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Conserved domains on  [gi|24640442|ref|NP_572420|]
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spidey [Drosophila melanogaster]

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) ...
 52-288 8.13e-119

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: 341.89  E-value: 8.13e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIYDKIREKTTGLNVG 131
Cdd:cd05356   1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSAGDDIYERIEKELEGLDIG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 132 VLVNNVGISYGHPEYFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKA 211
Cdd:cd05356  81 ILVNNVGISHSIPEYFLE---TPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKA 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24640442 212 FVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKIRKASVFAPSPETYVRSALSTLGIATQTAGYLPHALLQLVIHF 288
Cdd:cd05356 158 FLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKSSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARL 234
 
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) ...
 52-288 8.13e-119

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: 341.89  E-value: 8.13e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIYDKIREKTTGLNVG 131
Cdd:cd05356   1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSAGDDIYERIEKELEGLDIG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 132 VLVNNVGISYGHPEYFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKA 211
Cdd:cd05356  81 ILVNNVGISHSIPEYFLE---TPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKA 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24640442 212 FVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKIRKASVFAPSPETYVRSALSTLGIATQTAGYLPHALLQLVIHF 288
Cdd:cd05356 158 FLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKSSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARL 234
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 8-321 1.39e-72

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 227.06  E-value: 1.39e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442    8 VLSLLGGLAIgivgFQVFRKVLPWIYANVVGPkvfgsSVDLSKMGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLE 87
Cdd:PLN02780  18 VLFVLGSLSI----LKFFFTILNWVYVYFLRP-----AKNLKKYGSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   88 KLNVVAKEIGDKYG-VEVRVIDVDFTGG-DEIYDKIREKTTGLNVGVLVNNVGISYGHPEYFldcYKADPPFLRNIVAAN 165
Cdd:PLN02780  89 KLKDVSDSIQSKYSkTQIKTVVVDFSGDiDEGVKRIKETIEGLDVGVLINNVGVSYPYARFF---HEVDEELLKNLIKVN 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  166 IHSVTHMTALFLPGMISQRRGVIINVSSTAG-VIP-NPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PLN02780 166 VEGTTKVTQAVLPGMLKRKKGAIINIGSGAAiVIPsDPLYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKM 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24640442  244 SKIRKASVFAPSPETYVRSALSTLGIATQTAGYLPHALLQLVIhfteAVFGEQFARNIVMKNILGTRKRALRRLAKEQ 321
Cdd:PLN02780 246 ASIRRSSFLVPSSDGYARAALRWVGYEPRCTPYWPHSLIWGLI----SALPESAVDSWRLKFCLQIRKKGQQKDSRKK 319
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
49-264 2.71e-55

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 180.45  E-value: 2.71e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  49 SKMGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEI---YDKIREKt 125
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAA-GARVEVVALDVTDPDAVaalAEAVLAR- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 126 tGLNVGVLVNNVGIsyGHPEYFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSV 205
Cdd:COG0300  80 -FGPIDVLVNNAGV--GGGGPFEE---LDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAA 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640442 206 YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKIRKASVFAP--SPETYVRSAL 264
Cdd:COG0300 154 YAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPllSPEEVARAIL 214
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 53-245 2.80e-52

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 170.49  E-value: 2.80e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442    53 EWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEI---YDKIREKTTGLN 129
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAL-GGKALFIQGDVTDRAQVkalVEQAVERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   130 VgvLVNNVGISYGHPEYFLDcykaDPPFlRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSST 209
Cdd:pfam00106  80 I--LVNNAGITGLGPFSELS----DEDW-ERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSAS 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 24640442   210 KAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:pfam00106 153 KAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTK 188
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 55-251 4.44e-13

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: 68.02  E-value: 4.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442    55 AVVTGSTDGIGKAYAKELARR----GLKLVLISRSLEKLNVVAKEIGDKYG---VEVRVIDVDFTGGDEIYDKIRE---K 124
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAERSglrVVRVSLDLGAEAGLEQLLKALRelpR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   125 TTGLNVGVLVNNVGISYGHPEYFLDCykADPPFLRNIVAANIHSVTHMTALFL---PGMISQRRgVIINVSSTAGVIPNP 201
Cdd:TIGR01500  83 PKGLQRLLLINNAGTLGDVSKGFVDL--SDSTQVQNYWALNLTSMLCLTSSVLkafKDSPGLNR-TVVNISSLCAIQPFK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 24640442   202 LLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM-SKIRKASV 251
Cdd:TIGR01500 160 GWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMqQQVREESV 210
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 56-110 2.54e-03

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 38.23  E-value: 2.54e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24640442     56 VVTGSTDGIGKAYAKELARRG-LKLVLISRSLEKLNVVAKEIGD--KYGVEVRVIDVD 110
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGaRRLVLLSRSGPDAPGAAALLAEleAAGARVTVVACD 61
 
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) ...
 52-288 8.13e-119

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: 341.89  E-value: 8.13e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIYDKIREKTTGLNVG 131
Cdd:cd05356   1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSAGDDIYERIEKELEGLDIG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 132 VLVNNVGISYGHPEYFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKA 211
Cdd:cd05356  81 ILVNNVGISHSIPEYFLE---TPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKA 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24640442 212 FVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKIRKASVFAPSPETYVRSALSTLGIATQTAGYLPHALLQLVIHF 288
Cdd:cd05356 158 FLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKSSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARL 234
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 8-321 1.39e-72

