GPLLDVD--EAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKG 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:PRK07231 160 AVITLTKALAAELGPDKIRVNAVAPVVVETGLLE 193
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
50-239 1.55e-18

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: 82.97  E-value: 1.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLATLNQVEIgv 129
Cdd:cd08934    6 ALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGRLDI-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 LINNVGMSyeypdVLHKVDGG-IERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKY 208
Cdd:cd08934   84 LVNNAGIM-----LLGPVEDAdTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFG 158
                        170       180       190
                 ....*....|....*....|....*....|.
gi 392895268 209 VSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:cd08934  159 VNAFSEGLRQEVTERGVRVVVIEPGTVDTEL 189
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
50-241 1.90e-18

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: 82.73  E-value: 1.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFN-VLLVSRTQSKLDETKKeILEKYSSIEVRTAafDFTNAAPSAYKDLLATLNQVEIG 128
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGNNtVIATCRDPSAATELAA-LGASHSRLHILEL--DVTDEIAESAEAVAERLGDAGLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 VLINNVGMSYEYPdvlHKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGS---SAGANQMALWAVYSAT 205
Cdd:cd05325   78 VLINNAGILHSYG---PASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSrvgSIGDNTSGGWYSYRAS 154
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 392895268 206 KKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:cd05325  155 KAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGG 190
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
49-237 2.23e-18

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: 82.71  E-value: 2.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  49 WAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIleKYSSIEVRTAAFDFTNA--APSAYKDLLATLNQVE 126
Cdd:cd05344    3 VALVTAASSGIGLAIARALAREGARVAICARNRENLERAASEL--RAGGAGVLAVVADLTDPedIDRLVEKAGDAFGRVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IgvLINNVGmsyeypdvlhkvDGGIERLANIT--------TINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMAL 198
Cdd:cd05344   81 I--LVNNAG------------GPPPGPFAELTdedwleafDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPN 146
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 392895268 199 WAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:cd05344  147 LVLSNVARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDT 185
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
50-242 3.63e-18

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 82.16  E-value: 3.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSsIEVRTAAFDFTNAAP--SAYKDLLATLNQVEI 127
Cdd:PRK05557   8 ALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALG-GKALAVQGDVSDAESveRAVDEAKAEFGGVDI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gvLINNVGMSyeypdvlhkVDGGIERL-----ANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVY 202
Cdd:PRK05557  87 --LVNNAGIT---------RDNLLMRMkeedwDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANY 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 392895268 203 SATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKV 242
Cdd:PRK05557 156 AASKAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDA 195
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
50-241 8.70e-18

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: 80.96  E-value: 8.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKysSIEVRTAAFDFTNAapSAYKDLLATLNQV---E 126
Cdd:cd05329    9 ALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREK--GFKVEGSVCDVSSR--SERQELMDTVASHfggK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IGVLINNVGMsyeypdVLHK--VDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSA 204
Cdd:cd05329   85 LNILVNNAGT------NIRKeaKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGA 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 392895268 205 TKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:cd05329  159 TKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVE 195
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
49-241 1.89e-17

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: 80.35  E-value: 1.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  49 WAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKY--SSIEVRTAafDFTNAA--PSAYKDLLATLNQ 124
Cdd:cd05327    3 VVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETgnAKVEVIQL--DLSSLAsvRQFAEEFLARFPR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 125 VEIgvLINNVGMSY----EYPDvlhkvdgGIER-LAnittINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGA-----N 194
Cdd:cd05327   81 LDI--LINNAGIMApprrLTKD-------GFELqFA----VNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRagpidF 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392895268 195 QMAL---------WAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:cd05327  148 NDLDlennkeyspYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLR 203
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
50-239 2.38e-17

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: 79.59  E-value: 2.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSsiEVRTAAFDFTNaapsaYKDLLATLNQV---- 125
Cdd:cd05339    2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGG--KVHYYKCDVSK-----REEVYEAAKKIkkev 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 -EIGVLINNVGMSYEYPdVLHKVDGGIERLANittINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSA 204
Cdd:cd05339   75 gDVTILINNAGVVSGKK-LLELPDEEIEKTFE---VNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCA 150
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895268 205 TKKYVSWLTAILRKE---YEHQGITVQTIAPMMVATKM 239
Cdd:cd05339  151 SKAAAVGFHESLRLElkaYGKPGIKTTLVCPYFINTGM 188
PRK06124 PRK06124
SDR family oxidoreductase;
50-237 8.09e-17

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 78.60  E-value: 8.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVrtAAFDFTN--AAPSAYKDLLATLNQVEI 127
Cdd:PRK06124  14 ALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEA--LAFDIADeeAVAAAFARIDAEHGRLDI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gvLINNVGMSYEYPdVLHKVDGGIERLANIttiNTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:PRK06124  92 --LVNNVGARDRRP-LAELDDAAIRALLET---DLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAKQ 165
                        170       180       190
                 ....*....|....*....|....*....|
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK06124 166 GLTGLMRALAAEFGPHGITSNAIAPGYFAT 195
PRK06484 PRK06484
short chain dehydrogenase; Validated
50-239 8.73e-17

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 80.66  E-value: 8.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDftnAAPSAYKDLLATLNQVEigV 129
Cdd:PRK06484   8 VLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEA---QIREGFEQLHREFGRID--V 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 LINNVGMSYEYPDVLhkVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGV-IVNVGSSAGANQMALWAVYSATKKY 208
Cdd:PRK06484  83 LVNNAGVTDPTMTAT--LDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYSASKAA 160
                        170       180       190
                 ....*....|....*....|....*....|.
gi 392895268 209 VSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK06484 161 VISLTRSLACEWAAKGIRVNAVLPGYVRTQM 191
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
52-268 9.34e-17

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 78.26  E-value: 9.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  52 VTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKyssieVRTAAFDFTNAApsAYKDLLATLNQV--EIGV 129
Cdd:PRK10538   5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDN-----LYIAQLDVRNRA--AIEEMLASLPAEwrNIDV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 LINNVGMSYEYpDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKYV 209
Cdd:PRK10538  78 LVNNAGLALGL-EPAHKAS--VEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFV 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 210 SWLTAILRKEYEHQGITVQTIAPMMVA-TKMSKVKrtsfFTPDGAVFAKSALNTVGNTSD 268
Cdd:PRK10538 155 RQFSLNLRTDLHGTAVRVTDIEPGLVGgTEFSNVR----FKGDDGKAEKTYQNTVALTPE 210
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
51-248 1.47e-16

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: 77.23  E-value: 1.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlEKYSSIEVRTAAFDFTNAAPSAYKDLlATLNQVEIGVL 130
Cdd:cd05340    8 LVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHI-NEEGGRQPQWFILDLLTCTSENCQQL-AQRIAVNYPRL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 131 ---INNVGMSYEYPDVLHKVDggiERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:cd05340   86 dgvLHNAGLLGDVCPLSEQNP---QVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSKF 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVATKMskvkRTSFF 248
Cdd:cd05340  163 ATEGL*QVLADEYQQRNLRVNCINPGGTRTAM----RASAF 199
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
50-240 1.64e-16

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: 77.16  E-value: 1.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKyssieVRTAAFDFTNAApsAYKDLLATLNQV--EI 127
Cdd:cd08929    3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEG-----VLGLAGDVRDEA--DVRRAVDAMEEAfgGL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYEYPdvlhkvdggIERLANITTINTLPPTLLSAGI-----LPQMVARKAGVIVNVGSSAGANQMALWAVY 202
Cdd:cd08929   76 DALVNNAGVGVMKP---------VEELTPEEWRLVLDTNLTGAFYcihkaAPALLRRGGGTIVNVGSLAGKNAFKGGAAY 146
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895268 203 SATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMS 240
Cdd:cd08929  147 NASKFGLLGLSEAAMLDLREANIRVVNVMPGSVDTGFA 184
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
51-253 1.95e-16

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: 76.94  E-value: 1.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFN--VLLVSRTQSKLDETKKEIlekYSSIEVRTAAFDFTNAApsAYKDLLATLNQV--E 126
Cdd:cd05367    3 ILTGASRGIGRALAEELLKRGSPsvVVLLARSEEPLQELKEEL---RPGLRVTTVKADLSDAA--GVEQLLEAIRKLdgE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IGVLINNVGMSYeypDVLHKVDGGIERLANITTINTLPPTLLSAGILPQMVARKA-GVIVNVGSSAGANQMALWAVYSAT 205
Cdd:cd05367   78 RDLLINNAGSLG---PVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLYCSS 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 392895268 206 KKYVSWLTAILRKEYehQGITVQTIAPMMVATKMSKVKRTSFFTPDGA 253
Cdd:cd05367  155 KAARDMFFRVLAAEE--PDVRVLSYAPGVVDTDMQREIRETSADPETR 200
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
50-271 2.30e-16

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: 77.50  E-value: 2.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEK-YSSIEVRTAAFDFTNAApSAYKDLLATLNQVEIg 128
Cdd:cd08935    8 AVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALgGRAIALAADVLDRASLE-RAREEIVAQFGTVDI- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 vLINNVG----------MSYEYPDVLHKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMAL 198
Cdd:cd08935   86 -LINGAGgnhpdattdpEHYEPETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSPLTK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 199 WAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSkvkRTSFFTPDG-------AVFAKSALNTVGNTSDTTG 271
Cdd:cd08935  165 VPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQN---RKLLINPDGsytdrsnKILGRTPMGRFGKPEELLG 241
PRK09242 PRK09242
SDR family oxidoreductase;
50-241 2.52e-16

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 77.09  E-value: 2.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAapsayKDLLATLNQVE--- 126
Cdd:PRK09242  12 ALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEFPEREVHGLAADVSDD-----EDRRAILDWVEdhw 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 --IGVLINNVGMSyeypdvLHK--VDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVY 202
Cdd:PRK09242  87 dgLHILVNNAGGN------IRKaaIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPY 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 392895268 203 SATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:PRK09242 161 GMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTS 199
PRK12826 PRK12826
SDR family oxidoreductase;
50-239 3.32e-16

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 76.49  E-value: 3.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRtaAFDFTNAApsaykDLLATLNQVE--- 126
Cdd:PRK12826   9 ALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARAR--QVDVRDRA-----ALKAAVAAGVedf 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 --IGVLINNVGMSyeyPDVLHkVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAG-ANQMALWAVYS 203
Cdd:PRK12826  82 grLDILVANAGIF---PLTPF-AEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGpRVGYPGLAHYA 157
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 392895268 204 ATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK12826 158 ASKAGLVGFTRALALELAARNITVNSVHPGGVDTPM 193
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
50-253 5.03e-16

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: 75.74  E-value: 5.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFN-VLLVSRTQSKLDETKKEILEKYSSIEVRtaAFDFTNAAP--SAYKDLLATLNQVE 126
Cdd:cd05324    3 ALVTGANRGIGFEIVRQLAKSGPGtVILTARDVERGQAAVEKLRAEGLSVRFH--QLDVTDDASieAAADFVEEKYGGLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IgvLINNVGMSYE-YPDVLHKVDggierLANIT-TINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGanqmALWAVYSA 204
Cdd:cd05324   81 I--LVNNAGIAFKgFDDSTPTRE-----QARETmKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLG----SLTSAYGV 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 392895268 205 TKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKrtSFFTPD-GA 253
Cdd:cd05324  150 SKAALNALTRILAKELKETGIKVNACCPGWVKTDMGGGK--APKTPEeGA 197
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
50-242 6.80e-16

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 75.75  E-value: 6.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIleKYSSIEVRTAAFDFTNAAPSA--YKDLLATLNQVEI 127
Cdd:PRK08213  15 ALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHL--EALGIDALWIAADVADEADIErlAEETLERFGHVDI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gvLINNVGMSYEYPDVLHKVDgGIERLANITTINTLpptLLSAGILPQ-MVARKAGVIVNVGSSAGAN-----QMALWAv 201
Cdd:PRK08213  93 --LVNNAGATWGAPAEDHPVE-AWDKVMNLNVRGLF---LLSQAVAKRsMIPRGYGRIINVASVAGLGgnppeVMDTIA- 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392895268 202 YSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKV 242
Cdd:PRK08213 166 YNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRG 206
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
50-238 1.33e-15

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 75.16  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTqSKLDETKKEIlEKyssiEVRTAAF---DFTN--AAPSAYKDLLATLNQ 124
Cdd:PRK06935  18 AIVTGGNTGLGQGYAVALAKAGADIIITTHG-TNWDETRRLI-EK----EGRKVTFvqvDLTKpeSAEKVVKEALEEFGK 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 125 VEIgvLINNVGMSYEYPdVLHKVDGGIERLANItTINTLppTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSA 204
Cdd:PRK06935  92 IDI--LVNNAGTIRRAP-LLEYKDEDWNAVMDI-NLNSV--YHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVPAYTA 165
                        170       180       190
                 ....*....|....*....|....*....|....
gi 392895268 205 TKKYVSWLTAILRKEYEHQGITVQTIAPMMVATK 238
Cdd:PRK06935 166 SKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTA 199
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
50-243 1.53e-15

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: 74.79  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSklDETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLATLNQvEIG- 128
Cdd:cd08940    5 ALVTGSTSGIGLGIARALAAAGANIVLNGFGDA--AEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQR-QFGg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 --VLINNVGMSY-----EYPdvlhkvdggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAV 201
Cdd:cd08940   82 vdILVNNAGIQHvapieDFP---------TEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSA 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 392895268 202 YSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVK 243
Cdd:cd08940  153 YVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVEKQ 194
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
50-237 2.20e-15

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: 74.47  E-value: 2.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEK-YSSIEVRTAafDFTNAapsayKDLLATLNQVE-- 126
Cdd:cd05343    9 ALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAgYPTLFPYQC--DLSNE-----EQILSMFSAIRtq 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 ---IGVLINNVGMSyeYPDVLhkVDGGIERLANITTINTLPPTLLSAGILPQMVARKA--GVIVNVGSSAGAN--QMALW 199
Cdd:cd05343   82 hqgVDVCINNAGLA--RPEPL--LSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVddGHIININSMSGHRvpPVSVF 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 392895268 200 AVYSATKKYVSWLTAILRKE--YEHQGITVQTIAPMMVAT 237
Cdd:cd05343  158 HFYAATKHAVTALTEGLRQElrEAKTHIRATSISPGLVET 197
PRK12939 PRK12939
short chain dehydrogenase; Provisional
50-239 2.63e-15

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 74.24  E-value: 2.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKysSIEVRTAAFDFTNAAPsaykdLLATLNQVE--- 126
Cdd:PRK12939  10 ALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAA--GGRAHAIAADLADPAS-----VQRFFDAAAaal 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 --IGVLINNVGMSyeypDVLHKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSA 204
Cdd:PRK12939  83 ggLDGLVNNAGIT----NSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVA 158
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 392895268 205 TKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK12939 159 SKGAVIGMTRSLARELGGRGITVNAIAPGLTATEA 193
PRK08251 PRK08251
SDR family oxidoreductase;
51-247 3.29e-15

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 73.82  E-value: 3.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTN--AAPSAYKDLLATLNQveIG 128
Cdd:PRK08251   6 LITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARYPGIKVAVAALDVNDhdQVFEVFAEFRDELGG--LD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 VLINNVGMSYEYPdvlhkVDGGIERlANITTINTlppTLLSAgiLPQMVA-------RKAGVIVNVGSSAGANQM--ALw 199
Cdd:PRK08251  84 RVIVNAGIGKGAR-----LGTGKFW-ANKATAET---NFVAA--LAQCEAameifreQGSGHLVLISSVSAVRGLpgVK- 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 392895268 200 AVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMS-KVKRTSF 247
Cdd:PRK08251 152 AAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNaKAKSTPF 200
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
50-237 4.17e-15

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: 73.60  E-value: 4.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEK-YSSIEVRTAAFDFTNAapsayKDLLATLNQV--- 125
Cdd:cd05364    6 AIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAgVSEKKILLVVADLTEE-----EGQDRIISTTlak 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 --EIGVLINNVGMSyeYPDVLHkvDGGIERLANITTINTLPPTLLSAGILPQMVARKaGVIVNVGSSAGANQMALWAVYS 203
Cdd:cd05364   81 fgRLDILVNNAGIL--AKGGGE--DQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGGRSFPGVLYYC 155
                        170       180       190
                 ....*....|....*....|....*....|....
gi 392895268 204 ATKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:cd05364  156 ISKAALDQFTRCTALELAPKGVRVNSVSPGVIVT 189
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
36-240 4.66e-15