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 227.06  E-value: 1.39e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442    8 VLSLLGGLAIgivgFQVFRKVLPWIYANVVGPkvfgsSVDLSKMGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLE 87
Cdd:PLN02780  18 VLFVLGSLSI----LKFFFTILNWVYVYFLRP-----AKNLKKYGSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   88 KLNVVAKEIGDKYG-VEVRVIDVDFTGG-DEIYDKIREKTTGLNVGVLVNNVGISYGHPEYFldcYKADPPFLRNIVAAN 165
Cdd:PLN02780  89 KLKDVSDSIQSKYSkTQIKTVVVDFSGDiDEGVKRIKETIEGLDVGVLINNVGVSYPYARFF---HEVDEELLKNLIKVN 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  166 IHSVTHMTALFLPGMISQRRGVIINVSSTAG-VIP-NPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PLN02780 166 VEGTTKVTQAVLPGMLKRKKGAIINIGSGAAiVIPsDPLYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKM 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24640442  244 SKIRKASVFAPSPETYVRSALSTLGIATQTAGYLPHALLQLVIhfteAVFGEQFARNIVMKNILGTRKRALRRLAKEQ 321
Cdd:PLN02780 246 ASIRRSSFLVPSSDGYARAALRWVGYEPRCTPYWPHSLIWGLI----SALPESAVDSWRLKFCLQIRKKGQQKDSRKK 319
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
49-264 2.71e-55

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 180.45  E-value: 2.71e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  49 SKMGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEI---YDKIREKt 125
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAA-GARVEVVALDVTDPDAVaalAEAVLAR- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 126 tGLNVGVLVNNVGIsyGHPEYFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSV 205
Cdd:COG0300  80 -FGPIDVLVNNAGV--GGGGPFEE---LDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAA 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640442 206 YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKIRKASVFAP--SPETYVRSAL 264
Cdd:COG0300 154 YAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPllSPEEVARAIL 214
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 53-245 2.80e-52

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 170.49  E-value: 2.80e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442    53 EWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEI---YDKIREKTTGLN 129
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAL-GGKALFIQGDVTDRAQVkalVEQAVERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   130 VgvLVNNVGISYGHPEYFLDcykaDPPFlRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSST 209
Cdd:pfam00106  80 I--LVNNAGITGLGPFSELS----DEDW-ERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSAS 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 24640442   210 KAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:pfam00106 153 KAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTK 188
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 55-245 1.53e-43

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: 149.36  E-value: 1.53e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDV-DFTGGDEIYDKIREKTTGLNVgvL 133
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALGGNAVAVQADVsDEEDVEALVEEALEEFGRLDI--L 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 134 VNNVGISYGHPeyfldCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFV 213
Cdd:cd05233  79 VNNAGIARPGP-----LEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAAL 153

                       170       180       190
                ....*....|....*....|....*....|..
gi 24640442 214 NKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:cd05233 154 EGLTRSLALELAPYGIRVNAVAPGLVDTPMLA 185
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 55-244 2.72e-43

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: 148.79  E-value: 2.72e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKygVEVRVIDV-DFTGGDEIYDKIREKTTGLNVgvL 133
Cdd:COG4221   8 ALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGR--ALAVPLDVtDEAAVEAAVAAAVAEFGRLDV--L 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 134 VNNVGIsyGHPEYFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFV 213
Cdd:COG4221  84 VNNAGV--ALLGPLEE---LDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAV 158

                       170       180       190
                ....*....|....*....|....*....|.
gi 24640442 214 NKFSDDLQTEYKEHGILIQSVQPGFVATNMS 244
Cdd:COG4221 159 RGLSESLRAELRPTGIRVTVIEPGAVDTEFL 189
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 51-243 2.27e-40

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: 141.46  E-value: 2.27e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEI---YDKIREKTTG 127
Cdd:COG1028   5 KGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAA-GGRALAVAADVTDEAAVealVAAAVAAFGR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 128 LNVgvLVNNVGISYGHPeyFLDCykaDPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYS 207
Cdd:COG1028  84 LDI--LVNNAGITPPGP--LEEL---TEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYA 156

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24640442 208 STKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:COG1028 157 ASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPM 192
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 55-247 9.05e-38

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: 134.72  E-value: 9.05e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIYDKIREKTTGL-NVGVL 133
Cdd:cd05346   3 VLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFrDIDIL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 134 VNNVGISYGHPEYfldcYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFV 213
Cdd:cd05346  83 VNNAGLALGLDPA----QEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAV 158

                       170       180       190
                ....*....|....*....|....*....|....
gi 24640442 214 NKFSDDLQTEYKEHGILIQSVQPGFVATNMSKIR 247
Cdd:cd05346 159 RQFSLNLRKDLIGTGIRVTNIEPGLVETEFSLVR 192
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 52-245 5.57e-34

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 124.42  E-value: 5.57e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGdKYGVEVRVIDVDFTGGDEIYDKIREKTTGL-NV 130
Cdd:PRK07666   7 GKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVE-AYGVKVVIATADVSDYEEVTAAIEQLKNELgSI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 GVLVNNVGIS-YGHpeyFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSST 209
Cdd:PRK07666  86 DILINNAGISkFGK---FLE---LDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSAS 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 24640442  210 KAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:PRK07666 160 KFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAV 195
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 56-244 7.72e-34

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: 124.62  E-value: 7.72e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIYDKIRE--KTTGlNVGVL 133
Cdd:cd05332   7 IITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVPLDMSDLEDAEQVVEEalKLFG-GLDIL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 134 VNNVGISYghPEYFLDcYKADPpfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFV 213
Cdd:cd05332  86 INNAGISM--RSLFHD-TSIDV--DRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHAL 160

                       170       180       190
                ....*....|....*....|....*....|.
gi 24640442 214 NKFSDDLQTEYKEHGILIQSVQPGFVATNMS 244
Cdd:cd05332 161 QGFFDSLRAELSEPNISVTVVCPGLIDTNIA 191
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 52-241 2.34e-32

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: 120.46  E-value: 2.34e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGdKYGVEVRVIDVDFTGGDEIyDKIREKTTGLNVG 131
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELR-AGGAGVLAVVADLTDPEDI-DRLVEKAGDAFGR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 132 V--LVNNVGisYGHPEYFLDCYKADppFLRNiVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSST 209
Cdd:cd05344  79 VdiLVNNAG--GPPPGPFAELTDED--WLEA-FDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVA 153

                       170       180       190
                ....*....|....*....|....*....|..
gi 24640442 210 KAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:cd05344 154 RAGLIGLVKTLSRELAPDGVTVNSVLPGYIDT 185
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 55-245 3.76e-32

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: 120.03  E-value: 3.76e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLnvvaKEIGDKYGVEVRVIDVDFTGGDEIyDKIREKTTGLN--VGV 132
Cdd:cd05374   3 VLITGCSSGIGLALALALAAQGYRVIATARNPDKL----ESLGELLNDNLEVLELDVTDEESI-KAAVKEVIERFgrIDV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 133 LVNNVGISYGHPeyFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAF 212
Cdd:cd05374  78 LVNNAGYGLFGP--LEE---TSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAA 152

                       170       180       190
                ....*....|....*....|....*....|...
gi 24640442 213 VNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:cd05374 153 LEALSESLRLELAPFGIKVTIIEPGPVRTGFAD 185
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
51-245 4.71e-31

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 116.80  E-value: 4.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVI--DV-DFTGGDEIYDKIREKTTG 127
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAA-GGEARVLvfDVsDEAAVRALIEAAVEAFGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  128 LNvgVLVNNVGISyghpeyfldcykADPPFLR-------NIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPN 200
Cdd:PRK05653  83 LD--ILVNNAGIT------------RDALLPRmseedwdRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGN 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 24640442  201 PLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:PRK05653 149 PGQTNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDMTE 193
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 51-257 4.78e-29

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 111.47  E-value: 4.78e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLI-SRSLEKLNVVAKEIGdKYGVEVRVIDVDFT---GGDEIYDKIREKTT 126
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIAyDINEEAAQELLEEIK-EEGGDAIAVKADVSseeDVENLVEQIVEKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  127 GLNVgvLVNNVGISYGHPeyFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVY 206
Cdd:PRK05565  83 KIDI--LVNNAGISNFGL--VTDMTDEE---WDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLY 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24640442  207 SSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM-SKIRKASVFAPSPE 257
Cdd:PRK05565 156 SASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMwSSFSEEDKEGLAEE 207
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 55-243 7.91e-29

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 111.05  E-value: 7.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKL-NVVAKEIGDkYGVEVRVIDVDFTGGDEI---YDKIREKTTGLNV 130
Cdd:PRK05557   8 ALVTGASRGIGRAIAERLAAQGANVVINYASSEAGaEALVAEIGA-LGGKALAVQGDVSDAESVeraVDEAKAEFGGVDI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 gvLVNNVGISyghpeyfldcykADPPFLR-------NIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLL 203
Cdd:PRK05557  87 --LVNNAGIT------------RDNLLMRmkeedwdRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQ 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 24640442  204 SVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK05557 153 ANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDM 192
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 55-244 2.90e-28

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: 108.99  E-value: 2.90e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLnvvAKEIGDKYGVEVRVIDV-DFTGGDEIYDKIREKTTGLNVgvL 133
Cdd:cd08932   3 ALVTGASRGIGIEIARALARDGYRVSLGLRNPEDL---AALSASGGDVEAVPYDArDPEDARALVDALRDRFGRIDV--L 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 134 VNNVGIsyGHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFV 213
Cdd:cd08932  78 VHNAGI--GRPTTLREGSDAE---LEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFAL 152

                       170       180       190
                ....*....|....*....|....*....|.
gi 24640442 214 NKFSDDLQTEYKEHGILIQSVQPGFVATNMS 244
Cdd:cd08932 153 RALAHALRQEGWDHGVRVSAVCPGFVDTPMA 183
PRK07454 PRK07454
SDR family oxidoreductase;
55-241 3.14e-28

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 109.28  E-value: 3.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEIYDKIRE-KTTGLNVGVL 133
Cdd:PRK07454   9 ALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRST-GVKAAAYSIDLSNPEAIAPGIAElLEQFGCPDVL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  134 VNNVGISYGHPeyfldcyKADPPFLR--NIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKA 211
Cdd:PRK07454  88 INNAGMAYTGP-------LLEMPLSDwqWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKA 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 24640442  212 FVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK07454 161 ALAAFTKCLAEEERSHGIRVCTITLGAVNT 190
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 52-241 4.00e-28

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: 109.16  E-value: 4.00e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIgDKYGVEVRVIDVDFTGGDEIYDKIREKTTGL-NV 130
Cdd:cd08934   3 GKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADEL-EAEGGKALVLELDVTDEQQVDAAVERTVEALgRL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 131 GVLVNNVGISYGHPeyfldCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTK 210
Cdd:cd08934  82 DILVNNAGIMLLGP-----VEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATK 156

                       170       180       190
                ....*....|....*....|....*....|.
gi 24640442 211 AFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:cd08934 157 FGVNAFSEGLRQEVTERGVRVVVIEPGTVDT 187
FabG-like PRK07231
SDR family oxidoreductase;
55-245 1.18e-27

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 107.99  E-value: 1.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDkyGVEVRVIDVDFTGGDEIyDKIREKTTGL--NVGV 132
Cdd:PRK07231   8 AIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILA--GGRAIAVAADVSDEADV-EAAVAAALERfgSVDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  133 LVNNVGISYGhPEYFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAF 212
Cdd:PRK07231  85 LVNNAGTTHR-NGPLLD---VDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGA 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 24640442  213 VNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:PRK07231 161 VITLTKALAAELGPDKIRVNAVAPVVVETGLLE 193
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 52-245 4.47e-27