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: 73.52  E-value: 4.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  36 LSPIDLKKRAgaswAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSsieVRTAAF--DFTNaaps 113
Cdd:cd05352    1 LDLFSLKGKV----AIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYG---VKTKAYkcDVSS---- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 114 aYKDLLATLNQVE-----IGVLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVG 188
Cdd:cd05352   70 -QESVEKTFKQIQkdfgkIDILIANAGITVHKP----ALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITA 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392895268 189 SSAG--ANQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMS 240
Cdd:cd05352  145 SMSGtiVNRPQPQAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLT 198
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
51-241 6.55e-15

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 73.07  E-value: 6.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIleKYSSIEVRTAAFDFTNAApsaykDLLATLNQVE---- 126
Cdd:PRK08217   9 VITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAEC--GALGTEVRGYAANVTDEE-----DVEATFAQIAedfg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 -IGVLINNVGMSYEypDVLHKV-DGGIER---LANI-TTINT-LPPTLL---SAGIlpQMV-ARKAGVIVNVGSSAGANQ 195
Cdd:PRK08217  82 qLNGLINNAGILRD--GLLVKAkDGKVTSkmsLEQFqSVIDVnLTGVFLcgrEAAA--KMIeSGSKGVIINISSIARAGN 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 392895268 196 MAlWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:PRK08217 158 MG-QTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTA 202
PRK08703 PRK08703
SDR family oxidoreductase;
51-221 6.83e-15

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 72.66  E-value: 6.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKySSIEVRTAAFDFTNAAPSAYKDLLATLNQVEIGVL 130
Cdd:PRK08703  10 LVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEA-GHPEPFAIRFDLMSAEEKEFEQFAATIAEATQGKL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 131 INNVGMSYEYPDVLHKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKYVS 210
Cdd:PRK08703  89 DGIVHCAGYFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGGFGASKAALN 168
                        170
                 ....*....|.
gi 392895268 211 WLTAILRKEYE 221
Cdd:PRK08703 169 YLCKVAADEWE 179
PRK06181 PRK06181
SDR family oxidoreductase;
50-241 8.07e-15

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 73.09  E-value: 8.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSsiEVRTAAFDFTNAapSAYKDLLATLnqVE--- 126
Cdd:PRK06181   4 VIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGG--EALVVPTDVSDA--EACERLIEAA--VArfg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 -IGVLINNVGMSY-------EYPDVLHKVdggierlaniTTINTLPPTLLSAGILPQMVARKaGVIVNVGSSAGANQMAL 198
Cdd:PRK06181  78 gIDILVNNAGITMwsrfdelTDLSVFERV----------MRVNYLGAVYCTHAALPHLKASR-GQIVVVSSLAGLTGVPT 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 392895268 199 WAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:PRK06181 147 RSGYAASKHALHGFFDSLRIELADDGVAVTVVCPGFVATDIRK 189
PRK07825 PRK07825
short chain dehydrogenase; Provisional
51-240 9.75e-15

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 73.05  E-value: 9.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlekyssIEVRTAAFDFTNAAPSAykdllATLNQVE---- 126
Cdd:PRK07825   9 AITGGARGIGLATARALAALGARVAIGDLDEALAKETAAEL------GLVVGGPLDVTDPASFA-----AFLDAVEadlg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 -IGVLINNVGMSYEYPdVLHKVDGGIERlanITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSAT 205
Cdd:PRK07825  78 pIDVLVNNAGVMPVGP-FLDEPDAVTRR---ILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCAS 153
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 392895268 206 KKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMS 240
Cdd:PRK07825 154 KHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELI 188
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
50-242 1.09e-14

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: 72.12  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlEKYSSIEVRTAAFDFTNAApsaykdlLATLNQVEIgv 129
Cdd:cd05351   10 ALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVREC-PGIEPVCVDLSDWDATEEA-------LGSVGPVDL-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 LINNVGMSYEYPdVLHKVDGGIERLANittINTLPPTLLSAGILPQMVARKA-GVIVNVGSSAGANQMALWAVYSATKKY 208
Cdd:cd05351   80 LVNNAAVAILQP-FLEVTKEAFDRSFD---VNVRAVIHVSQIVARGMIARGVpGSIVNVSSQASQRALTNHTVYCSTKAA 155
                        170       180       190
                 ....*....|....*....|....*....|....
gi 392895268 209 VSWLTAILRKEYEHQGITVQTIAPMMVATKMSKV 242
Cdd:cd05351  156 LDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRD 189
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
51-239 1.14e-14

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: 72.55  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAP-SAYKDllATLNQV-EIG 128
Cdd:cd05330    7 LITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPDAEVLLIKADVSDEAQvEAYVD--ATVEQFgRID 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 VLINNVGMSYEYPDVlhkVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAG----ANQMAlwavYSA 204
Cdd:cd05330   85 GFFNNAGIEGKQNLT---EDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGirgvGNQSG----YAA 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 392895268 205 TKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:cd05330  158 AKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPM 192
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
51-237 1.30e-14

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: 72.03  E-value: 1.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAafDFTNAAPSAYKDLLATLNQVEIGVL 130
Cdd:cd05360    4 VITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVA--DVADAAQVERAADTAVERFGRIDTW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 131 INNVGMSYeypdVLHKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKYVS 210
Cdd:cd05360   82 VNNAGVAV----FGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVR 157
                        170       180
                 ....*....|....*....|....*....
gi 392895268 211 WLTAILRKEYEHQG--ITVQTIAPMMVAT 237
Cdd:cd05360  158 GFTESLRAELAHDGapISVTLVQPTAMNT 186
PRK12743 PRK12743
SDR family oxidoreductase;
50-239 1.33e-14

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 72.37  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSK-LDETKKEILEKYSSIEVRTaaFDFTNA--APSAYKDLLATLNQve 126
Cdd:PRK12743   5 AIVTASDSGIGKACALLLAQQGFDIGITWHSDEEgAKETAEEVRSHGVRAEIRQ--LDLSDLpeGAQALDKLIQRLGR-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IGVLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVAR-KAGVIVNVGSSAGANQMALWAVYSAT 205
Cdd:PRK12743  81 IDVLVNNAGAMTKAP----FLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHEHTPLPGASAYTAA 156
                        170       180       190
                 ....*....|....*....|....*....|....
gi 392895268 206 KKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK12743 157 KHALGGLTKAMALELVEHGILVNAVAPGAIATPM 190
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
50-241 2.22e-14

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: 71.55  E-value: 2.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSK-LDETKKEILEKYSSIEVRTAAfDFTNAAPSA---YKDLLATLNQV 125
Cdd:cd05371    5 AVVTGGASGLGLATVERLLAQGAKVVILDLPNSPgETVAKLGDNCRFVPVDVTSEK-DVKAALALAkakFGRLDIVVNCA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 EIGVLINNVGMSYEYPDVLHKvdggIERLANITTINTLPPTLLSAGilpQMVARKA------GVIVNVGSSAGANQMALW 199
Cdd:cd05371   84 GIAVAAKTYNKKGQQPHSLEL----FQRVINVNLIGTFNVIRLAAG---AMGKNEPdqggerGVIINTASVAAFEGQIGQ 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 392895268 200 AVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:cd05371  157 AAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLA 198
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
40-232 2.51e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 71.34  E-value: 2.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  40 DLKKRAgaswAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIleKYSSIEVRTAAFDFTN--AAPSAYKD 117
Cdd:PRK07523   7 DLTGRR----ALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESL--KGQGLSAHALAFDVTDhdAVRAAIDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 118 LLATLNQVEIgvLINNVGMSYEYPDVLHKVDgGIERL--ANITTINTlpptlLSAGILPQMVARKAGVIVNVGSSAGANQ 195
Cdd:PRK07523  81 FEAEIGPIDI--LVNNAGMQFRTPLEDFPAD-AFERLlrTNISSVFY-----VGQAVARHMIARGAGKIINIASVQSALA 152
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 392895268 196 MALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:PRK07523 153 RPGIAPYTATKGAVGNLTKGMATDWAKHGLQCNAIAP 189
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
52-239 2.59e-14

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 71.06  E-value: 2.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  52 VTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlEKYSSIEVRTAAFDFTNAAPSAYKDLLATLNQvEIGVL- 130
Cdd:PRK08945  17 VTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEI-EAAGGPQPAIIPLDLLTATPQNYQQLADTIEE-QFGRLd 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 131 --INNVG-------MSYEYPDVLHKVdggierlaniTTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAV 201
Cdd:PRK08945  95 gvLHNAGllgelgpMEQQDPEVWQDV----------MQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANWGA 164
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895268 202 YSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK08945 165 YAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAM 202
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
50-240 3.36e-14

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: 70.95  E-value: 3.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQS-KLDETKKEILekysSIEVRTAAFDFTNAAPSAYKDLL-ATLNQV-E 126
Cdd:cd05337    4 AIVTGASRGIGRAIATELAARGFDIAINDLPDDdQATEVVAEVL----AAGRRAIYFQADIGELSDHEALLdQAWEDFgR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IGVLINNVGMSY-EYPDVLHKVDGGIERLANittINTLPPTLLSAGILPQMVARKA------GVIVNVGSSAGANQMALW 199
Cdd:cd05337   80 LDCLVNNAGIAVrPRGDLLDLTEDSFDRLIA---INLRGPFFLTQAVARRMVEQPDrfdgphRSIIFVTSINAYLVSPNR 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392895268 200 AVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMS 240
Cdd:cd05337  157 GEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMT 197
PRK06172 PRK06172
SDR family oxidoreductase;
50-264 3.65e-14

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 70.94  E-value: 3.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSsiEVRTAAFDFTNAApsAYKDLLA-TLNQV-EI 127
Cdd:PRK06172  10 ALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGG--EALFVACDVTRDA--EVKALVEqTIAAYgRL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYEYPDVlhkVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:PRK06172  86 DYAFNNAGIEIEQGRL---AEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKH 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVATKMskVKRTSFFTPDGAVFAkSALNTVG 264
Cdd:PRK06172 163 AVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDM--FRRAYEADPRKAEFA-AAMHPVG 216
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
50-247 4.83e-14

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: 70.64  E-value: 4.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEkySSIEVRTAAFDFTNaaPSAYKDLLATLNQV--EI 127
Cdd:cd08945    6 ALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELRE--AGVEADGRTCDVRS--VPEIEALVAAAVARygPI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYeypdvlhkvDGGIERLA----------NITTINTLPPTLLSAGilpQMVARKAGVIVNVGSSAGANQMA 197
Cdd:cd08945   82 DVLVNNAGRSG---------GGATAELAdelwldvvetNLTGVFRVTKEVLKAG---GMLERGTGRIINIASTGGKQGVV 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 392895268 198 LWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTSF 247
Cdd:cd08945  150 HAAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAASVREHY 199
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
50-239 1.05e-13

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 69.51  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSR-TQSKLDETKKEIleKYSSIEVRTAAFDFTNAApsaykDLLATLNQVE-- 126
Cdd:PRK12825   9 ALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAV--EALGRRAQAVQADVTDKA-----ALEAAVAAAVer 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 ---IGVLINNVG---------MS-YEYPDVlhkVDGgierlaNIT-TINTLPPTLlsagilPQMVARKAGVIVNVGSSAG 192
Cdd:PRK12825  82 fgrIDILVNNAGifedkpladMSdDEWDEV---IDV------NLSgVFHLLRAVV------PPMRKQRGGRIVNISSVAG 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 392895268 193 ANQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK12825 147 LPGWPGRSNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDM 193
PRK12937 PRK12937
short chain dehydrogenase; Provisional
50-239 1.35e-13

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 69.00  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLL-VSRTQSKLDETKKEILEKYSsievRTAAFDFTNAAPSAYKDLLATLNQV--E 126
Cdd:PRK12937   8 AIVTGASRGIGAAIARRLAADGFAVAVnYAGSAAAADELVAEIEAAGG----RAIAVQADVADAAAVTRLFDAAETAfgR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IGVLINNVG-MSYEYPDvlhkvDGGIERLANITTINtLPPTLLSAG-ILPQMvaRKAGVIVNVGSSAGANQMALWAVYSA 204
Cdd:PRK12937  84 IDVLVNNAGvMPLGTIA-----DFDLEDFDRTIATN-LRGAFVVLReAARHL--GQGGRIINLSTSVIALPLPGYGPYAA 155
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 392895268 205 TKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK12937 156 SKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
50-239 1.45e-13

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: 69.04  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLvsrtqSKLDETKKEILEKYSSIEVRTAafDFTNAApsaykDLLATLNQVE-IG 128
Cdd:cd05368    5 ALITAAAQGIGRAIALAFAREGANVIA-----TDINEEKLKELERGPGITTRVL--DVTDKE-----QVAALAKEEGrID 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 VLINNVGMSYeYPDVLHKVDGGIERLANittINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGA-----NQMalwaVYS 203
Cdd:cd05368   73 VLFNCAGFVH-HGSILDCEDDDWDFAMN---LNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSikgvpNRF----VYS 144
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 392895268 204 ATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:cd05368  145 TTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPS 180
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
50-237 1.63e-13

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 69.14  E-value: 1.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKysSIEVRTAAFDFTNaaPSAYKDLLA----TLNQV 125
Cdd:PRK12429   7 ALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKA--GGKAIGVAMDVTD--EEAINAGIDyaveTFGGV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 EIgvLINNVGMSY-----EYPdvlhkvdggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWA 200
Cdd:PRK12429  83 DI--LVNNAGIQHvapieDFP---------TEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKA 151
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 392895268 201 VYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK12429 152 AYVSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDT 188
PRK08219 PRK08219
SDR family oxidoreductase;
50-239 2.28e-13

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 68.04  E-value: 2.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRgFNVLLVSRTQSKLDETKKEIlekyssIEVRTAAFDFTNAAPSAYkdllATLNQVEIGV 129
Cdd:PRK08219   6 ALITGASRGIGAAIARELAPT-HTLLLGGRPAERLDELAAEL------PGATPFPVDLTDPEAIAA----AVEQLGRLDV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 LINNVGMSYeypdvLHKV-DGGIERLANITTINTLPPTLLSAGILPQMVARKaGVIVNVGSSAGANQMALWAVYSATKKY 208
Cdd:PRK08219  75 LVHNAGVAD-----LGPVaESTVDEWRATLEVNVVAPAELTRLLLPALRAAH-GHVVFINSGAGLRANPGWGSYAASKFA 148
                        170       180       190
                 ....*....|....*....|....*....|.
gi 392895268 209 VSWLTAILRKEyEHQGITVQTIAPMMVATKM 239
Cdd:PRK08219 149 LRALADALREE-EPGNVRVTSVHPGRTDTDM 178
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
50-252 2.60e-13

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 68.77  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEK-YSSIEVRTAAFDFTNAApSAYKDLLATLNQVEIg 128
Cdd:PRK08277  13 AVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAgGEALAVKADVLDKESLE-QARQQILEDFGPCDI- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 vLINNVG-----------MSYEYPDVLHKVD---GGIERLANITTINTLPPTLLSAgilPQMVARKAGVIVNVGSSAGAN 194
Cdd:PRK08277  91 -LINGAGgnhpkattdneFHELIEPTKTFFDldeEGFEFVFDLNLLGTLLPTQVFA---KDMVGRKGGNIINISSMNAFT 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392895268 195 QMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSkvkRTSFFTPDG 252
Cdd:PRK08277 167 PLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQN---RALLFNEDG 221
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
50-253 2.62e-13

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: 68.29  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVrtaafDFTNAapSAYKDLLATLNQVEIGV 129
Cdd:cd08944    6 AIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRV-----DVTDE--QQVAALFERAVEEFGGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 --LINNVGMSYEYPDVLhkvDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:cd08944   79 dlLVNNAGAMHLTPAII---DTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKA 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTSFFTPDGA 253
Cdd:cd08944  156 AIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEGALGP 201
PRK07774 PRK07774
SDR family oxidoreductase;
50-242 2.89e-13

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 68.23  E-value: 2.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEK-YSSIEVRTAAFDFTNAAPSAYkdllATLNQV-EI 127
Cdd:PRK07774   9 AIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADgGTAIAVQVDVSDPDSAKAMAD----ATVSAFgGI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINN----VGMSyeyPDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNvGSSAGAnqmalW---A 200
Cdd:PRK07774  85 DYLVNNaaiyGGMK---LDLLITVP--WDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVN-QSSTAA-----WlysN 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 392895268 201 VYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKV 242
Cdd:PRK07774 154 FYGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRT 195
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
51-239 6.49e-13

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 67.34  E-value: 6.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDEtkkeilEKYSSIEVrtaafDFTNAApsAYKDLLATLNQV--EIG 128
Cdd:PRK06171  13 IVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQH------ENYQFVPT-----DVSSAE--EVNHTVAEIIEKfgRID 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 VLINNVGMSYeyPDVLhkVD-----GGIERLAN----ITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALW 199
Cdd:PRK06171  80 GLVNNAGINI--PRLL--VDekdpaGKYELNEAafdkMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQ 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392895268 200 AVYSATKKYVSWLTAILRKEYEHQGITVQTIAP-MMVATKM 239
Cdd:PRK06171 156 SCYAATKAALNSFTRSWAKELGKHNIRVVGVAPgILEATGL 196
PRK07063 PRK07063
SDR family oxidoreductase;
50-237 6.62e-13

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 67.38  E-value: 6.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAApsaykDLLATLNQVE--- 126
Cdd:PRK07063  10 ALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVAGARVLAVPADVTDAA-----SVAAAVAAAEeaf 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 --IGVLINNVGMSYeYPDVLHKVDGGIERLANIttintlppTLLSA-----GILPQMVARKAGVIVNVGSSAGANQMALW 199
Cdd:PRK07063  85 gpLDVLVNNAGINV-FADPLAMTDEDWRRCFAV--------DLDGAwngcrAVLPGMVERGRGSIVNIASTHAFKIIPGC 155
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895268 200 AVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK07063 156 FPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIET 193
PRK08267 PRK08267
SDR family oxidoreductase;
52-239 7.37e-13

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 67.27  E-value: 7.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  52 VTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlekySSIEVRTAAFDFTNAApsAYKDLLA---TLNQVEIG 128
Cdd:PRK08267   6 ITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAEL----GAGNAWTGALDVTDRA--AWDAALAdfaAATGGRLD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 VLINNVGMSYEYPdvLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKY 208
Cdd:PRK08267  80 VLFNNAGILRGGP--FEDIP--LEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFA 155
                        170       180       190
                 ....*....|....*....|....*....|.
gi 392895268 209 VSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK08267 156 VRGLTEALDLEWRRHGIRVADVMPLFVDTAM 186
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
50-246 8.81e-13

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 67.02  E-value: 8.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKldetkkeilEKYSSIEVRTAAFDFTN-------AAPSAYKDLLATL 122
Cdd:PRK06924   4 VIITGTSQGLGEAIANQLLEKGTHVISISRTENK---------ELTKLAEQYNSNLTFHSldlqdvhELETNFNEILSSI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 123 NQVEIG--VLINNVGMsyeypdvlhkVDgGIERLANIT--------TINTLPPTLLSAGILPQMVARKAG-VIVNVGSSA 191
Cdd:PRK06924  75 QEDNVSsiHLINNAGM----------VA-PIKPIEKAEseelitnvHLNLLAPMILTSTFMKHTKDWKVDkRVINISSGA 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 392895268 192 GANQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIA--PMMVATKMSKVKRTS 246
Cdd:PRK06924 144 AKNPYFGWSAYCSSKAGLDMFTQTVATEQEEEEYPVKIVAfsPGVMDTNMQAQIRSS 200
PRK07326 PRK07326
SDR family oxidoreductase;
50-237 1.30e-12

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 66.19  E-value: 1.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEiLEKYSsiEVRTAAFDFTNAAP--SAYKDLLATLNQVEi 127
Cdd:PRK07326   9 ALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAE-LNNKG--NVLGLAADVRDEADvqRAVDAIVAAFGGLD- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gVLINNVGmsyeypdvlhkvdggierLANITTINTLPP--------TLLSaGI-------LPQMvARKAGVIVNVGSSAG 192
Cdd:PRK07326  85 -VLIANAG------------------VGHFAPVEELTPeewrlvidTNLT-GAfytikaaVPAL-KRGGGYIINISSLAG 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 392895268 193 ANQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK07326 144 TNFFAGGAAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVAT 188
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
50-271 1.84e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 66.24  E-value: 1.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKysSIEVRTAAFDFTNAApsAYKDLLATLnQVEIGV 129
Cdd:PRK07097  13 ALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYREL--GIEAHGYVCDVTDED--GVQAMVSQI-EKEVGV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 ---LINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVG---SSAGANQMalwAVYS 203
Cdd:PRK07097  88 idiLVNNAGIIKRIP----MLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICsmmSELGRETV---SAYA 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392895268 204 ATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRTSFFTPDGAVF-----AKSALNTVGNTSDTTG 271
Cdd:PRK07097 161 AAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPQTAPLRELQADGSRHPFdqfiiAKTPAARWGDPEDLAG 233
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
51-239 1.88e-12

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 65.75  E-value: 1.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVsrtqsklDETKKEILEKyssiEVRTAAFDFTNAapsaYKDLLATLNQVEIgvL 130
Cdd:PRK06550   9 LITGAASGIGLAQARAFLAQGAQVYGV-------DKQDKPDLSG----NFHFLQLDLSDD----LEPLFDWVPSVDI--L 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 131 INNVGMSYEYPDVLhkvDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKYVS 210
Cdd:PRK06550  72 CNTAGILDDYKPLL---DTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHALA 148
                        170       180
                 ....*....|....*....|....*....
gi 392895268 211 WLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK06550 149 GFTKQLALDYAKDGIQVFGIAPGAVKTPM 177
PRK12828 PRK12828
short chain dehydrogenase; Provisional
50-277 2.65e-12

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 65.20  E-value: 2.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETkkeiLEKYSSIEVRTAAFDFTNaaPSAYKDLLATLNQV--EI 127
Cdd:PRK12828  10 VAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQT----LPGVPADALRIGGIDLVD--PQAARRAVDEVNRQfgRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGmSYEYPDVLHKVDGGIERLANI---TTINTlpptllSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSA 204
Cdd:PRK12828  84 DALVNIAG-AFVWGTIADGDADTWDRMYGVnvkTTLNA------SKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 205 TKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKR-----TSFFTPD--GAVFAKSAlntvgntSDTTGYITHQL 277
Cdd:PRK12828 157 AKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNRADMpdadfSRWVTPEqiAAVIAFLL-------SDEAQAITGAS 229
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
50-239 2.75e-12

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 65.51  E-value: 2.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLL-VSRTQSKLDETKKEILEKYSS-------IEVRTAAFDFTNAAPSAYKdllat 121
Cdd:PRK06077   9 VVVTGSGRGIGRAIAVRLAKEGSLVVVnAKKRAEEMNETLKMVKENGGEgigvladVSTREGCETLAKATIDRYG----- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 122 lnqvEIGVLINNVGMSYEYPdVLHKVDGGIERLanittintLPPTLLSAGILPQMVA---RKAGVIVNVGSSAGANQMAL 198
Cdd:PRK06077  84 ----VADILVNNAGLGLFSP-FLNVDDKLIDKH--------ISTDFKSVIYCSQELAkemREGGAIVNIASVAGIRPAYG 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392895268 199 WAVYSATKKYVSWLTAILRKEYEhQGITVQTIAPMMVATKM 239
Cdd:PRK06077 151 LSIYGAMKAAVINLTKYLALELA-PKIRVNAIAPGFVKTKL 190
PRK05693 PRK05693
SDR family oxidoreductase;
50-241 2.84e-12

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 65.97  E-value: 2.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRtqskldetKKEILEKYSSIEVRTAAFDFTNAApsAYKDLLATLNQV--EI 127
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWATAR--------KAEDVEALAAAGFTAVQLDVNDGA--ALARLAEELEAEhgGL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMvARKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:PRK05693  74 DVLINNAGYGAMGP----LLDGGVEAMRRQFETNVFAVVGVTRALFPLL-RRSRGLVVNIGSVSGVLVTPFAGAYCASKA 148
                        170       180       190
                 ....*....|....*....|....*....|....
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:PRK05693 149 AVHALSDALRLELAPFGVQVMEVQPGAIASQFAS 182
PRK07775 PRK07775
SDR family oxidoreductase;
50-239 2.88e-12

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 65.93  E-value: 2.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLdetkKEILEKYSSI--EVRTAAFDFTNaaPSAYKDLLATLNQV-- 125
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKC----EELVDKIRADggEAVAFPLDVTD--PDSVKSFVAQAEEAlg 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 EIGVLINNVGMSyeYPDVLHKVDGgiERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSAT 205
Cdd:PRK07775  87 EIEVLVSGAGDT--YFGKLHEIST--EQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAA 162
                        170       180       190
                 ....*....|....*....|....*....|....
gi 392895268 206 KKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK07775 163 KAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGM 196
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
50-239 3.67e-12

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 65.13  E-value: 3.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQskldETKKEILEKYSSIEVRTAAF--DFTN-----AAPSAYKDLLATL 122
Cdd:PRK08643   5 ALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNE----ETAQAAADKLSKDGGKAIAVkaDVSDrdqvfAAVRQVVDTFGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 123 NqveigVLINNVGMSYEYP--DVLHKVdggIERLANITTINTLpptllsAGILPQMVARKA----GVIVNVGSSAGANQM 196
Cdd:PRK08643  81 N-----VVVNNAGVAPTTPieTITEEQ---FDKVYNINVGGVI------WGIQAAQEAFKKlghgGKIINATSQAGVVGN 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 392895268 197 ALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK08643 147 PELAVYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPM 189
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
50-276 3.96e-12

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: 65.05  E-value: 3.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSiEVRTAAFDFTNAAP--SAYKDLLATLNQVEI 127
Cdd:cd08930    5 ILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKN-RVIALELDITSKESikELIESYLEKFGRIDI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gvLINNVGMS----------YEYPDVLHKVDGGIErlaniTTIntlpptLLSAGILPQMVARKAGVIVNVGSSAGAN--- 194
Cdd:cd08930   84 --LINNAYPSpkvwgsrfeeFPYEQWNEVLNVNLG-----GAF------LCSQAFIKLFKKQGKGSIINIASIYGVIapd 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 195 -------QMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK--VKRTSFFTPDGAVFAKSALntVGN 265
Cdd:cd08930  151 friyentQMYSPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNNQPSefLEKYTKKCPLKRMLNPEDL--RGA 228
                        250
                 ....*....|....*
gi 392895268 266 ----TSDTTGYITHQ 276
Cdd:cd08930  229 iiflLSDASSYVTGQ 243
PRK06841 PRK06841
short chain dehydrogenase; Provisional
50-241 4.52e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 65.06  E-value: 4.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRtqsklDETKKEILEKYSSIEVRTAAFDFTN--AAPSAYKDLLATLNQVEI 127
Cdd:PRK06841  18 AVVTGGASGIGHAIAELFAAKGARVALLDR-----SEDVAEVAAQLLGGNAKGLVCDVSDsqSVEAAVAAVISAFGRIDI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gvLINNVGMSYeypdvLHKVDGGIERLANIT-TINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATK 206
Cdd:PRK06841  93 --LVNSAGVAL-----LAPAEDVSEEDWDKTiDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASK 165
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 392895268 207 KYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:PRK06841 166 AGVVGMTKVLALEWGPYGITVNAISPTVVLTELGK 200
PRK07832 PRK07832
SDR family oxidoreductase;
50-239 4.73e-12

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 65.06  E-value: 4.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIeVRTAAFDFTN-AAPSAY-KDLLATLNQVEi 127
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTV-PEHRALDISDyDAVAAFaADIHAAHGSMD- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gVLINNVGMSyeypdvlhkVDGGIERLA-----NITTINTLPPTLLSAGILPQMV-ARKAGVIVNVGSSAGANQMALWAV 201
Cdd:PRK07832  81 -VVMNIAGIS---------AWGTVDRLTheqwrRMVDVNLMGPIHVIETFVPPMVaAGRGGHLVNVSSAAGLVALPWHAA 150
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895268 202 YSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK07832 151 YSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPL 188
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
50-242 5.81e-12

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: 64.49  E-value: 5.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKysSIEVRTAAFDFTNAapSAYKDLLATLNQVEIGV 129
Cdd:cd08936   13 ALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGE--GLSVTGTVCHVGKA--EDRERLVATAVNLHGGV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 --LINNVGMSYEYPDVLhkvDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:cd08936   89 diLVSNAAVNPFFGNIL---DSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVSKT 165
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKV 242
Cdd:cd08936  166 ALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSA 200
PRK07024 PRK07024
SDR family oxidoreductase;
51-263 7.33e-12

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 64.18  E-value: 7.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEiLEKYSSIEVRTAafDFTNAAP--SAYKDLLATLNQVEig 128
Cdd:PRK07024   6 FITGASSGIGQALAREYARQGATLGLVARRTDALQAFAAR-LPKAARVSVYAA--DVRDADAlaAAAADFIAAHGLPD-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 VLINNVGMS-------YEYPDVLHKVdggierLA--NITTINTLPPtllsagILPQMVARKAGVIVNVGSSAGANQMALW 199
Cdd:PRK07024  81 VVIANAGISvgtlteeREDLAVFREV------MDtnYFGMVATFQP------FIAPMRAARRGTLVGIASVAGVRGLPGA 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392895268 200 AVYSATKKYV-SWLTAiLRKEYEHQGITVQTIAPMMVATKMSKVKRTSF-FTPDGAVFAKSALNTV 263
Cdd:PRK07024 149 GAYSASKAAAiKYLES-LRVELRPAGVRVVTIAPGYIRTPMTAHNPYPMpFLMDADRFAARAARAI 213
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
50-244 8.38e-12

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 64.26  E-value: 8.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLL----VSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLAtlnqv 125
Cdd:PRK12938   6 AYVTGGMGGIGTSICQRLHKDGFKVVAgcgpNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVG----- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 EIGVLINNVGMSYeypDVLHK----------VDGGIERLANITTintlpptllsaGILPQMVARKAGVIVNVGSSAGANQ 195
Cdd:PRK12938  81 EIDVLVNNAGITR---DVVFRkmtredwtavIDTNLTSLFNVTK-----------QVIDGMVERGWGRIINISSVNGQKG 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 392895268 196 MALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKR 244
Cdd:PRK12938 147 QFGQTNYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIR 195
PRK06179 PRK06179
short chain dehydrogenase; Provisional
50-239 8.94e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 64.15  E-value: 8.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDetkkeilekySSIEVRTAAFDFTNAAP--SAYKDLLATLNQveI 127
Cdd:PRK06179   7 ALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAA----------PIPGVELLELDVTDDASvqAAVDEVIARAGR--I 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSyeypdvlhkVDGG-----IERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAG---ANQMALw 199
Cdd:PRK06179  75 DVLVNNAGVG---------LAGAaeessIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGflpAPYMAL- 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 392895268 200 avYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK06179 145 --YAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNF 182
PRK07109 PRK07109
short chain dehydrogenase; Provisional
43-237 1.17e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 64.56  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  43 KRAGASWAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSsiEVRTAAFDFTNAApsaykDLLATL 122
Cdd:PRK07109   4 KPIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGG--EALAVVADVADAE-----AVQAAA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 123 NQVE-----IGVLINNVGMSyeypdVLHKVDG----GIERLANITTINTLPPTLLSagiLPQMVARKAGVIVNVGSSAGA 193
Cdd:PRK07109  77 DRAEeelgpIDTWVNNAMVT-----VFGPFEDvtpeEFRRVTEVTYLGVVHGTLAA---LRHMRPRDRGAIIQVGSALAY 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 392895268 194 NQMALWAVYSATKKYVSWLTAILRKEYEHQG--ITVQTIAPMMVAT 237
Cdd:PRK07109 149 RSIPLQSAYCAAKHAIRGFTDSLRCELLHDGspVSVTMVQPPAVNT 194
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
50-232 1.48e-11

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: 63.18  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLD------------ETKKEILEKYSS---IEVRTAAFDFTNAAPSA 114
Cdd:cd05338    6 AFVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDngsakslpgtieETAEEIEAAGGQalpIVVDVRDEDQVRALVEA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 115 YKDLlatlnQVEIGVLINNVGMSYeYPDVLhkvDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGAN 194
Cdd:cd05338   86 TVDQ-----FGRLDILVNNAGAIW-LSLVE---DTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLR 156
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895268 195 QMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:cd05338  157 PARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWP 194
PRK07890 PRK07890
short chain dehydrogenase; Provisional
51-232 2.11e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 63.05  E-value: 2.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEK-YSSIEVRTaafDFTNAAPSAYkdlLATLNQVEIG- 128
Cdd:PRK07890   9 VVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLgRRALAVPT---DITDEDQCAN---LVALALERFGr 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 --VLINNvgmSYEYPDVLHKVDGGIERLANITTINTLPPTLLSAGILPQMvARKAGVIVNVGSSAGANQMALWAVYSATK 206
Cdd:PRK07890  83 vdALVNN---AFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPAL-AESGGSIVMINSMVLRHSQPKYGAYKMAK 158
                        170       180
                 ....*....|....*....|....*.
gi 392895268 207 KYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:PRK07890 159 GALLAASQSLATELGPQGIRVNSVAP 184
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
50-237 2.52e-11