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: 106.29  E-value: 4.47e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIgDKYGVEVRVIDVDFTGGDEIYDKIR--EKTTGlN 129
Cdd:cd05347   5 GKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLI-EKEGVEATAFTCDVSDEEAIKAAVEaiEEDFG-K 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 130 VGVLVNNVGISYGHPeyFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSST 209
Cdd:cd05347  83 IDILVNNAGIIRRHP--AEEFPEAE---WRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAAS 157

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24640442 210 KAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:cd05347 158 KGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTE 193
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 57-273 4.76e-27

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: 106.40  E-value: 4.76e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  57 VTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGdkyGVEVRVIDV-DFTGGDEIYDKIREKTTGLNVgvLVN 135
Cdd:COG3967  10 ITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANP---GLHTIVLDVaDPASIAALAEQVTAEFPDLNV--LIN 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 136 NVGISYghPEYFLDcykaDPPFLRNI---VAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAF 212
Cdd:COG3967  85 NAGIMR--AEDLLD----EAEDLADAereITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATKAA 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640442 213 VNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKIRKASVFAPSPETYVRSALStlGIATQT 273
Cdd:COG3967 159 LHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQGGDPRAMPLDEFADEVMA--GLETGK 217
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 56-244 1.05e-26

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 106.18  E-value: 1.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVD-FtggDEIYDKIRekTTGLNVGVLV 134
Cdd:PRK07825   9 AITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGLVVGGPLDVTDPAsF---AAFLDAVE--ADLGPIDVLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  135 NNVGI-SYGHpeyFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFV 213
Cdd:PRK07825  84 NNAGVmPVGP---FLD---EPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKHAV 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 24640442  214 NKFSDDLQTEYKEHGILIQSVQPGFVATNMS 244
Cdd:PRK07825 158 VGFTDAARLELRGTGVHVSVVLPSFVNTELI 188
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 55-260 1.31e-26

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: 105.02  E-value: 1.31e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGdKYGVEVRVIDVDFTGGDEIY---DKIREKttGLNVG 131
Cdd:cd05339   2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVR-KAGGKVHYYKCDVSKREEVYeaaKKIKKE--VGDVT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 132 VLVNNVGISYGHPeyFLDCykaDPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKA 211
Cdd:cd05339  79 ILINNAGVVSGKK--LLEL---PDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKA 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24640442 212 FVNKFSDDLQTE---YKEHGILIQSVQPGFVATNM---SKIRKASVFAPSPETYV 260
Cdd:cd05339 154 AAVGFHESLRLElkaYGKPGIKTTLVCPYFINTGMfqgVKTPRPLLAPILEPEYV 208
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 55-243 1.56e-26

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: 104.94  E-value: 1.56e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIgDKYGVEVRVIDVDFTGGDEI---YDKIREKTTGlnVG 131
Cdd:cd05333   3 ALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEI-KALGGNAAALEADVSDREAVealVEKVEAEFGP--VD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 132 VLVNNVGISyghpeyfldcykADPPFLR-------NIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLS 204
Cdd:cd05333  80 ILVNNAGIT------------RDNLLMRmseedwdAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQA 147

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24640442 205 VYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd05333 148 NYAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDM 186
PRK06181 PRK06181
SDR family oxidoreductase;
55-245 4.98e-26

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 103.90  E-value: 4.98e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDkYGVEVRVIDVDFTGGDE---IYDKIREKTTGLNVg 131
Cdd:PRK06181   4 VIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELAD-HGGEALVVPTDVSDAEAcerLIEAAVARFGGIDI- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  132 vLVNNVGISygHPEYFldCYKADPPFLRNIVAANIHSVTHMTALFLPGMIsQRRGVIINVSSTAGVIPNPLLSVYSSTKA 211
Cdd:PRK06181  82 -LVNNAGIT--MWSRF--DELTDLSVFERVMRVNYLGAVYCTHAALPHLK-ASRGQIVVVSSLAGLTGVPTRSGYAASKH 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 24640442  212 FVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:PRK06181 156 ALHGFFDSLRIELADDGVAVTVVCPGFVATDIRK 189
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 55-245 5.01e-26

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: 103.09  E-value: 5.01e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRG-LKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEI---YDKIREKTTGLNV 130
Cdd:cd05324   3 ALVTGANRGIGFEIVRQLAKSGpGTVILTARDVERGQAAVEKLRAE-GLSVRFHQLDVTDDASIeaaADFVEEKYGGLDI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 131 gvLVNNVGISYGHpeyfLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPllsvYSSTK 210
Cdd:cd05324  82 --LVNNAGIAFKG----FDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLTSA----YGVSK 151

                       170       180       190
                ....*....|....*....|....*....|....*
gi 24640442 211 AFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:cd05324 152 AALNALTRILAKELKETGIKVNACCPGWVKTDMGG 186
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 55-245 9.83e-26

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: 102.72  E-value: 9.83e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVE---VRVIDVDFTGGDEI---YDKIREKttGL 128
Cdd:cd08939   4 VLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANASgqkVSYISADLSDYEEVeqaFAQAVEK--GG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 129 NVGVLVNNVGISygHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSS 208
Cdd:cd08939  82 PPDLVVNCAGIS--IPGLFEDLTAEE---FERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCP 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24640442 209 TKAFVNKFSDDLQTEYKEHGILIQSV------QPGFVATNMSK 245
Cdd:cd08939 157 SKFALRGLAESLRQELKPYNIRVSVVyppdtdTPGFEEENKTK 199
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 52-243 3.12e-25

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: 100.84  E-value: 3.12e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGdkyGVEVRVIDV-DFTGGDEIYDKIreKTTGLNV 130
Cdd:cd05370   5 GNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELP---NIHTIVLDVgDAESVEALAEAL--LSEYPNL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 131 GVLVNNVGISYGH----PEYFLDcyKADppflrNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVY 206
Cdd:cd05370  80 DILINNAGIQRPIdlrdPASDLD--KAD-----TEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVY 152