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 62.99  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEkySSIEVRTAAFDFTNA-APSAYKDLLA-TLNQVEI 127
Cdd:PRK13394  10 AVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINK--AGGKAIGVAMDVTNEdAVNAGIDKVAeRFGSVDI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gvLINNVGMSYEYPdvlhkvdggIERLA-----NITTINTLPPTLLSAGILPQMV-ARKAGVIVNVGSSAGANQMALWAV 201
Cdd:PRK13394  88 --LVSNAGIQIVNP---------IENYSfadwkKMQAIHVDGAFLTTKAALKHMYkDDRGGVVIYMGSVHSHEASPLKSA 156
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 392895268 202 YSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK13394 157 YVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 192
PRK05855 PRK05855
SDR family oxidoreductase;
50-237 2.63e-11

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 64.23  E-value: 2.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlekySSIEVRTAAF--DFTNAApsAYKDLlATLNQVEI 127
Cdd:PRK05855 318 VVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELI----RAAGAVAHAYrvDVSDAD--AMEAF-AEWVRAEH 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GV---LINN--VGMS--------YEYPDVLHKVDGGIerlanittINTlpptllSAGILPQMVAR-KAGVIVNVGSSAGA 193
Cdd:PRK05855 391 GVpdiVVNNagIGMAggfldtsaEDWDRVLDVNLWGV--------IHG------CRLFGRQMVERgTGGHIVNVASAAAY 456
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 392895268 194 NQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK05855 457 APSRSLPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDT 500
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
50-239 2.66e-11

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 62.90  E-value: 2.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQsKLDETKKEILEK---YSSIEVRTAAFDFTNAAPSAYKDLLAtlnqvE 126
Cdd:PRK08226   9 ALITGALQGIGEGIARVFARHGANLILLDISP-EIEKLADELCGRghrCTAVVADVRDPASVAAAIKRAKEKEG-----R 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IGVLINNVG---------MSYEYPDVlhKVDGGIERLANITTintlpptllsaGILPQMVARKAGVIVNVGSSAG----- 192
Cdd:PRK08226  83 IDILVNNAGvcrlgsfldMSDEDRDF--HIDINIKGVWNVTK-----------AVLPEMIARKDGRIVMMSSVTGdmvad 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 392895268 193 ANQMAlwavYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK08226 150 PGETA----YALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPM 192
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
50-265 3.45e-11

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: 62.04  E-value: 3.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGF-NVLLVSRTQSKLDETKKEILEKYSSIEVrtaafDFTNaaPSAYKDLLATLNQVEig 128
Cdd:cd05354    6 VLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGDKVVPLRL-----DVTD--PESIKAAAAQAKDVD-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 VLINNVGMSyEYPDVLHkvDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKY 208
Cdd:cd05354   77 VVINNAGVL-KPATLLE--EGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSA 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 392895268 209 VSWLTAILRKEYEHQGITVQTIAPMMVATKMSKvkrtsfftpdGAVFAKSALNTVGN 265
Cdd:cd05354  154 AYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAA----------GAGGPKESPETVAE 200
PRK12829 PRK12829
short chain dehydrogenase; Provisional
50-239 4.17e-11

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 62.38  E-value: 4.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEilekYSSIEVRTAAFDFTNaaPSAYKDLLATlnQVE--- 126
Cdd:PRK12829  14 VLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAAR----LPGAKVTATVADVAD--PAQVERVFDT--AVErfg 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 -IGVLINNVGMSYEypdvlhkvDGGIERLA-----NITTINTLPPTLLSAGILPQMVARKAG-VIVNVGSSAGANQMALW 199
Cdd:PRK12829  86 gLDVLVNNAGIAGP--------TGGIDEITpeqweQTLAVNLNGQFYFARAAVPLLKASGHGgVIIALSSVAGRLGYPGR 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 392895268 200 AVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK12829 158 TPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPR 197
PRK06182 PRK06182
short chain dehydrogenase; Validated
50-232 4.25e-11

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 62.28  E-value: 4.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKldetkkeiLEKYSSIEVRTAAFDFTNAApsaykDLLATLNQVE--- 126
Cdd:PRK06182   6 ALVTGASSGIGKATARRLAAQGYTVYGAARRVDK--------MEDLASLGVHPLSLDVTDEA-----SIKAAVDTIIaee 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 --IGVLINNVGM-SYeypdvlhkvdGGIErlaNITT--------INTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQ 195
Cdd:PRK06182  73 grIDVLVNNAGYgSY----------GAIE---DVPIdearrqfeVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIY 139
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 392895268 196 MALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:PRK06182 140 TPLGAWYHATKFALEGFSDALRLEVAPFGIDVVVIEP 176
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
50-244 5.14e-11

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: 62.02  E-value: 5.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRtqSKLDETkKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLATLNQV--EI 127
Cdd:cd05358    6 ALVTGASSGIGKAIAIRLATAGANVVVNYR--SKEDAA-EEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEfgTL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMV-ARKAGVIVNVGSsagANQMALWAV---YS 203
Cdd:cd05358   83 DILVNNAGLQGDAS----SHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRkSKIKGKIINMSS---VHEKIPWPGhvnYA 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392895268 204 ATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKR 244
Cdd:cd05358  156 ASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAW 196
PRK06484 PRK06484
short chain dehydrogenase; Validated
50-237 5.34e-11

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 63.33  E-value: 5.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVrtaafDFTNAAP--SAYKDLLATLNqvEI 127
Cdd:PRK06484 272 VAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQA-----DITDEAAveSAFAQIQARWG--RL 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSyeypDVLHK-VDGGIERLANITTINTLPPTLLSAGILPQMvaRKAGVIVNVGSSAGANQMALWAVYSATK 206
Cdd:PRK06484 345 DVLVNNAGIA----EVFKPsLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAYCASK 418
                        170       180       190
                 ....*....|....*....|....*....|.
gi 392895268 207 KYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK06484 419 AAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
50-239 5.75e-11

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: 61.62  E-value: 5.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQsklDETKKEILEKYSSIEVRTAAF--DFTNAAP--SAYKDLLATLNQv 125
Cdd:cd05366    5 AIITGAAQGIGRAIAERLAADGFNIVLADLNL---EEAAKSTIQEISEAGYNAVAVgaDVTDKDDveALIDQAVEKFGS- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 eIGVLINNVGMSYEYPdVLHKVDGGIERLANITTINTLpptllsAGIlpQMVARK------AGVIVNVGSSAGANQMALW 199
Cdd:cd05366   81 -FDVMVNNAGIAPITP-LLTITEEDLKKVYAVNVFGVL------FGI--QAAARQfkklghGGKIINASSIAGVQGFPNL 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 392895268 200 AVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:cd05366  151 GAYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEM 190
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
52-245 6.33e-11

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: 61.31  E-value: 6.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  52 VTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlekySSIEVRTAAFDFTNaaPSAYKDLLATLNQVEIG--- 128
Cdd:cd08931    5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAEL----GAENVVAGALDVTD--RAAWAAALADFAAATGGrld 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 VLINNVGMSYEYPdvLHKV-DGGIERLANITTINTLPPTLLSagiLPQMVARKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:cd08931   79 ALFNNAGVGRGGP--FEDVpLAAHDRMVDINVKGVLNGAYAA---LPYLKATPGARVINTASSSAIYGQPDLAVYSATKF 153
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRT 245
Cdd:cd08931  154 AVRGLTEALDVEWARHGIRVADVWPWFVDTPILTKGET 191
PRK07060 PRK07060
short chain dehydrogenase; Provisional
51-239 7.39e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 61.27  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEilekyssIEVRTAAFDFTNAApsAYKDLLATLNQVEIgvL 130
Cdd:PRK07060  13 LVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGE-------TGCEPLRLDVGDDA--AIRAALAAAGAFDG--L 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 131 INNVGMSyeypdVLHKV-DGGIERLANITTINTLPPTLLSAGILPQMVA-RKAGVIVNVGSSAGANQMALWAVYSATKKY 208
Cdd:PRK07060  82 VNCAGIA-----SLESAlDMTAEGFDRVMAVNARGAALVARHVARAMIAaGRGGSIVNVSSQAALVGLPDHLAYCASKAA 156
                        170       180       190
                 ....*....|....*....|....*....|.
gi 392895268 209 VSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK07060 157 LDAITRVLCVELGPHGIRVNSVNPTVTLTPM 187
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
50-232 1.04e-10

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 60.96  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGAT--DGIGKAYAFELARRGFNVLLV-------SRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLA 120
Cdd:PRK12859   9 AVVTGVSrlDGIGAAICKELAEAGADIFFTywtaydkEMPWGVDQDEQIQLQEELLKNGVKVSSMELDLTQNDAPKELLN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 121 TL-NQVEI-GVLINNVgmSYEYPDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMAL 198
Cdd:PRK12859  89 KVtEQLGYpHILVNNA--AYSTNNDFSNLT--AEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSGQFQGPMVG 164
                        170       180       190
                 ....*....|....*....|....*....|....
gi 392895268 199 WAVYSATKKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:PRK12859 165 ELAYAATKGAIDALTSSLAAEVAHLGITVNAINP 198
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
50-232 1.06e-10

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 60.86  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGAT--DGIGKAYAFELARRGFNVLLVSRTQSKLDETK----------KEILEKYSsieVRTAAFDFTNAAPSAYKD 117
Cdd:PRK12748   8 ALVTGASrlNGIGAAVCRRLAAKGIDIFFTYWSPYDKTMPWgmhdkepvllKEEIESYG---VRCEHMEIDLSQPYAPNR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 118 LLATLNQvEIG---VLINNVgmSYEYPDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGAN 194
Cdd:PRK12748  85 VFYAVSE-RLGdpsILINNA--AYSTHTRLEELT--AEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTSGQSLG 159
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895268 195 QMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:PRK12748 160 PMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNP 197
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
50-240 1.15e-10

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 60.95  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQsklDETKKEILEKysSIEVRTAAFDFTNAAPSAYKDLLATLNQVEigV 129
Cdd:PRK06463  10 ALITGGTRGIGRAIAEAFLREGAKVAVLYNSA---ENEAKELREK--GVFTIKCDVGNRDQVKKSKEVVEKEFGRVD--V 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 LINNVGMSYEYPdvLHKVDGgiERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAV-YSATKKY 208
Cdd:PRK06463  83 LVNNAGIMYLMP--FEEFDE--EKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGTAAEGTTfYAITKAG 158
                        170       180       190
                 ....*....|....*....|....*....|..
gi 392895268 209 VSWLTAILRKEYEHQGITVQTIAPMMVATKMS 240
Cdd:PRK06463 159 IIILTRRLAFELGKYGIRVNAVAPGWVETDMT 190
PRK06138 PRK06138
SDR family oxidoreductase;
50-239 1.27e-10

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 60.55  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKySSIEVRTAAFDFTNAAPSAYKDLLATLNQVEigV 129
Cdd:PRK06138   8 AIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAG-GRAFARQGDVGSAEAVEALVDFVAARWGRLD--V 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 LINNVGMSYEYpdvlHKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKYV 209
Cdd:PRK06138  85 LVNNAGFGCGG----TVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAI 160
                        170       180       190
                 ....*....|....*....|....*....|
gi 392895268 210 SWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK06138 161 ASLTRAMALDHATDGIRVNAVAPGTIDTPY 190
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
50-246 1.81e-10

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: 60.31  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268   50 AVVTGATDGIGKAYAFELARR----GFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAPSA--YKDLLATL- 122
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAERSGLRVVRVSLDLGAEAGLEqlLKALRELPr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  123 -NQVEIGVLINNVGMSYEypdvLHKVDGGIERLANITTINTLppTLLSAGILPQMVARK-------AGVIVNVGSSAGAN 194
Cdd:TIGR01500  83 pKGLQRLLLINNAGTLGD----VSKGFVDLSDSTQVQNYWAL--NLTSMLCLTSSVLKAfkdspglNRTVVNISSLCAIQ 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392895268  195 QMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM-SKVKRTS 246
Cdd:TIGR01500 157 PFKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMqQQVREES 209
PRK12827 PRK12827
short chain dehydrogenase; Provisional
50-239 2.22e-10

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 60.12  E-value: 2.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVS----RTQSKLDETKKEILEKYSSieVRTAAFDFTN--AAPSAYKDLLATLN 123
Cdd:PRK12827   9 VLITGGSGGLGRAIAVRLAADGADVIVLDihpmRGRAEADAVAAGIEAAGGK--ALGLAFDVRDfaATRAALDAGVEEFG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 124 QVEIgvLINNVGMSYEYPdvlhKVDGGIERLANITTIN-TLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVY 202
Cdd:PRK12827  87 RLDI--LVNNAGIATDAA----FAELSIEEWDDVIDVNlDGFFNVTQAALPPMIRARRGGRIVNIASVAGVRGNRGQVNY 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 392895268 203 SATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK12827 161 AASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPM 197
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
50-242 2.32e-10

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 59.77  E-value: 2.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIleKYSSIEVRTAAFDFTNAapsayKDLLATLNQVE--- 126
Cdd:PRK08085  12 ILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKL--RQEGIKAHAAPFNVTHK-----QEVEAAIEHIEkdi 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 --IGVLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSA 204
Cdd:PRK08085  85 gpIDVLINNAGIQRRHP----FTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAA 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895268 205 TKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKV 242
Cdd:PRK08085 161 SKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKA 198
PRK07577 PRK07577
SDR family oxidoreductase;
50-277 2.45e-10

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 59.74  E-value: 2.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSklDETKKEILekyssievrtaAFDFTNAAPSAykdllATLNQV---- 125
Cdd:PRK07577   6 VLVTGATKGIGLALSLRLANLGHQVIGIARSAI--DDFPGELF-----------ACDLADIEQTA-----ATLAQIneih 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 EIGVLINNVGMSyeYPDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSA--GANQMalwAVYS 203
Cdd:PRK07577  68 PVDAIVNNVGIA--LPQPLGKID--LAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRAifGALDR---TSYS 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 204 ATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKRtsfftPDGAVFAKSALNT-----VGNT-----------S 267
Cdd:PRK07577 141 AAKSALVGCTRTWALELAEYGITVNAVAPGPIETELFRQTR-----PVGSEEEKRVLASipmrrLGTPeevaaaiafllS 215
                        250
                 ....*....|
gi 392895268 268 DTTGYITHQL 277
Cdd:PRK07577 216 DDAGFITGQV 225
PRK06949 PRK06949
SDR family oxidoreductase;
39-239 3.40e-10

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 59.39  E-value: 3.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  39 IDLKKRAgaswAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVrtAAFDFTNaapsaYKDL 118
Cdd:PRK06949   5 INLEGKV----ALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHV--VSLDVTD-----YQSI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 119 LATLNQVE-----IGVLINNVGMSyeypDVLHKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGV--------IV 185
Cdd:PRK06949  74 KAAVAHAEteagtIDILVNNSGVS----TTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGAgntkpggrII 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392895268 186 NVGSSAGANQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK06949 150 NIASVAGLRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEI 203
PRK07102 PRK07102
SDR family oxidoreductase;
52-239 3.69e-10

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 59.17  E-value: 3.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  52 VTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSiEVRTAAFDFTNAA--PSAYKDLLATLNQVEIGV 129
Cdd:PRK07102   6 IIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAV-AVSTHELDILDTAshAAFLDSLPALPDIVLIAV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 linnvGmsyEYPDvLHKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKYV 209
Cdd:PRK07102  85 -----G---TLGD-QAACEADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKAAL 155
                        170       180       190
                 ....*....|....*....|....*....|
gi 392895268 210 SWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK07102 156 TAFLSGLRNRLFKSGVHVLTVKPGFVRTPM 185
PRK06101 PRK06101
SDR family oxidoreductase;
52-250 5.57e-10

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 58.73  E-value: 5.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  52 VTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDEtkkeiLEKYSSiEVRTAAFDFTNaapsaYKDLLATLNQVEI--GV 129
Cdd:PRK06101   6 ITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDE-----LHTQSA-NIFTLAFDVTD-----HPGTKAALSQLPFipEL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 LINNVGmSYEYPDvlhkvDGGIER--LANITTINTLPPTLLSAGILPQMvaRKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:PRK06101  75 WIFNAG-DCEYMD-----DGKVDAtlMARVFNVNVLGVANCIEGIQPHL--SCGHRVVIVGSIASELALPRAEAYGASKA 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVATKMSkvKRTSFFTP 250
Cdd:PRK06101 147 AVAYFARTLQLDLRPKGIEVVTVFPGFVATPLT--DKNTFAMP 187
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
50-251 5.69e-10

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: 58.56  E-value: 5.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVR-TAAFDFTNAAPSAykdlLATLNQVEIg 128
Cdd:cd05345    8 AIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADvTKRADVEAMVEAA----LSKFGRLDI- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 vLINNVGMSYEYPDVLHKVDGGIERlanITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKY 208
Cdd:cd05345   83 -LVNNAGITHRNKPMLEVDEEEFDR---VFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGW 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 392895268 209 VSWLTAILRKEYEHQGITVQTIAPMMVATKMSKvkrtSFFTPD 251
Cdd:cd05345  159 VVTATKAMAVELAPRNIRVNCLCPVAGETPLLS----MFMGED 197
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
50-241 5.80e-10

(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: 58.87  E-value: 5.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLL-------------VSRTQSKLDETKK---EILEKYSSIEvrtaafdftnAAPS 113
Cdd:cd05353    8 VLVTGAGGGLGRAYALAFAERGAKVVVndlggdrkgsgksSSAADKVVDEIKAaggKAVANYDSVE----------DGEK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 114 AYKDLLATLNQVEIgvLINNVG---------MSYEYPDVLHKV--DGGIerlanittintlpptLLSAGILPQMVARKAG 182
Cdd:cd05353   78 IVKTAIDAFGRVDI--LVNNAGilrdrsfakMSEEDWDLVMRVhlKGSF---------------KVTRAAWPYMRKQKFG 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392895268 183 VIVNVGSSAG-------ANqmalwavYSATKKYVSWLTAILRKEYEHQGITVQTIAPmMVATKMSK 241
Cdd:cd05353  141 RIINTSSAAGlygnfgqAN-------YSAAKLGLLGLSNTLAIEGAKYNITCNTIAP-AAGSRMTE 198
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
50-253 7.83e-10

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: 58.25  E-value: 7.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlekyssievRTAAFDFTNAAPSAykdllATLNQVE--- 126
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGDPL---------RLTPLDVADAAAVR-----EVCSRLLaeh 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 --IGVLINNVGMSYeyPDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSA 204
Cdd:cd05331   67 gpIDALVNCAGVLR--PGATDPLS--TEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGA 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 392895268 205 TKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMskvKRTSFFTPDGA 253
Cdd:cd05331  143 SKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAM---QRTLWHDEDGA 188
PRK06125 PRK06125
short chain dehydrogenase; Provisional
50-194 8.66e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 58.13  E-value: 8.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEiLEKYSSIEVRTAAFDFTnaAPSAYKDLLATLNqvEIGV 129
Cdd:PRK06125  10 VLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAAD-LRAAHGVDVAVHALDLS--SPEAREQLAAEAG--DIDI 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392895268 130 LINNVGmsyeypDV----LHKVDGGIER----LANITTINtlpptlLSAGILPQMVARKAGVIVNVGSSAGAN 194
Cdd:PRK06125  85 LVNNAG------AIpgggLDDVDDAAWRagweLKVFGYID------LTRLAYPRMKARGSGVIVNVIGAAGEN 145
PRK06180 PRK06180
short chain dehydrogenase; Provisional
52-232 9.88e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 58.39  E-value: 9.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  52 VTGATDGIGKAYAFELARRGFNVLLVSRTQSKLdetkkEILEKYSSIEVRTAAFDFTNAA--PSAYKDLLATLNQveIGV 129
Cdd:PRK06180   9 ITGVSSGFGRALAQAALAAGHRVVGTVRSEAAR-----ADFEALHPDRALARLLDVTDFDaiDAVVADAEATFGP--IDV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 LINNVGMSYEypdvlhkvdGGIER--LANITT---INTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSA 204
Cdd:PRK06180  82 LVNNAGYGHE---------GAIEEspLAEMRRqfeVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCG 152
                        170       180
                 ....*....|....*....|....*...
gi 392895268 205 TKKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:PRK06180 153 SKFALEGISESLAKEVAPFGIHVTAVEP 180
PRK07074 PRK07074
SDR family oxidoreductase;
48-238 1.05e-09

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 57.86  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  48 SWAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlekySSIEVRTAAFDFTNAAPSAYKDLLATLNQVEI 127
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADAL----GDARFVPVACDLTDAASLAAALANAAAERGPV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYEYPdvLHKVDGGIERLANitTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAvYSATKK 207
Cdd:PRK07074  79 DVLVANAGAARAAS--LHDTTPASWRADN--ALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMAALGHPA-YSAAKA 153
                        170       180       190
                 ....*....|....*....|....*....|.
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVATK 238
Cdd:PRK07074 154 GLIHYTKLLAVEYGRFGIRANAVAPGTVKTQ 184
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
50-239 1.17e-09

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 57.73  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlekysSIEVRTAAFDFTNAAP--SAYKDLLATLNQVEI 127
Cdd:PRK07067   9 ALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEI-----GPAAIAVSLDVTRQDSidRIVAAAVERFGGIDI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gvLINNVGMSyeypDVLHKVDGGIERLANITTINTLPPTLLSAGILPQMVAR-KAGVIVNVGSSAGANQMALWAVYSATK 206
Cdd:PRK07067  84 --LFNNAALF----DMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMASQAGRRGEALVSHYCATK 157
                        170       180       190
                 ....*....|....*....|....*....|...
gi 392895268 207 KYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK07067 158 AAVISYTQSAALALIRHGINVNAIAPGVVDTPM 190
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
50-232 1.36e-09

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: 57.60  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlEKYSSIEVRTAAFDFTN--AAPSAYKDLLATLNQVEI 127
Cdd:cd05369    6 AFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEI-SSATGGRAHPIQCDVRDpeAVEAAVDETLKEFGKIDI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gvLINNVGMSYEYPdvlhkvdggIERL-AN----ITTINTLPPTLLSAGILPQMVARKA-GVIVNVGSSAGANQMALWAV 201
Cdd:cd05369   85 --LINNAAGNFLAP---------AESLsPNgfktVIDIDLNGTFNTTKAVGKRLIEAKHgGSILNISATYAYTGSPFQVH 153
                        170       180       190
                 ....*....|....*....|....*....|.
gi 392895268 202 YSATKKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:cd05369  154 SAAAKAGVDALTRSLAVEWGPYGIRVNAIAP 184
PRK07023 PRK07023
SDR family oxidoreductase;
50-206 1.66e-09

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 57.33  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSR-TQSKLDETKKEILEkyssiEVRTAAFDFTNAAPSAYKDLLAT-LNQVEI 127
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPGIAVLGVARsRHPSLAAAAGERLA-----EVELDLSDAAAAAAWLAGDLLAAfVDGASR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMsyeypdvlhkVD--GGIERL-----ANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWA 200
Cdd:PRK07023  79 VLLINNAGT----------VEpiGPLATLdaaaiARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWS 148

                 ....*.
gi 392895268 201 VYSATK 206
Cdd:PRK07023 149 VYCATK 154
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
50-227 1.74e-09

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: 57.01  E-value: 1.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAfDFTNAApsaykDLLATLNQVE--- 126
Cdd:cd05373    2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVPT-DARDED-----EVIALFDLIEeei 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 --IGVLINNVGMSYEYPdVLHKVDggiERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSA 204
Cdd:cd05373   76 gpLEVLVYNAGANVWFP-ILETTP---RVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAG 151
                        170       180
                 ....*....|....*....|...
gi 392895268 205 TKKYVSWLTAILRKEYEHQGITV 227
Cdd:cd05373  152 AKFALRALAQSMARELGPKGIHV 174
PRK07814 PRK07814
SDR family oxidoreductase;
50-242 1.88e-09

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 57.48  E-value: 1.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLATLNQVEIgv 129
Cdd:PRK07814  13 AVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLDI-- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 LINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVARK-AGVIVNVGSSAGANQMALWAVYSATKKY 208
Cdd:PRK07814  91 VVNNVGGTMPNP----LLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSgGGSVINISSTMGRLAGRGFAAYGTAKAA 166
                        170       180       190
                 ....*....|....*....|....*....|....
gi 392895268 209 VSWLTAILRKEYEHQgITVQTIAPMMVATKMSKV 242
Cdd:PRK07814 167 LAHYTRLAALDLCPR-IRVNAIAPGSILTSALEV 199
PRK05650 PRK05650
SDR family oxidoreductase;
51-276 1.97e-09

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 57.36  E-value: 1.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKeilekyssiEVRTA---AF----DFTNaapsaYKDLLATLN 123
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLK---------LLREAggdGFyqrcDVRD-----YSQLTALAQ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 124 QVE-----IGVLINNVGMSyeypdvlhkVDGGIERLAN-----ITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGA 193
Cdd:PRK05650  70 ACEekwggIDVIVNNAGVA---------SGGFFEELSLedwdwQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 194 NQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSkvkrTSFFTPD-------GAVFAKSALntvgNT 266
Cdd:PRK05650 141 MQGPAMSSYNVAKAGVVALSETLLVELADDEIGVHVVCPSFFQTNLL----DSFRGPNpamkaqvGKLLEKSPI----TA 212
                        250
                 ....*....|
gi 392895268 267 SDTTGYITHQ 276
Cdd:PRK05650 213 ADIADYIYQQ 222
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
50-237 2.47e-09

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: 56.92  E-value: 2.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLV--SRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLATLNQVEI 127
Cdd:cd05355   29 ALITGGDSGIGRAVAIAFAREGADVAINylPEEEDDAEETKKLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEFGKLDI 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gvLINNVGMSYEYPDVLhkvDGGIERLANITTINTLPPTLLSAGILPQMvaRKAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:cd05355  109 --LVNNAAYQHPQESIE---DITTEQLEKTFRTNIFSMFYLTKAALPHL--KKGSSIINTTSVTAYKGSPHLLDYAATKG 181
                        170       180       190
                 ....*....|....*....|....*....|
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:cd05355  182 AIVAFTRGLSLQLAEKGIRVNAVAPGPIWT 211
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
50-259 2.58e-09

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: 56.59  E-value: 2.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKL-DETKKEILEKYSSIEVRTAafDFTNAApsaykDLLATLNQVE-- 126
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAaAEVAAEIEELGGKAVVVRA--DVSQPQ-----DVEEMFAAVKer 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 ---IGVLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYS 203
Cdd:cd05359   74 fgrLDVLVSNAAAGAFRP----LSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVG 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392895268 204 ATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKvkrtSFFTPDGAVFAKSA 259
Cdd:cd05359  150 TAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDALA----HFPNREDLLEAAAA 201
PRK06523 PRK06523
short chain dehydrogenase; Provisional
50-237 2.82e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 56.84  E-value: 2.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSklDETKKEIleKYSSIEVRTAafDFTNAAPSAykdLLATLNQVEIgv 129
Cdd:PRK06523  12 ALVTGGTKGIGAATVARLLEAGARVVTTARSRP--DDLPEGV--EFVAADLTTA--EGCAAVARA---VLERLGGVDI-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 LINNVGMSYEYPdvlhkvdGGI-----ERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGAnqMALWAV--- 201
Cdd:PRK06523  81 LVHVLGGSSAPA-------GGFaaltdEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRR--LPLPEStta 151
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 392895268 202 YSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK06523 152 YAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIET 187
PRK08589 PRK08589
SDR family oxidoreductase;
50-237 3.33e-09

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 56.71  E-value: 3.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSrTQSKLDETKKEILEKYSSIEvrtaAFDFTNAAPSAYKDLLATLNQV--EI 127
Cdd:PRK08589   9 AVITGASTGIGQASAIALAQEGAYVLAVD-IAEAVSETVDKIKSNGGKAK----AYHVDISDEQQVKDFASEIKEQfgRV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMS------YEYPdvlhkvdggIERLANITTINTLPPTLLSAGILPQMVaRKAGVIVNVGSSAGANQMALWAV 201
Cdd:PRK08589  84 DVLFNNAGVDnaagriHEYP---------VDVFDKIMAVDMRGTFLMTKMLLPLMM-EQGGSIINTSSFSGQAADLYRSG 153
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 392895268 202 YSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK08589 154 YNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIET 189
PRK06914 PRK06914
SDR family oxidoreductase;
50-232 3.41e-09

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 56.57  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSR---TQSKLDETKKEiLEKYSSIEVRtaAFDFTN-AAPSAYKDLLATLNQv 125
Cdd:PRK06914   6 AIVTGASSGFGLLTTLELAKKGYLVIATMRnpeKQENLLSQATQ-LNLQQNIKVQ--QLDVTDqNSIHNFQLVLKEIGR- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 eIGVLINNVGMSYeypdvlhkvdGG-IERLA--------NITTINTLPPTLLsagILPQMVARKAGVIVNVGSSAGANQM 196
Cdd:PRK06914  82 -IDLLVNNAGYAN----------GGfVEEIPveeyrkqfETNVFGAISVTQA---VLPYMRKQKSGKIINISSISGRVGF 147
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 392895268 197 ALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:PRK06914 148 PGLSPYVSSKYALEGFSESLRLELKPFGIDVALIEP 183
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
50-271 6.98e-09

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: 55.57  E-value: 6.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEiLEKYSSIEVRTAAFDFTNAAPSaykdLLATLNQVE--I 127
Cdd:cd08942    9 VLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEE-LSAYGECIAIPADLSSEEGIEA----LVARVAERSdrL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSY-----EYPDvlhkvdGGIERlanITTINTLPPTLLSAGILPQMvaRKAGV------IVNVGSSAGANQM 196
Cdd:cd08942   84 DVLVNNAGATWgapleAFPE------SGWDK---VMDINVKSVFFLTQALLPLL--RAAATaenparVINIGSIAGIVVS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 197 ALWAV-YSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMskvkrTSFFTPDGAVFAKSA----LNTVGNTSDTTG 271
Cdd:cd08942  153 GLENYsYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKM-----TAFLLNDPAALEAEEksipLGRWGRPEDMAG 227
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
50-237 7.30e-09

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: 55.27  E-value: 7.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEK----------YSSIEVRTAAFDFTNAAPSAykdll 119
Cdd:cd05365    2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAggqaiglecnVTSEQDLEAVVKATVSQFGG----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 120 atlnqveIGVLINNVGMSYEYPDvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALW 199
Cdd:cd05365   77 -------ITILVNNAGGGGPKPF---DMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRI 146
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895268 200 AVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:cd05365  147 AAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKT 184
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
50-239 7.38e-09

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: 55.54  E-value: 7.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSI---EVRTAAfDFTNAAPSAYkDLLATLNqve 126
Cdd:cd05326    7 AIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFvhcDVTVEA-DVRAAVDTAV-ARFGRLD--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 igVLINNVGMSYEYPDVLhkVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATK 206
Cdd:cd05326   82 --IMFNNAGVLGAPCYSI--LETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASK 157
                        170       180       190
                 ....*....|....*....|....*....|...
gi 392895268 207 KYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:cd05326  158 HAVLGLTRSAATELGEHGIRVNCVSPYGVATPL 190
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
49-262 1.06e-08

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 55.10  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  49 WAVVTGATDGIGKAYAFELARRGFNVLL-VSRTQSKLDETKKEILEKysSIEVRTaafDFTNAApsAYKDLLATLNQ--- 124
Cdd:PRK08642   7 TVLVTGGSRGLGAAIARAFAREGARVVVnYHQSEDAAEALADELGDR--AIALQA---DVTDRE--QVQAMFATATEhfg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 125 VEIGVLINN--VGMSY-----------EYPDVLHKVDGGIErlaniTTINTLpptllsAGILPQMVARKAGVIVNVGSSA 191
Cdd:PRK08642  80 KPITTVVNNalADFSFdgdarkkaddiTWEDFQQQLEGSVK-----GALNTI------QAALPGMREQGFGRIINIGTNL 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392895268 192 GANQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQtiapmMVATKMSKVKRTSFFTPDgAVFAKSALNT 262
Cdd:PRK08642 149 FQNPVVPYHDYTTAKAALLGLTRNLAAELGPYGITVN-----MVSGGLLRTTDASAATPD-EVFDLIAATT 213
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
50-239 1.28e-08

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: 54.70  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRtqskLDETKKEILEkyssiEVRTAA----FDFTNaaPSAYKDLLATLnQV 125
Cdd:cd05341    8 AIVTGGARGLGLAHARLLVAEGAKVVLSDI----LDEEGQAAAA-----ELGDAArffhLDVTD--EDGWTAVVDTA-RE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 EIG---VLINNVGMSyeypdVLHKV-DGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAV 201
Cdd:cd05341   76 AFGrldVLVNNAGIL-----TGGTVeTTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAA 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 392895268 202 YSATKKYVSWLTAILRKEYEHQ--GITVQTIAPMMVATKM 239
Cdd:cd05341  151 YNASKGAVRGLTKSAALECATQgyGIRVNSVHPGYIYTPM 190
PRK07478 PRK07478
short chain dehydrogenase; Provisional
50-239 1.39e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 54.55  E-value: 1.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEkySSIEVRTAAFDFTNAapsAYKDLLATLNQVEIGV 129
Cdd:PRK07478   9 AIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRA--EGGEAVALAGDVRDE---AYAKALVALAVERFGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 L---INNVGMSYEYPDVLH-KVDGGIERLA-NITTintlppTLLSAGI-LPQMVARKAGVIV----NVGSSAGANQMalw 199
Cdd:PRK07478  84 LdiaFNNAGTLGEMGPVAEmSLEGWRETLAtNLTS------AFLGAKHqIPAMLARGGGSLIftstFVGHTAGFPGM--- 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 392895268 200 AVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK07478 155 AAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPM 194
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
50-239 1.39e-08