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24640442 207 SSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd05370 153 CATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTEL 189
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 55-261 1.52e-24

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: 99.33  E-value: 1.52e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEI-GDKYGVEVRVIDVdfTGGDEIYDKIREKTTGLN-VGV 132
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELlNPNPSVEVEILDV--TDEERNQLVIAELEAELGgLDL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 133 LVNNVGISYGHPeyFLDCY-KADppflRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKA 211
Cdd:cd05350  79 VIINAGVGKGTS--LGDLSfKAF----RETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKA 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 24640442 212 FVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKIRKASVFAPSPETYVR 261
Cdd:cd05350 153 ALSSLAESLRYDVKKRGIRVTVINPGFIDTPLTANMFTMPFLMSVEQAAK 202
PRK12826 PRK12826
SDR family oxidoreductase;
51-243 1.93e-24

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 99.22  E-value: 1.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGvEVRVIDVDFTGGDEIYDKIREKTTGLN- 129
Cdd:PRK12826   5 EGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGG-KARARQVDVRDRAALKAAVAAGVEDFGr 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VGVLVNNVGISygHPEYFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVI-PNPLLSVYSS 208
Cdd:PRK12826  84 LDILVANAGIF--PLTPFAE---MDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRvGYPGLAHYAA 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 24640442  209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK12826 159 SKAGLVGFTRALALELAARNITVNSVHPGGVDTPM 193
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 51-241 2.37e-24

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: 99.44  E-value: 2.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLIS-RSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIYDKIR--EKTTG 127
Cdd:cd08940   1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGfGDAAEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAyaQRQFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 128 lNVGVLVNNVGISYGHP--EYFLDCYKAdppflrnIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSV 205
Cdd:cd08940  81 -GVDILVNNAGIQHVAPieDFPTEKWDA-------IIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSA 152

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24640442 206 YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:cd08940 153 YVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLT 188
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 51-241 8.50e-24

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: 97.58  E-value: 8.50e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  51 MGEW----AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIY---DKIRE 123
Cdd:cd05343   1 MERWrgrvALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLFPYQCDLSNEEQILsmfSAIRT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 124 KTTGlnVGVLVNNVGIsyGHPEYFLDCYKAD--PPFLRNIVAANI---HSVTHMTAlflpgmISQRRGVIINVSSTAG-- 196
Cdd:cd05343  81 QHQG--VDVCINNAGL--ARPEPLLSGKTEGwkEMFDVNVLALSIctrEAYQSMKE------RNVDDGHIININSMSGhr 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 24640442 197 VIPNPLLSVYSSTKAFVNKFSDDLQTEYKE--HGILIQSVQPGFVAT 241
Cdd:cd05343 151 VPPVSVFHFYAATKHAVTALTEGLRQELREakTHIRATSISPGLVET 197
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 55-243 9.08e-24

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


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 97.37  E-value: 9.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNvvAKEIGDKYG-VEVRVIDVDFTGGDEI---YDKIREKTTGLNV 130
Cdd:cd05323   3 AIITGGASGIGLATAKLLLKKGAKVAILDRNENPGA--AAELQAINPkVKATFVQCDVTSWEQLaaaFKKAIEKFGRVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 131 gvLVNNVGISYGHPEYFLDCYKADPpflRNIVAANIHSVTHMTALFLPGM---ISQRRGVIINVSSTAGVIPNPLLSVYS 207
Cdd:cd05323  81 --LINNAGILDEKSYLFAGKLPPPW---EKTIDVNLTGVINTTYLALHYMdknKGGKGGVIVNIGSVAGLYPAPQFPVYS 155

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24640442 208 STKAFVNKFSDDL-QTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd05323 156 ASKHGVVGFTRSLaDLLEYKTGVRVNAICPGFTNTPL 192
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
51-243 9.30e-24

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 97.53  E-value: 9.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSlekLNVVAKEIGDKYG-----VEVRVIDV-DFTGGDEIYDKIREK 124
Cdd:PRK12824   1 MKKIALVTGAKRGIGSAIARELLNDGYRVIATYFS---GNDCAKDWFEEYGftedqVRLKELDVtDTEECAEALAEIEEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  125 TTGlnVGVLVNNVGISyghpeyfldcykADPPFLR-------NIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGV 197
Cdd:PRK12824  78 EGP--VDILVNNAGIT------------RDSVFKRmshqewnDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGL 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 24640442  198 IPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK12824 144 KGQFGQTNYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPM 189
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 52-241 2.47e-23

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


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 96.36  E-value: 2.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDK-YGVEVRVIDV-DFTGGDEIYDKIrEKTTGLN 129
Cdd:cd05329   6 GKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKgFKVEGSVCDVsSRSERQELMDTV-ASHFGGK 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 130 VGVLVNNVGISYGHP--EYFLDCYKAdppflrnIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYS 207
Cdd:cd05329  85 LNILVNNAGTNIRKEakDYTEEDYSL-------IMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYG 157

                       170       180       190
                ....*....|....*....|....*....|....
gi 24640442 208 STKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:cd05329 158 ATKGALNQLTRSLACEWAKDNIRVNAVAPWVIAT 191
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 52-257 3.79e-23

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: 95.61  E-value: 3.79e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLnvvaKEIGDKYGVEVRVIDV-DFTGGDEIYDKIREkttglnV 130
Cdd:cd05368   2 GKVALITAAAQGIGRAIALAFAREGANVIATDINEEKL----KELERGPGITTRVLDVtDKEQVAALAKEEGR------I 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 131 GVLVNNVGISygHPEYFLDCYKADPPFLRNIvaaNIHSVTHMTALFLPGMISQRRGVIINVSSTAGVI---PNPLlsVYS 207
Cdd:cd05368  72 DVLFNCAGFV--HHGSILDCEDDDWDFAMNL---NVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIkgvPNRF--VYS 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 24640442 208 STKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKIRKASvfAPSPE 257
Cdd:cd05368 145 TTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERIQA--QPDPE 192
PRK05866 PRK05866
SDR family oxidoreductase;
30-243 6.95e-23

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 95.96  E-value: 6.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   30 PWIYANVVGPKVFGSSVDLSkmGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDV 109
Cdd:PRK05866  20 PPISPQLLINRPPRQPVDLT--GKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRA-GGDAMAVPC 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  110 DFTGGDEIyDKIREKTTGL--NVGVLVNNVGISYGHP-----EYFLDcykadppFLRNIvAANIHSVTHMTALFLPGMIS 182
Cdd:PRK05866  97 DLSDLDAV-DALVADVEKRigGVDILINNAGRSIRRPlaeslDRWHD-------VERTM-VLNYYAPLRLIRGLAPGMLE 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24640442  183 QRRGVIINVsSTAGVIPN--PLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK05866 168 RGDGHIINV-ATWGVLSEasPLFSVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPM 229
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 57-247 7.90e-23

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 94.82  E-value: 7.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   57 VTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKygveVRVIDVDFTGGDEIYDKIREKTTGL-NVGVLVN 135
Cdd:PRK10538   5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDN----LYIAQLDVRNRAAIEEMLASLPAEWrNIDVLVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  136 NVGISYG-HPeyfldCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFVN 214
Cdd:PRK10538  81 NAGLALGlEP-----AHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVR 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 24640442  215 KFSDDLQTEYKEHGILIQSVQPGFVA-TNMSKIR 247
Cdd:PRK10538 156 QFSLNLRTDLHGTAVRVTDIEPGLVGgTEFSNVR 189
PRK09291 PRK09291
SDR family oxidoreductase;
51-241 1.82e-22

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 94.29  E-value: 1.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKL---VLISRSLEKLNVVAKEIGdkygVEVRVIDVDFTggDEiYDkiREKTTG 127
Cdd:PRK09291   1 MSKTILITGAGSGFGREVALRLARKGHNViagVQIAPQVTALRAEAARRG----LALRVEKLDLT--DA-ID--RAQAAE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  128 LNVGVLVNNVGISYGHPeyfldcyKADPPF--LRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSV 205
Cdd:PRK09291  72 WDVDVLLNNAGIGEAGA-------VVDIPVelVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGA 144

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 24640442  206 YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK09291 145 YCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLT 180
PRK05855 PRK05855
SDR family oxidoreductase;
52-253 2.20e-22

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 97.36  E-value: 2.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDkYGVEVRVIDVDFTGGDEIYDKIREKTTGLNV- 130
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRA-AGAVAHAYRVDVSDADAMEAFAEWVRAEHGVp 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 GVLVNNVGIsyGHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRR-GVIINVSSTAGVIPNPLLSVYSST 209
Cdd:PRK05855 394 DIVVNNAGI--GMAGGFLDTSAED---WDRVLDVNLWGVIHGCRLFGRQMVERGTgGHIVNVASAAAYAPSRSLPAYATS 468

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 24640442  210 KAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNmskIRKASVFA 253
Cdd:PRK05855 469 KAAVLMLSECLRAELAAAGIGVTAICPGFVDTN---IVATTRFA 509
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 52-243 4.28e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 93.88  E-value: 4.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDV-DFTGGDEIYDKIREKTTGlnV 130
Cdd:PRK05872   9 GKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVLTVVADVtDLAAMQAAAEEAVERFGG--I 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 GVLVNNVGISYGHPeyFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMIsQRRGVIINVSSTAGVIPNPLLSVYSSTK 210
Cdd:PRK05872  87 DVVVANAGIASGGS--VAQ---VDPDAFRRVIDVNLLGVFHTVRATLPALI-ERRGYVLQVSSLAAFAAAPGMAAYCASK 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 24640442  211 AFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK05872 161 AGVEAFANALRLEVAHHGVTVGSAYLSWIDTDL 193
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 51-243 9.04e-22

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 92.24  E-value: 9.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRS-LEKLNVVAKEIGDkYGVEVRVIDVDFTGGDEIYDKIRE--KTTG 127
Cdd:PRK12825   5 MGRVALVTGAARGLGRAIALRLARAGADVVVHYRSdEEAAEELVEAVEA-LGRRAQAVQADVTDKAALEAAVAAavERFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  128 lNVGVLVNNVGISYGHP--EYFLDCYkadppflRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSV 205
Cdd:PRK12825  84 -RIDILVNNAGIFEDKPlaDMSDDEW-------DEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSN 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 24640442  206 YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK12825 156 YAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDM 193
PRK06182 PRK06182
short chain dehydrogenase; Validated
 55-242 9.87e-22

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 92.72  E-value: 9.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKeigdkYGVevRVIDVDFTGGDEI---YDKIREKTTGlnVG 131
Cdd:PRK06182   6 ALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLAS-----LGV--HPLSLDVTDEASIkaaVDTIIAEEGR--ID 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  132 VLVNNVGI-SYGHPEyfldcykaDPPFL--RNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSS 208
Cdd:PRK06182  77 VLVNNAGYgSYGAIE--------DVPIDeaRRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHA 148

                        170       180       190
                 ....*....|....*....|....*....|....
gi 24640442  209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATN 242
Cdd:PRK06182 149 TKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTE 182
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 51-236 1.01e-21

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: 92.07  E-value: 1.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDkygvEVRVIDVDFTGGDEIYDKIR---EKTTG 127
Cdd:cd05345   4 EGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGE----AAIAIQADVTKRADVEAMVEaalSKFGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 128 LNVgvLVNNVGISYgHPEYFLDCYKADppFLRnIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYS 207
Cdd:cd05345  80 LDI--LVNNAGITH-RNKPMLEVDEEE--FDR-VFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYN 153