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 54.58  E-value: 1.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQsklDETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLATLNQV--EI 127
Cdd:PRK12745   5 ALVTGGRRGIGLGIARALAAAGFDLAINDRPD---DEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAwgRI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMS-YEYPDVLhkvDGGIERLANITTINTLPPTLLSAGILPQMVARKA------GVIVNVGSSAGANQMALWA 200
Cdd:PRK12745  82 DCLVNNAGVGvKVRGDLL---DLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVSSVNAIMVSPNRG 158
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 392895268 201 VYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK12745 159 EYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDM 197
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
50-232 1.71e-08

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 55.62  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKyssIEVRTAAFDFTNAAP--SAYKDLLATLNQVEI 127
Cdd:PRK08324 425 ALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGP---DRALGVACDVTDEAAvqAAFEEAALAFGGVDI 501
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gvLINNVGMSYEYPDvlhkVDGGIERLANITTINTLPPTLLSAGILPQMVARKAG-VIVNVGSSAGANQMALWAVYSATK 206
Cdd:PRK08324 502 --VVSNAGIAISGPI----EETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLGgSIVFIASKNAVNPGPNFGAYGAAK 575
                        170       180
                 ....*....|....*....|....*.
gi 392895268 207 KYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:PRK08324 576 AAELHLVRQLALELGPDGIRVNGVNP 601
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
50-239 1.94e-08

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: 54.16  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIevrtaAFDFTNAApSAYKDLLATLNQV-EIG 128
Cdd:cd05363    6 ALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAI-----SLDVTDQA-SIDRCVAALVDRWgSID 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 VLINNVGMsYEYPDVLHKVDGGIERLANITTINTLpptLLSAGILPQMVAR-KAGVIVNVGSSAGANQMALWAVYSATKK 207
Cdd:cd05363   80 ILVNNAAL-FDLAPIVDITRESYDRLFAINVSGTL---FMMQAVARAMIAQgRGGKIINMASQAGRRGEALVGVYCATKA 155
                        170       180       190
                 ....*....|....*....|....*....|..
gi 392895268 208 YVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:cd05363  156 AVISLTQSAGLNLIRHGINVNAIAPGVVDGEH 187
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
52-232 2.06e-08

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: 54.59  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  52 VTGATDGIGKAYAFELARRGFNVLLVSRTqskLDETKKEILEKYSSIEVRTAAFDFTNAapsayKDLLATLNQVEIGV-- 129
Cdd:cd09805    5 ITGCDSGFGNLLAKKLDSLGFTVLAGCLT---KNGPGAKELRRVCSDRLRTLQLDVTKP-----EQIKRAAQWVKEHVge 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 -----LINNVGMSyeypdvlhkVDGGIERLANITT------INTLPPTLLSAGILPqMVARKAGVIVNVGSSAGANQMAL 198
Cdd:cd09805   77 kglwgLVNNAGIL---------GFGGDEELLPMDDyrkcmeVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRVPFPA 146
                        170       180       190
                 ....*....|....*....|....*....|....
gi 392895268 199 WAVYSATKKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:cd09805  147 GGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEP 180
PRK08264 PRK08264
SDR family oxidoreductase;
50-241 2.28e-08

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 53.74  E-value: 2.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRG-FNVLLVSRTQSKLDETKKEILekyssievrTAAFDFTN-----AAPSAYKDllatln 123
Cdd:PRK08264   9 VLVTGANRGIGRAFVEQLLARGaAKVYAAARDPESVTDLGPRVV---------PLQLDVTDpasvaAAAEAASD------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 124 qveIGVLINNVGMSYEYPDVLhkvDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYS 203
Cdd:PRK08264  74 ---VTILVNNAGIFRTGSLLL---EGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYS 147
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392895268 204 ATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:PRK08264 148 ASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAA 185
PRK06057 PRK06057
short chain dehydrogenase; Provisional
50-237 3.39e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 53.58  E-value: 3.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTqsklDETKKEILEKYSSIEVRTaafDFTNAApsAYKDLLATLNQV--EI 127
Cdd:PRK06057  10 AVITGGGSGIGLATARRLAAEGATVVVGDID----PEAGKAAADEVGGLFVPT---DVTDED--AVNALFDTAAETygSV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYEYPDVLhkVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGS-----SAGANQMAlwavY 202
Cdd:PRK06057  81 DIAFNNAGISPPEDDSI--LNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASfvavmGSATSQIS----Y 154
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 392895268 203 SATKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK06057 155 TASKGGVLAMSRELGVQFARQGIRVNALCPGPVNT 189
PRK06114 PRK06114
SDR family oxidoreductase;
50-241 3.63e-08

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 53.63  E-value: 3.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVS-RTQSKLDETKKEILEKYSSIEVRTAafDFTNAApsaykDLLATLNQVE-- 126
Cdd:PRK06114  11 AFVTGAGSGIGQRIAIGLAQAGADVALFDlRTDDGLAETAEHIEAAGRRAIQIAA--DVTSKA-----DLRAAVARTEae 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 ---IGVLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAG--ANQMALWAV 201
Cdd:PRK06114  84 lgaLTLAVNAAGIANANP----AEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGiiVNRGLLQAH 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 392895268 202 YSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:PRK06114 160 YNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNT 199
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
49-232 4.52e-08

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: 53.05  E-value: 4.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  49 WAVVTGATDGIGKAYAFELARRGFNVLLVSRT-QSKLDETKKEIlekySSIEVRTAAF--DFTNAApsAYKDLLATLNQV 125
Cdd:cd05357    2 VALVTGAAKRIGRAIAEALAAEGYRVVVHYNRsEAEAQRLKDEL----NALRNSAVLVqaDLSDFA--ACADLVAAAFRA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 --EIGVLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYS 203
Cdd:cd05357   76 fgRCDVLVNNASAFYPTP----LGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYC 151
                        170       180
                 ....*....|....*....|....*....
gi 392895268 204 ATKKYVSWLTAILRKEYEHQgITVQTIAP 232
Cdd:cd05357  152 MSKAALEGLTRSAALELAPN-IRVNGIAP 179
PRK07035 PRK07035
SDR family oxidoreductase;
50-240 5.55e-08

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 52.71  E-value: 5.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLATLNQVEIgv 129
Cdd:PRK07035  11 ALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHGRLDI-- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 130 LINNVGMSYEYPDVLHKVDGGIERLANittINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKYV 209
Cdd:PRK07035  89 LVNNAAANPYFGHILDTDLGAFQKTVD---VNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITKAAV 165
                        170       180       190
                 ....*....|....*....|....*....|.
gi 392895268 210 SWLTAILRKEYEHQGITVQTIAPMMVATKMS 240
Cdd:PRK07035 166 ISMTKAFAKECAPFGIRVNALLPGLTDTKFA 196
PRK06198 PRK06198
short chain dehydrogenase; Provisional
50-213 6.10e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 52.70  E-value: 6.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGF-NVLLVSRTQSKLDETKKEILEkySSIEVRTAAFDFTNAApsAYKDLLATLNQV--E 126
Cdd:PRK06198   9 ALVTGGTQGLGAAIARAFAERGAaGLVICGRNAEKGEAQAAELEA--LGAKAVFVQADLSDVE--DCRRVVAAADEAfgR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IGVLINNVGMSyeypDVLHKVDGGIERLANITTINTLPPTLLSAGILPQMVARKA-GVIVNVGS-SAGANQMALwAVYSA 204
Cdd:PRK06198  85 LDALVNAAGLT----DRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIGSmSAHGGQPFL-AAYCA 159

                 ....*....
gi 392895268 205 TKKYVSWLT 213
Cdd:PRK06198 160 SKGALATLT 168
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
50-273 9.22e-08

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: 52.45  E-value: 9.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRT-QSKLDETKKEILEKYS-SIEVRTaafDFTN-AAPSAYKDLLATLNQVE 126
Cdd:cd09763    6 ALVTGASRGIGRGIALQLGEAGATVYITGRTiLPQLPGTAEEIEARGGkCIPVRC---DHSDdDEVEALFERVAREQQGR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IGVLINNVGMSYEYPDVLHKVDGGIERLANITTINTlpptllsAGI----------LPQMVARKAGVIVNVgSSAGANQM 196
Cdd:cd09763   83 LDILVNNAYAAVQLILVGVAKPFWEEPPTIWDDINN-------VGLrahyacsvyaAPLMVKAGKGLIVII-SSTGGLEY 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392895268 197 ALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKVKrtsFFTPDGAVFAKsaLNTVGNTSDTTGYI 273
Cdd:cd09763  155 LFNVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEM---PEDDEGSWHAK--ERDAFLNGETTEYS 226
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
51-174 1.01e-07

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: 52.21  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNaaPSAYKDLLATLNQV--EIG 128
Cdd:cd09808    5 LITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETESGNQNIFLHIVDMSD--PKQVWEFVEEFKEEgkKLH 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 392895268 129 VLINNVGMSYEYPDVlhkVDGGIERlaNITTiNTLPPTLLSAGILP 174
Cdd:cd09808   83 VLINNAGCMVNKREL---TEDGLEK--NFAT-NTLGTYILTTHLIP 122
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
50-268 1.15e-07

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 52.16  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLlVSRTQSkldETKKEILEKYSSIEVRTAAF--DFT-NAAPSAYKDllATLNQV- 125
Cdd:PRK06113  14 AIITGAGAGIGKEIAITFATAGASVV-VSDINA---DAANHVVDEIQQLGGQAFACrcDITsEQELSALAD--FALSKLg 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 EIGVLINNVGMSYEYPdvlhkVDGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSAT 205
Cdd:PRK06113  88 KVDILVNNAGGGGPKP-----FDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASS 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392895268 206 KKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMSKvkrtSFFTPD--GAVFAKSALNTVGNTSD 268
Cdd:PRK06113 163 KAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALK----SVITPEieQKMLQHTPIRRLGQPQD 223
PRK12746 PRK12746
SDR family oxidoreductase;
50-240 1.43e-07

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 51.57  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLL-VSRTQSKLDETKKEILE---KYSSIEVRTAAFDFTNAAPSAYK-DLLATLNQ 124
Cdd:PRK12746   9 ALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIESnggKAFLIEADLNSIDGVKKLVEQLKnELQIRVGT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 125 VEIGVLINNVGMSYEypdvlhkvdGGIERLA-----NITTINTLPPTLLSAGILPQMvaRKAGVIVNVGSSAGANQMALW 199
Cdd:PRK12746  89 SEIDILVNNAGIGTQ---------GTIENTTeeifdEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRLGFTGS 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392895268 200 AVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMS 240
Cdd:PRK12746 158 IAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDIN 198
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
50-268 1.66e-07

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: 51.30  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLL-VSRTQSKLDETKKEILEKysSIEVRTAAFDFtNAAPSAYKDllATLNQVEIG 128
Cdd:cd05349    3 VLVTGASRGLGAAIARSFAREGARVVVnYYRSTESAEAVAAEAGER--AIAIQADVRDR-DQVQAMIEE--AKNHFGPVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 VLINNV-------------GMSYEYPDVLHKVDGGIERLANITTIntlpptllsagILPQMVARKAGVIVNVGSSAGANQ 195
Cdd:cd05349   78 TIVNNAlidfpfdpdqrktFDTIDWEDYQQQLEGAVKGALNLLQA-----------VLPDFKERGSGRVINIGTNLFQNP 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392895268 196 MALWAVYSATKKYVSWLTAILRKEYEHQGITVQtiapmMVATKMSKVKRTSFFTPDgAVF----AKSALNTVGNTSD 268
Cdd:cd05349  147 VVPYHDYTTAKAALLGFTRNMAKELGPYGITVN-----MVSGGLLKVTDASAATPK-EVFdaiaQTTPLGKVTTPQD 217
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
51-136 2.48e-07

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: 50.93  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFtnAAPSAYKDLLATLNQVE--IG 128
Cdd:cd09807    5 IITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLNHEVIVRHLDL--ASLKSIRAFAAEFLAEEdrLD 82

                 ....*...
gi 392895268 129 VLINNVGM 136
Cdd:cd09807   83 VLINNAGV 90
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
50-206 2.51e-07

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 51.04  E-value: 2.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKkeilekyssieVRTAAFDFTNAApsAYKDLLA-TLNQVE-I 127
Cdd:PRK08220  11 VWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDYP-----------FATFVLDVSDAA--AVAQVCQrLLAETGpL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGmsyeypdVLHKvdGGIERL-----ANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAgAN----QMal 198
Cdd:PRK08220  78 DVLVNAAG-------ILRM--GATDSLsdedwQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNA-AHvpriGM-- 145

                 ....*...
gi 392895268 199 wAVYSATK 206
Cdd:PRK08220 146 -AAYGASK 152
PRK07069 PRK07069
short chain dehydrogenase; Validated
50-213 2.74e-07

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 50.86  E-value: 2.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVS-RTQSKLDETKKEILEKYSSIEVRTAAFDFTNAApsAYKDLLATLNQV--E 126
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDiNDAAGLDAFAAEINAAHGEGVAFAAVQDVTDEA--QWQALLAQAADAmgG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IGVLINNVGMSyeypdvlhkVDGGIERLA-----NITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAV 201
Cdd:PRK07069  80 LSVLVNNAGVG---------SFGAIEQIEldewrRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTA 150
                        170
                 ....*....|..
gi 392895268 202 YSATKKYVSWLT 213
Cdd:PRK07069 151 YNASKAAVASLT 162
PRK06398 PRK06398
aldose dehydrogenase; Validated
50-213 3.03e-07

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 50.60  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTqskldetkkeilekyssiEVRTAAFDFTNAAPSAYKDLLATLNQV---- 125
Cdd:PRK06398   9 AIVTGGSQGIGKAVVNRLKEEGSNVINFDIK------------------EPSYNDVDYFKVDVSNKEQVIKGIDYVisky 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 -EIGVLINNVGMsyEYPDVLHKVDGGIERlaNITTINTLPPTLLSAGILPQMVARKAGVIVNVGS--SAGANQMAlwAVY 202
Cdd:PRK06398  71 gRIDILVNNAGI--ESYGAIHAVEEDEWD--RIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASvqSFAVTRNA--AAY 144
                        170
                 ....*....|.
gi 392895268 203 SATKKYVSWLT 213
Cdd:PRK06398 145 VTSKHAVLGLT 155
PRK08339 PRK08339
short chain dehydrogenase; Provisional
39-237 3.08e-07

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 50.62  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  39 IDLKKRAgaswAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKySSIEVRTAAFDFTNAapsayKDL 118
Cdd:PRK08339   4 IDLSGKL----AFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSE-SNVDVSYIVADLTKR-----EDL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 119 LATLNQV-EIGVlinnvgmsyeyPDVLHKVDGG----------IERLANITTINTLPPTLLSAGILPQMVARKAGVIVNV 187
Cdd:PRK08339  74 ERTVKELkNIGE-----------PDIFFFSTGGpkpgyfmemsMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYS 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 392895268 188 GSSAGANQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK08339 143 TSVAIKEPIPNIALSNVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRT 192
PRK12747 PRK12747
short chain dehydrogenase; Provisional
50-240 3.16e-07

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 50.46  E-value: 3.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLL-VSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLATLN----Q 124
Cdd:PRK12747   7 ALVTGASRGIGRAIAKRLANDGALVAIhYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNELQnrtgS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 125 VEIGVLINNVGMSyeyPDVLhkVDGGIERLAN-ITTINTLPPTLLSAGILPQMvaRKAGVIVNVGSSAGANQMALWAVYS 203
Cdd:PRK12747  87 TKFDILINNAGIG---PGAF--IEETTEQFFDrMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLPDFIAYS 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 392895268 204 ATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMS 240
Cdd:PRK12747 160 MTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMN 196
PRK07062 PRK07062
SDR family oxidoreductase;
39-237 3.72e-07