                       170       180
                ....*....|....*....|....*....
gi 24640442 208 STKAFVNKFSDDLQTEYKEHGILIQSVQP 236
Cdd:cd05345 154 ASKGWVVTATKAMAVELAPRNIRVNCLCP 182
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 55-245 1.37e-21

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: 91.70  E-value: 1.37e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIgDKYGV---EVRVIDVDFTGGDEIyDKIREKTTGL--N 129
Cdd:cd05364   6 AIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSC-LQAGVsekKILLVVADLTEEEGQ-DRIISTTLAKfgR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 130 VGVLVNNVGISYghPEYFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRrGVIINVSSTAGVIPNPLLSVYSST 209
Cdd:cd05364  84 LDILVNNAGILA--KGGGED---QDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGGRSFPGVLYYCIS 157

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24640442 210 KAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:cd05364 158 KAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHR 193
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 47-246 1.51e-21

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: 91.38  E-value: 1.51e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  47 DLSKMGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGdkyGVEVRVIDVdftgGDeiYDKIREKTT 126
Cdd:cd05351   2 ELDFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECP---GIEPVCVDL----SD--WDATEEALG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 127 GLN-VGVLVNNVGISYGHPeyFLDCYKADppFLRNIvAANIHSVTHMTALFLPGMISQR-RGVIINVSSTAGVIPNPLLS 204
Cdd:cd05351  73 SVGpVDLLVNNAAVAILQP--FLEVTKEA--FDRSF-DVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHT 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24640442 205 VYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKI 246
Cdd:cd05351 148 VYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRD 189
PRK09072 PRK09072
SDR family oxidoreductase;
56-243 1.83e-21

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 91.54  E-value: 1.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIYDKIREKTTGLNvgVLVN 135
Cdd:PRK09072   9 LLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGRHRWVVADLTSEAGREAVLARAREMGGIN--VLIN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  136 NVGISygHPEYFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFVNK 215
Cdd:PRK09072  87 NAGVN--HFALLED---QDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFALRG 161

                        170       180
                 ....*....|....*....|....*...
gi 24640442  216 FSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK09072 162 FSEALRRELADTGVRVLYLAPRATRTAM 189
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 55-257 1.93e-21

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: 91.09  E-value: 1.93e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIgDKYGVEVRVIDVDFTGGDEIYDKIREKTTGL-NVGVL 133
Cdd:cd05365   2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAI-QQAGGQAIGLECNVTSEQDLEAVVKATVSQFgGITIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 134 VNNVGISYGHPEyfldcykaDPPFLRNIVAA----NIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSST 209
Cdd:cd05365  81 VNNAGGGGPKPF--------DMPMTEEDFEWafklNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSS 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 24640442 210 KAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSkirkASVFAPSPE 257
Cdd:cd05365 153 KAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDAL----ASVLTPEIE 196
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 56-247 2.17e-21

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: 90.81  E-value: 2.17e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  56 VVTGSTDGIGKAYAKELARRGL--KLVLISRSLEKLNVVAKEIgdKYGVEVRVIDVDFT---GGDEIYDKIREKTTGLNV 130
Cdd:cd05367   3 ILTGASRGIGRALAEELLKRGSpsVVVLLARSEEPLQELKEEL--RPGLRVTTVKADLSdaaGVEQLLEAIRKLDGERDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 131 gvLVNNVGISYGHPEYFldcyKADPPFLRNIVAANIHSVTHMTALFLPGMISQR-RGVIINVSSTAGVIPNPLLSVYSST 209
Cdd:cd05367  81 --LINNAGSLGPVSKIE----FIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGlKKTVVNVSSGAAVNPFKGWGLYCSS 154

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24640442 210 KAFVNKFSDDLQTEykEHGILIQSVQPGFVATNM-SKIR 247
Cdd:cd05367 155 KAARDMFFRVLAAE--EPDVRVLSYAPGVVDTDMqREIR 191
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 55-245 2.48e-21

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: 91.37  E-value: 2.48e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEI----GDKYGVEVRVIDVdftggdEIYDKIREKTTGL-- 128
Cdd:cd08935   8 AVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEItalgGRAIALAADVLDR------ASLERAREEIVAQfg 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 129 NVGVLVNNVGISygHPEYFLDCYKADPPFLRNIVAANIHSVTHMTAL-----FLPG------MISQRRGVIINVSSTAGV 197
Cdd:cd08935  82 TVDILINGAGGN--HPDATTDPEHYEPETEQNFFDLDEEGWEFVFDLnlngsFLPSqvfgkdMLEQKGGSIINISSMNAF 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 24640442 198 IPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:cd08935 160 SPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNR 207
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 51-243 3.41e-21

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 90.89  E-value: 3.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRViDV-DFTGGDEIYDKIREKTTGLN 129
Cdd:PRK12829  10 DGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGAKVTATVA-DVaDPAQVERVFDTAVERFGGLD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VgvLVNNVGISygHPEYFLDcyKADPPFLRNIVAANIHSVTHMTALFLPGMI-SQRRGVIINVSSTAGVIPNPLLSVYSS 208
Cdd:PRK12829  89 V--LVNNAGIA--GPTGGID--EITPEQWEQTLAVNLNGQFYFARAAVPLLKaSGHGGVIIALSSVAGRLGYPGRTPYAA 162

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 24640442  209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK12829 163 SKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPR 197
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 55-243 4.21e-21

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 90.73  E-value: 4.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAkeigdkyGVEVRVIDVdfTGGDEIYDKIRE--KTTGlNVGV 132
Cdd:PRK06179   7 ALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIP-------GVELLELDV--TDDASVQAAVDEviARAG-RIDV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  133 LVNNVGISY--GHPEYFLDCYKAdppflrnIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTK 210
Cdd:PRK06179  77 LVNNAGVGLagAAEESSIAQAQA-------LFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASK 149