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 50.43  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  39 IDLKKRAgaswAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAApsaykDL 118
Cdd:PRK07062   4 IQLEGRV----AVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFPGARLLAARCDVLDEA-----DV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 119 LATLNQVE-----IGVLINNVGMSYeypdVLHKVDGGIERL---ANITTINTLPPTllsAGILPQMVARKAGVIVNVGSS 190
Cdd:PRK07062  75 AAFAAAVEarfggVDMLVNNAGQGR----VSTFADTTDDAWrdeLELKYFSVINPT---RAFLPLLRASAAASIVCVNSL 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 392895268 191 AGANQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK07062 148 LALQPEPHMVATSAARAGLLNLVKSLATELAPKGVRVNSILLGLVES 194
PRK06947 PRK06947
SDR family oxidoreductase;
51-239 4.84e-07

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 50.19  E-value: 4.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLL-VSRTQSKLDETKKEIleKYSSIEVRTAAFDFTNAApsaykDLLATLNQVE--- 126
Cdd:PRK06947   6 LITGASRGIGRATAVLAAARGWSVGInYARDAAAAEETADAV--RAAGGRACVVAGDVANEA-----DVIAMFDAVQsaf 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 --IGVLINNVGMSYEYPDVlhkVDGGIERLANITTINTLPPTLlsagilpqmVARKA------------GVIVNVGSSAG 192
Cdd:PRK06947  79 grLDALVNNAGIVAPSMPL---ADMDAARLRRMFDTNVLGAYL---------CAREAarrlstdrggrgGAIVNVSSIAS 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392895268 193 ----ANQmalWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK06947 147 rlgsPNE---YVDYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
50-237 6.43e-07

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 49.52  E-value: 6.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSklDETKKEIlekyssiEVRTAAFDFTNAAPSAYKDLLATLNQV---- 125
Cdd:PRK12481  11 AIITGCNTGLGQGMAIGLAKAGADIVGVGVAEA--PETQAQV-------EALGRKFHFITADLIQQKDIDSIVSQAvevm 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 -EIGVLINNVGMsYEYPDVLhkvDGGIERLANITTINTLPPTLLSAGILPQMVAR-KAGVIVNVGSSAGANQMALWAVYS 203
Cdd:PRK12481  82 gHIDILINNAGI-IRRQDLL---EFGNKDWDDVININQKTVFFLSQAVAKQFVKQgNGGKIINIASMLSFQGGIRVPSYT 157
                        170       180       190
                 ....*....|....*....|....*....|....
gi 392895268 204 ATKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK12481 158 ASKSAVMGLTRALATELSQYNINVNAIAPGYMAT 191
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
50-240 9.01e-07

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 49.14  E-value: 9.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNA-APSAYKDLLAtlnqveIG 128
Cdd:PRK12936   9 ALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKAlGQKAEADLEG------VD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 VLINNVGMSYeypdvlhkvDGGIERLA-----NITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYS 203
Cdd:PRK12936  83 ILVNNAGITK---------DGLFVRMSdedwdSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYC 153
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 392895268 204 ATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMS 240
Cdd:PRK12936 154 ASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMT 190
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
52-240 1.24e-06

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 49.03  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  52 VTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEkyssIEVRTAAfDFTNAAPSayKDLLATLNQV-EIGVL 130
Cdd:cd08951   12 ITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPG----AAGVLIG-DLSSLAET--RKLADQVNAIgRFDAV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 131 INNVGMSYEyPDVLHKVDGGIERLAnittINTLPPTLLSAGILPQmvarKAGVIVNVGSSAGANQMA---LW-------- 199
Cdd:cd08951   85 IHNAGILSG-PNRKTPDTGIPAMVA----VNVLAPYVLTALIRRP----KRLIYLSSGMHRGGNASLddiDWfnrgends 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392895268 200 AVYSATKKYVSWLTAILRKEYehQGITVQTIAPMMVATKMS 240
Cdd:cd08951  156 PAYSDSKLHVLTLAAAVARRW--KDVSSNAVHPGWVPTKMG 194
PRK07677 PRK07677
short chain dehydrogenase; Provisional
51-133 1.35e-06

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 48.52  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlEKYSSiEVRTAAFDFTN--AAPSAYKDLLATLNQVEig 128
Cdd:PRK07677   5 IITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEI-EQFPG-QVLTVQMDVRNpeDVQKMVEQIDEKFGRID-- 80

                 ....*
gi 392895268 129 VLINN 133
Cdd:PRK07677  81 ALINN 85
PRK05872 PRK05872
short chain dehydrogenase; Provisional
50-239 1.83e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 48.43  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlekYSSIEVRTAAFDFTNAAP--SAYKDLLATLNQveI 127
Cdd:PRK05872  12 VVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAEL---GGDDRVLTVVADVTDLAAmqAAAEEAVERFGG--I 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSyEYPDVLHKVDGGIERLANITTI---NTLPPTllsagiLPQMVARKaGVIVNVGSSAGANQMALWAVYSA 204
Cdd:PRK05872  87 DVVVANAGIA-SGGSVAQVDPDAFRRVIDVNLLgvfHTVRAT------LPALIERR-GYVLQVSSLAAFAAAPGMAAYCA 158
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 392895268 205 TKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK05872 159 SKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDL 193
PRK07831 PRK07831
SDR family oxidoreductase;
50-232 2.28e-06

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 48.11  E-value: 2.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATD-GIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAApsaykDLLATLNQVE-- 126
Cdd:PRK07831  20 VLVTAAAGtGIGSATARRALEEGARVVISDIHERRLGETADELAAELGLGRVEAVVCDVTSEA-----QVDALIDAAVer 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 ---IGVLINNVGMSYEYPdVLHKVDGGIERLANITTINTLPPTllsAGILPQMVARK-AGVIVNVGSSAGANQMALWAVY 202
Cdd:PRK07831  95 lgrLDVLVNNAGLGGQTP-VVDMTDDEWSRVLDVTLTGTFRAT---RAALRYMRARGhGGVIVNNASVLGWRAQHGQAHY 170
                        170       180       190
                 ....*....|....*....|....*....|...
gi 392895268 203 SATKKYVSWLT---AILRKEYehqGITVQTIAP 232
Cdd:PRK07831 171 AAAKAGVMALTrcsALEAAEY---GVRINAVAP 200
PRK07856 PRK07856
SDR family oxidoreductase;
38-240 2.77e-06

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 47.62  E-value: 2.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  38 PIDLKKRAgaswAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSkldetkkeilekySSIEVRTAAFDFTNAA-PSAYK 116
Cdd:PRK07856   1 NLDLTGRV----VLVTGGTRGIGAGIARAFLAAGATVVVCGRRAP-------------ETVDGRPAEFHAADVRdPDQVA 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 117 DLLATLnqVE----IGVLINNVGMSyeyPDVLhKVDGGIERLANITTINTLPPTLLSAGILPQMVARKA-GVIVNVGSSA 191
Cdd:PRK07856  64 ALVDAI--VErhgrLDVLVNNAGGS---PYAL-AAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGgGSIVNIGSVS 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 392895268 192 GANQMALWAVYSATKKYVSWLTAILRKEYEHQgITVQTIAPMMVATKMS 240
Cdd:PRK07856 138 GRRPSPGTAAYGAAKAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQS 185
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
39-96 3.01e-06

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 48.30  E-value: 3.01e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392895268  39 IDLKKragASWAVVtGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYS 96
Cdd:COG5322  147 IDLKK---ATVAVV-GATGSIGSVCARLLAREVKRLTLVARNLERLEELAEEILRNPG 200
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
50-239 3.46e-06

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 48.29  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSK--LDETKKEilekyssIEVRTAAFDFTNA-APSAYKDLLATlNQVE 126
Cdd:PRK08261 213 ALVTGAARGIGAAIAEVLARDGAHVVCLDVPAAGeaLAAVANR-------VGGTALALDITAPdAPARIAEHLAE-RHGG 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IGVLINNvgmsyeypdvlhkvdGGIER---LANIT--------TINTLPPTLLSAGILPQMVARKAGVIVNVGSSAG--- 192
Cdd:PRK08261 285 LDIVVHN---------------AGITRdktLANMDearwdsvlAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGiag 349
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392895268 193 ----ANqmalwavYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK08261 350 nrgqTN-------YAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQM 393
PRK06139 PRK06139
SDR family oxidoreductase;
51-237 4.93e-06

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 47.41  E-value: 4.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKysSIEVRTAAFDFTNAApsAYKDLLATLNQV--EIG 128
Cdd:PRK06139  11 VITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRAL--GAEVLVVPTDVTDAD--QVKALATQAASFggRID 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 VLINNVGMS-----YEYPdvlhkvdggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYS 203
Cdd:PRK06139  87 VWVNNVGVGavgrfEETP---------IEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYS 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 392895268 204 ATKKYVSWLTAILRKEY-EHQGITVQTIAPMMVAT 237
Cdd:PRK06139 158 ASKFGLRGFSEALRGELaDHPDIHVCDVYPAFMDT 192
PRK08263 PRK08263
short chain dehydrogenase; Provisional
52-232 5.70e-06

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 46.95  E-value: 5.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  52 VTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKkeilEKYSSiEVRTAAFDFTNAApsaykdllATLNQVE----- 126
Cdd:PRK08263   8 ITGASRGFGRAWTEAALERGDRVVATARDTATLADLA----EKYGD-RLLPLALDVTDRA--------AVFAAVEtaveh 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 ---IGVLINNVG-MSYeypdvlhkvdGGIERL------ANITTiNTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQM 196
Cdd:PRK08263  75 fgrLDIVVNNAGyGLF----------GMIEEVtesearAQIDT-NFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAF 143
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 392895268 197 ALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:PRK08263 144 PMSGIYHASKWALEGMSEALAQEVAEFGIKVTLVEP 179
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
50-239 6.16e-06

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 46.54  E-value: 6.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLL-VSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLATLNQVEIg 128
Cdd:PRK12935   9 AIVTGGAKGIGKAITVALAQEGAKVVInYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGKVDI- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 vLINNVGMSYEypDVLHKVdgGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKY 208
Cdd:PRK12935  88 -LVNNAGITRD--RTFKKL--NREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAG 162
                        170       180       190
                 ....*....|....*....|....*....|.
gi 392895268 209 VSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK12935 163 MLGFTKSLALELAKTNVTVNAICPGFIDTEM 193
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
40-237 9.38e-06

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 46.26  E-value: 9.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  40 DLKKRAgaswAVVTGATDGIGKAYAFELARRGFNVLLVSRT-QSKLDETKKEILEK-YSSIEVR---TAAFDFTNAAPSA 114
Cdd:PRK08936   4 DLEGKV----VVITGGSTGLGRAMAVRFGKEKAKVVINYRSdEEEANDVAEEIKKAgGEAIAVKgdvTVESDVVNLIQTA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 115 YKDlLATLNqveigVLINNVGMSYEYPDvlHKVDggIERLANITTINTLPPTLLSAGILPQMVAR-KAGVIVNVGSsagA 193
Cdd:PRK08936  80 VKE-FGTLD-----VMINNAGIENAVPS--HEMS--LEDWNKVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSS---V 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 392895268 194 NQMALW---AVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK08936 147 HEQIPWplfVHYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINT 193
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
58-241 1.12e-05

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: 45.88  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268   58 GIGKAYAFELARRGFNVLLVSRtQSKLDETKKEILEKYSSiEVRTAafDFTNAApsaykDLLATLNQVE-----IGVLIN 132
Cdd:pfam13561   7 GIGWAIARALAEEGAEVVLTDL-NEALAKRVEELAEELGA-AVLPC--DVTDEE-----QVEALVAAAVekfgrLDILVN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  133 NVGMSyeypDVLHK--VDGGIERLANITTINTLPPTLLSAGILPQMvaRKAGVIVNVGSSAGANQMALWAVYSATKKYVS 210
Cdd:pfam13561  78 NAGFA----PKLKGpfLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALE 151
                         170       180       190
                  ....*....|....*....|....*....|.
gi 392895268  211 WLTAILRKEYEHQGITVQTIAPMMVATKMSK 241
Cdd:pfam13561 152 ALTRYLAVELGPRGIRVNAISPGPIKTLAAS 182
PRK05854 PRK05854
SDR family oxidoreductase;
50-135 1.22e-05

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 46.21  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAPSAykDLLATLNQ--VEI 127
Cdd:PRK05854  17 AVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTAVPDAKLSLRALDLSSLASVA--ALGEQLRAegRPI 94

                 ....*...
gi 392895268 128 GVLINNVG 135
Cdd:PRK05854  95 HLLINNAG 102
PRK06123 PRK06123
SDR family oxidoreductase;
50-239 1.54e-05

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 45.54  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAfdfTNAAPSAYKDLLATLNQvEIG- 128
Cdd:PRK06123   5 MIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVVQAIRRQGGEALAVAA---DVADEADVLRLFEAVDR-ELGr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 --VLINNVGMsYEYPDVLHKVDGgiERLANITTINTLPPTLLSAGILPQMVAR---KAGVIVNVGSSAG-ANQMALWAVY 202
Cdd:PRK06123  81 ldALVNNAGI-LEAQMRLEQMDA--ARLTRIFATNVVGSFLCAREAVKRMSTRhggRGGAIVNVSSMAArLGSPGEYIDY 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 392895268 203 SATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:PRK06123 158 AASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEI 194
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
50-237 1.68e-05

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 45.48  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLV-SRTQSKLDETKKEIlekySSIEVRTAAFDFTNAAPSAYKDLLATLNQV--E 126
Cdd:PRK08063   7 ALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEI----EALGRKALAVKANVGDVEKIKEMFAQIDEEfgR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IGVLINNVGMSYEYPdvLHKVDggiERLANIT-TINTLPPTLLSAGILPQMVARKAGVIVNVgSSAGANQ-MALWAVYSA 204
Cdd:PRK08063  83 LDVFVNNAASGVLRP--AMELE---ESHWDWTmNINAKALLFCAQEAAKLMEKVGGGKIISL-SSLGSIRyLENYTTVGV 156
                        170       180       190
                 ....*....|....*....|....*....|...
gi 392895268 205 TKKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK08063 157 SKAALEALTRYLAVELAPKGIAVNAVSGGAVDT 189
PRK08265 PRK08265
short chain dehydrogenase; Provisional
50-232 2.36e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 45.00  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRtqsklDETKKEILEKYSSIEVRTAAFDFTN--AAPSAYKDLLATLNQVEI 127
Cdd:PRK08265   9 AIVTGGATLIGAAVARALVAAGARVAIVDI-----DADNGAAVAASLGERARFIATDITDdaAIERAVATVVARFGRVDI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 gvLINNvGMSYeypdvlhkVDGGI-----ERLANItTINTLPPTLLSAGILPQMVARkAGVIVNVGS-SAGANQMALWaV 201
Cdd:PRK08265  84 --LVNL-ACTY--------LDDGLassraDWLAAL-DVNLVSAAMLAQAAHPHLARG-GGAIVNFTSiSAKFAQTGRW-L 149
                        170       180       190
                 ....*....|....*....|....*....|.
gi 392895268 202 YSATKKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:PRK08265 150 YPASKAAIRQLTRSMAMDLAPDGIRVNSVSP 180
PRK06197 PRK06197
short chain dehydrogenase; Provisional
50-138 2.44e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 45.40  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAP--SAYKDLLAtlNQVEI 127
Cdd:PRK06197  19 AVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAATPGADVTLQELDLTSLASvrAAADALRA--AYPRI 96
                         90
                 ....*....|.
gi 392895268 128 GVLINNVGMSY 138
Cdd:PRK06197  97 DLLINNAGVMY 107
PRK06500 PRK06500
SDR family oxidoreductase;
50-237 2.85e-05

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 44.56  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEkySSIEVRTAAFDFtnaapSAYKDLLATLNQ--VEI 127
Cdd:PRK06500   9 ALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGE--SALVIRADAGDV-----AAQKALAQALAEafGRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYEYPdvLHKVD-GGIERLANittINTLPPTLLSAGILPqMVARKAGVIVNVGSSAGANqMALWAVYSATK 206
Cdd:PRK06500  82 DAVFINAGVAKFAP--LEDWDeAMFDRSFN---TNVKGPYFLIQALLP-LLANPASIVLNGSINAHIG-MPNSSVYAASK 154
                        170       180       190
                 ....*....|....*....|....*....|.
gi 392895268 207 KYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK06500 155 AALLSLAKTLSGELLPRGIRVNAVSPGPVQT 185
PRK08416 PRK08416
enoyl-ACP reductase;
51-124 3.49e-05

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 44.38  E-value: 3.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKL-DETKKEILEKYsSIEVRTAAFDFTNaaPSAYKDLLATLNQ 124
Cdd:PRK08416  12 VISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVEEaNKIAEDLEQKY-GIKAKAYPLNILE--PETYKELFKKIDE 83
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
50-135 4.76e-05

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 44.91  E-value: 4.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLATLnqvEIGV 129
Cdd:COG3347  428 ALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGADAVDATDVDVTAEAAVAAAFGFAGL---DIGG 504

                 ....*.
gi 392895268 130 LINNVG 135
Cdd:COG3347  505 SDIGVA 510
PRK05875 PRK05875
short chain dehydrogenase; Provisional
51-277 5.43e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 44.02  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNaapsayKDLLATLnqveigvl 130
Cdd:PRK05875  11 LVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEALKGAGAVRYEPADVTD------EDQVARA-------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 131 innVGMSYEYPDVLHKV---DGGIERLANITTI-------------NTLPPTLLSAGilPQMVARKAGVIVNVGSSAGAN 194
Cdd:PRK05875  77 ---VDAATAWHGRLHGVvhcAGGSETIGPITQIdsdawrrtvdlnvNGTMYVLKHAA--RELVRGGGGSFVGISSIAASN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 195 QMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMskvkrTSFFTPDGAVFAKSALNT----VGNT---- 266
Cdd:PRK05875 152 THRWFGAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDL-----VAPITESPELSADYRACTplprVGEVedva 226
                        250
                 ....*....|....*...
gi 392895268 267 -------SDTTGYITHQL 277
Cdd:PRK05875 227 nlamfllSDAASWITGQV 244
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
51-206 6.56e-05

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: 43.60  E-value: 6.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELAR---RGFNVLLVSRTQSKlDETKKEILEKYSSIEVRTAAFDFTNaaPSAYKDLLATLNQVEI 127
Cdd:cd09806    4 LITGCSSGIGLHLAVRLASdpsKRFKVYATMRDLKK-KGRLWEAAGALAGGTLETLQLDVCD--SKSVAAAVERVTERHV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 128 GVLINNVGMSYEYPdvlhkVDG-GIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATK 206
Cdd:cd09806   81 DVLVCNAGVGLLGP-----LEAlSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASK 155
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
50-239 7.53e-05

Short-chain dehydrogenases/reductases (SDR); 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 (KR) 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: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 42.89  E-value: 7.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRG-FNVLLVSRTQskldetkkeilekyssievrtaafdftnaapsaykdllatlnqveig 128
Cdd:cd02266    1 VLVTGGSGGIGGAIARWLASRGsPKVLVVSRRD----------------------------------------------- 33
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 129 VLINNVGMSYEYPdVLHKVDGGIERLANITTINTLppTLLSAgILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKY 208
Cdd:cd02266   34 VVVHNAAILDDGR-LIDLTGSRIERAIRANVVGTR--RLLEA-ARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAA 109
                        170       180       190
                 ....*....|....*....|....*....|.
gi 392895268 209 VSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:cd02266  110 LDGLAQQWASEGWGNGLPATAVACGTWAGSG 140
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
50-237 8.96e-05

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 43.32  E-value: 8.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKldETKKEIL---EKYSSIEVRTAAFDftnAAPSAYKDLLATLNQVE 126
Cdd:PRK08993  13 AVVTGCDTGLGQGMALGLAEAGCDIVGINIVEPT--ETIEQVTalgRRFLSLTADLRKID---GIPALLERAVAEFGHID 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 127 IgvLINNVGMSYEYpdvlHKVDGGIERLANITTINTLPPTLLSAGILPQMVAR-KAGVIVNVGSSAGANQMALWAVYSAT 205
Cdd:PRK08993  88 I--LVNNAGLIRRE----DAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgNGGKIINIASMLSFQGGIRVPSYTAS 161
                        170       180       190
                 ....*....|....*....|....*....|..
gi 392895268 206 KKYVSWLTAILRKEYEHQGITVQTIAPMMVAT 237
Cdd:PRK08993 162 KSGVMGVTRLMANEWAKHNINVNAIAPGYMAT 193
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
51-232 1.98e-04

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 42.06  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEiLEKYSSIEVRTAAFDFTNAAPSAYKDLLATLNqvEIGVL 130
Cdd:PRK05786   9 AIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKT-LSKYGNIHYVVGDVSSTESARNVIEKAAKVLN--AIDGL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 131 INNVGMSYEypDVLHKVDGGIERLANittiNTLPPTLLSAGILPQMvaRKAGVIVNVGSSAGA-----NQMAlwavYSAT 205
Cdd:PRK05786  86 VVTVGGYVE--DTVEEFSGLEEMLTN----HIKIPLYAVNASLRFL--KEGSSIVLVSSMSGIykaspDQLS----YAVA 153
                        170       180
                 ....*....|....*....|....*..
gi 392895268 206 KKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:PRK05786 154 KAGLAKAVEILASELLGRGIRVNGIAP 180
PRK06194 PRK06194
hypothetical protein; Provisional
50-91 2.38e-04

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 41.92  E-value: 2.38e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEI 91
Cdd:PRK06194   9 AVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAEL 50
PLN02253 PLN02253
xanthoxin dehydrogenase
50-240 3.29e-04

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 41.73  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSrTQSKLDETKKEILEK-----YSSIEVRTAAfDFTNAAPSAYKDlLATLNq 124
Cdd:PLN02253  21 ALVTGGATGIGESIVRLFHKHGAKVCIVD-LQDDLGQNVCDSLGGepnvcFFHCDVTVED-DVSRAVDFTVDK-FGTLD- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 125 veigVLINNVGMS-YEYPDVLHKVDGGIERLANITTINTLPPTLLSAGIlpqMVARKAGVIVNVGSSAGANQMALWAVYS 203
Cdd:PLN02253  97 ----IMVNNAGLTgPPCPDIRNVELSEFEKVFDVNVKGVFLGMKHAARI---MIPLKKGSIVSLCSVASAIGGLGPHAYT 169
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 392895268 204 ATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKMS 240
Cdd:PLN02253 170 GSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALA 206
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
52-111 3.94e-04

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 41.45  E-value: 3.94e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392895268  52 VTGATDGIGKAYAFELARRGFN-VLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAA 111
Cdd:cd05237    7 VTGGAGSIGSELVRQILKFGPKkLIVFDRDENKLHELVRELRSRFPHDKLRFIIGDVRDKE 67
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
50-232 4.99e-04

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: 40.84  E-value: 4.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSrtqskLDEtkkEILEKYSSIE---VRTAAF--DFTNAAP--SAYKDLLATL 122
Cdd:cd08943    4 ALVTGGASGIGLAIAKRLAAEGAAVVVAD-----IDP---EIAEKVAEAAqggPRALGVqcDVTSEAQvqSAFEQAVLEF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 123 NQVEIgvLINNVGMSYEYPdvlhKVDGGIERLANITTINTLPPTLLSAGILPQM-VARKAGVIVNVGSSAGANQMALWAV 201
Cdd:cd08943   76 GGLDI--VVSNAGIATSSP----IAETSLEDWNRSMDINLTGHFLVSREAFRIMkSQGIGGNIVFNASKNAVAPGPNAAA 149
                        170       180       190
                 ....*....|....*....|....*....|.
gi 392895268 202 YSATKKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:cd08943  150 YSAAKAAEAHLARCLALEGGEDGIRVNTVNP 180
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
50-108 8.55e-04

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 40.27  E-value: 8.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFT 108
Cdd:cd09809    4 IIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEEWHKARVEAMTLDLA 62
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
51-239 9.88e-04

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: 40.17  E-value: 9.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSkldetkkEILEKYSSIEVRTAAFDftnaapsaykDLLATLNQVeIGVL 130
Cdd:cd05328    3 VITGAASGIGAATAELLEDAGHTVIGIDLREA-------DVIADLSTPEGRAAAIA----------DVLARCSGV-LDGL 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 131 INNVGMsyeypdvlhkvdGGIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNVGSSAGAN---------------- 194
Cdd:cd05328   65 VNCAGV------------GGTTVAGLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAGwaqdklelakalaagt 132
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 392895268 195 ---QMALW--------AVYSATKKYVS-WLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:cd05328  133 earAVALAehagqpgyLAYAGSKEALTvWTRRRAATWLYGAGVRVNTVAPGPVETPI 189
PRK09134 PRK09134
SDR family oxidoreductase;
50-187 1.22e-03

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 39.91  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLL-VSRTQSKLDETKKEIlekySSIEVRTAAF--DFTNAAPSA--YKDLLATLNq 124
Cdd:PRK09134  12 ALVTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALAAEI----RALGRRAVALqaDLADEAEVRalVARASAALG- 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392895268 125 vEIGVLINNVGMsYEYpDVLHKVDggIERLANITTINTLPPTLLSAGILPQMVARKAGVIVNV 187
Cdd:PRK09134  87 -PITLLVNNASL-FEY-DSAASFT--RASWDRHMATNLRAPFVLAQAFARALPADARGLVVNM 144
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
50-141 1.73e-03

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 39.25  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAApsaykDLLATLNQVE--- 126
Cdd:PRK12384   5 AVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEGMAYGFGADATSEQ-----SVLALSRGVDeif 79
                         90
                 ....*....|....*..
gi 392895268 127 --IGVLINNVGMSYEYP 141
Cdd:PRK12384  80 grVDLLVYNAGIAKAAF 96
PLN02657 PLN02657
3,8-divinyl protochlorophyllide a 8-vinyl reductase
40-111 2.03e-03

3,8-divinyl protochlorophyllide a 8-vinyl reductase


Pssm-ID: 178263 [Multi-domain]  Cd Length: 390  Bit Score: 39.36  E-value: 2.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392895268  40 DLKKRAGASWAVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKL--DETKKEILEKYSSIEVRTAafDFTNAA 111
Cdd:PLN02657  53 FRSKEPKDVTVLVVGATGYIGKFVVRELVRRGYNVVAVAREKSGIrgKNGKEDTKKELPGAEVVFG--DVTDAD 124
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
44-239 2.05e-03

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: 39.06  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  44 RAGASWAVVTGATDGIGKAYAFELARRGFNVLLVSRtqsklDETKKEILEKYSSIEVRTAAFdFTNAAPSAYKDLLATLN 123
Cdd:cd08933    6 RYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCAR-----GEAAGQALESELNRAGPGSCK-FVPCDVTKEEDIKTLIS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 124 QV-----EIGVLINNVGM--SYEYPDvlhkvDGGIERLANITTINTLPPTLLSAGILPQMvaRKA-GVIVNVGSSAGANQ 195
Cdd:cd08933   80 VTverfgRIDCLVNNAGWhpPHQTTD-----ETSAQEFRDLLNLNLISYFLASKYALPHL--RKSqGNIINLSSLVGSIG 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 392895268 196 MALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAPMMVATKM 239
Cdd:cd08933  153 QKQAAPYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPL 196
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
50-91 2.08e-03

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: 38.66  E-value: 2.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEI 91
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEV 42
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
12-130 2.11e-03

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: 39.66  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  12 YVALAAVAYRLLTIFSNILGPyvllSPIDLKKRAGASWA-----VVTGATDGIGKAYAFELARR-GFNVLLVSRTQskLD 85
Cdd:cd08953  169 APGAAEVRYRDGLRYVQTLEP----LPLPAGAAASAPLKpggvyLVTGGAGGIGRALARALARRyGARLVLLGRSP--LP 242
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 392895268  86 ETKKEILEKYSSIEVRTAAF-----DFTNAA--PSAYKDLLATLNQVEiGVL 130
Cdd:cd08953  243 PEEEWKAQTLAALEALGARVlyisaDVTDAAavRRLLEKVRERYGAID-GVI 293
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
50-79 2.14e-03

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: 38.84  E-value: 2.14e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 392895268   50 AVVTGATDGIGKAYAFELARRGFNVLLVSR 79
Cdd:TIGR04504   4 ALVTGAARGIGAATVRRLAADGWRVVAVDL 33
PRK08862 PRK08862
SDR family oxidoreductase;
52-189 2.63e-03

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 38.55  E-value: 2.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  52 VTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNAAPSAYKDLLATLNQVeIGVLI 131
Cdd:PRK08862  10 ITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCSALTDNVYSFQLKDFSQESIRHLFDAIEQQFNRA-PDVLV 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392895268 132 NNVgMSYEYPDVL--HKVDGGIERLANITTintlppTLLSAGilpQMVA------RKAGVIVNVGS 189
Cdd:PRK08862  89 NNW-TSSPLPSLFdeQPSESFIQQLSSLAS------TLFTYG---QVAAermrkrNKKGVIVNVIS 144
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
50-192 3.03e-03

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: 38.65  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  50 AVVTGATDGIGKAYAFELARRG-FNVLLVSRTQSKLDETKKEIL---EKYSSIEVRTAAFDftnAAPSAYKDLLATLNQv 125
Cdd:cd09810    4 VVITGASSGLGLAAAKALARRGeWHVVMACRDFLKAEQAAQEVGmpkDSYSVLHCDLASLD---SVRQFVDNFRRTGRP- 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 126 eIGVLINNVGMSYEYPDVLHKVDGGIERlanITTINTLPPTLLSAGILPQMvARKAGV---IVNVGSSAG 192
Cdd:cd09810   80 -LDALVCNAAVYLPTAKEPRFTADGFEL---TVGVNHLGHFLLTNLLLEDL-QRSENAsprIVIVGSITH 144
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
165-232 3.27e-03

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: 38.33  E-value: 3.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392895268 165 PTLLSAGILPQMVARKAGVIVNVGSSAGANQMALWAVYSATKKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:cd05361  108 PFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGP 175
PRK05884 PRK05884
SDR family oxidoreductase;
51-232 3.28e-03

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 38.25  E-value: 3.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEIlekyssiEVRTAAFDftNAAPSAYKDLLATLNQvEIGVL 130
Cdd:PRK05884   4 LVTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVAAKEL-------DVDAIVCD--NTDPASLEEARGLFPH-HLDTI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268 131 INNVGMSYEYPDvlhkvdggiERLANITTI-----NTLPPTLLSAGILPQMVA---RKAGVIVNV---GSSAGAnqmalw 199
Cdd:PRK05884  74 VNVPAPSWDAGD---------PRTYSLADTanawrNALDATVLSAVLTVQSVGdhlRSGGSIISVvpeNPPAGS------ 138
                        170       180       190
                 ....*....|....*....|....*....|...
gi 392895268 200 aVYSATKKYVSWLTAILRKEYEHQGITVQTIAP 232
Cdd:PRK05884 139 -AEAAIKAALSNWTAGQAAVFGTRGITINAVAC 170
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
54-103 3.56e-03

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 38.81  E-value: 3.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 392895268  54 GATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTA 103
Cdd:PRK08655   7 GGTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKELGVEYANDNIDAA 56
PRK08278 PRK08278
SDR family oxidoreductase;
50-80 3.84e-03

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 38.35  E-value: 3.84e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRT 80
Cdd:PRK08278   9 LFITGASRGIGLAIALRAARDGANIVIAAKT 39
PRK07041 PRK07041
SDR family oxidoreductase;
51-111 4.24e-03

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 38.09  E-value: 4.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392895268  51 VVTGATDGIGKAYAFELARRGFNVLLVSRTQSKLDETKKEILEKYssiEVRTAAFDFTNAA 111
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGA---PVRTAALDITDEA 58
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
50-118 5.25e-03

3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other enzymes) catalyzes NADP-dependent sterol C-4 demethylation, as part of steroid biosynthesis. 3-keto reductase is a classical SDR, with a well conserved canonical active site tetrad and fairly well conserved characteristic 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: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 38.14  E-value: 5.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392895268  50 AVVTGATDGIGKAYAFEL-----ARRGFNVLLVSRTQSKLDETKKEILEKYSSIEVRTA--AFDFTNAAP--SAYKDL 118
Cdd:cd08941    4 VLVTGANSGLGLAICERLlaeddENPELTLILACRNLQRAEAACRALLASHPDARVVFDyvLVDLSNMVSvfAAAKEL 81
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
44-124 6.33e-03

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: 37.75  E-value: 6.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895268  44 RAGASWAVVTGATDGIGKAYAFELARRGF-NVLLVSRTQSKLDETKKEILEKYSSIEVRTAAFDFTNaaPSAYKDLLATL 122
Cdd:cd05274  147 GGLDGTYLITGGLGGLGLLVARWLAARGArHLVLLSRRGPAPRAAARAALLRAGGARVSVVRCDVTD--PAALAALLAEL 224

                 ..
gi 392895268 123 NQ 124
Cdd:cd05274  225 AA 226
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
50-84 9.55e-03

atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. 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: 187540 [Multi-domain]  Cd Length: 302  Bit Score: 37.31  E-value: 9.55e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 392895268  50 AVVTGATDGIGKAYAFELARRGFNVLLVSRTQSKL 84
Cdd:cd05229    2 AHVLGASGPIGREVARELRRRGWDVRLVSRSGSKL 36
 
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.
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