                        170       180       190
                 ....*....|....*....|....*....|...
gi 24640442  211 AFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK06179 150 HAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNF 182
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 55-241 4.81e-21

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 90.33  E-value: 4.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIgDKYGVEVRVIDVDFTGGDEIYDKIR--EKTTGlNVGV 132
Cdd:PRK12429   7 ALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEAL-QKAGGKAIGVAMDVTDEEAINAGIDyaVETFG-GVDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  133 LVNNVGISYGHP--EYFLDCYKAdppflrnIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTK 210
Cdd:PRK12429  85 LVNNAGIQHVAPieDFPTEKWKK-------MIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAK 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 24640442  211 AFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK12429 158 HGLIGLTKVVALEGATHGVTVNAICPGYVDT 188
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 55-268 1.14e-20

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


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 89.00  E-value: 1.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLV-LISRSLEKlnvvAKEIGDKYGVEVRVIDVDFTGGDEIyDKIREKTTglNVGVL 133
Cdd:cd05354   6 VLVTGANRGIGKAFVESLLAHGAKKVyAAVRDPGS----AAHLVAKYGDKVVPLRLDVTDPESI-KAAAAQAK--DVDVV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 134 VNNVGISYGH---PEYFLDCYKADppflrniVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTK 210
Cdd:cd05354  79 INNAGVLKPAtllEEGALEALKQE-------MDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASK 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24640442 211 AFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKirKASVFAPSPETYVRSALSTLG 268
Cdd:cd05354 152 SAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAA--GAGGPKESPETVAEAVLKALK 207
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 55-264 1.39e-20

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: 88.56  E-value: 1.39e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISR-SLEKLNVVAKEIGDKyGVEVRVI--DVDFTGG-DEIYDKIREKTTGLNV 130
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVINYRkSKDAAAEVAAEIEEL-GGKAVVVraDVSQPQDvEEMFAAVKERFGRLDV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 131 gvLVNNvgisyGHPEYFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTK 210
Cdd:cd05359  80 --LVSN-----AAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAK 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 24640442 211 AFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKirkasvFAPSPETYVRSAL 264
Cdd:cd05359 153 AALEALVRYLAVELGPRGIRVNAVSPGVIDTDALA------HFPNREDLLEAAA 200
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 52-241 1.63e-20

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 89.18  E-value: 1.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRViDVDFTGGDEI---YDKIREKTTgl 128
Cdd:PRK13394   7 GKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGV-AMDVTNEDAVnagIDKVAERFG-- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  129 NVGVLVNNVGISYGHPEYFLDCYKADppflrNIVAANIHSVTHMTALFLPGMISQRR-GVIINVSSTAGVIPNPLLSVYS 207
Cdd:PRK13394  84 SVDILVSNAGIQIVNPIENYSFADWK-----KMQAIHVDGAFLTTKAALKHMYKDDRgGVVIYMGSVHSHEASPLKSAYV 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 24640442  208 STKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK13394 159 TAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 192
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
52-243 2.69e-20

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 88.32  E-value: 2.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSlEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEIYDKIR--EKTTGlN 129
Cdd:PRK08226   6 GKTALITGALQGIGEGIARVFARHGANLILLDIS-PEIEKLADELCGR-GHRCTAVVADVRDPASVAAAIKraKEKEG-R 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VGVLVNNVGISYGHPeyFLDCYKADPPFLRNIvaaNIHSVTHMTALFLPGMISQRRGVIINVSSTAG-VIPNPLLSVYSS 208
Cdd:PRK08226  83 IDILVNNAGVCRLGS--FLDMSDEDRDFHIDI---NIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGdMVADPGETAYAL 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 24640442  209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK08226 158 TKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPM 192
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 55-244 3.37e-20

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


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 87.98  E-value: 3.37e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEIYDKIREKTTGLN-VGVL 133
Cdd:cd08945   6 ALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREA-GVEADGRTCDVRSVPEIEALVAAAVARYGpIDVL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 134 VNNVGISYGHpeyflDCYKADPPFLRNIVAANIHSVTHMT--ALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKA 211
Cdd:cd08945  85 VNNAGRSGGG-----ATAELADELWLDVVETNLTGVFRVTkeVLKAGGMLERGTGRIINIASTGGKQGVVHAAPYSASKH 159

                       170       180       190
                ....*....|....*....|....*....|...
gi 24640442 212 FVNKFSDDLQTEYKEHGILIQSVQPGFVATNMS 244
Cdd:cd08945 160 GVVGFTKALGLELARTGITVNAVCPGFVETPMA 192
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 47-241 5.47e-20

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 87.52  E-value: 5.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   47 DLSkmGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEIYDKIR--EK 124
Cdd:PRK07523   7 DLT--GRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQ-GLSAHALAFDVTDHDAVRAAIDafEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  125 TTGlNVGVLVNNVGISYGHPeyfLDCYKADPpfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLS 204
Cdd:PRK07523  84 EIG-PIDILVNNAGMQFRTP---LEDFPADA--FERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIA 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 24640442  205 VYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK07523 158 PYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDT 194
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 47-245 7.86e-20

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 86.92  E-value: 7.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   47 DLSkmGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIgDKYGVEVRVIDVDFTGGDEIYDKIREKTT 126
Cdd:PRK08213   9 DLS--GKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHL-EALGIDALWIAADVADEADIERLAEETLE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  127 GL-NVGVLVNNVGISYGHPeyfldcyKADPPF--LRNIVAANIhsvthmTALFL-------PGMISQRRGVIINVSSTAG 196
Cdd:PRK08213  86 RFgHVDILVNNAGATWGAP-------AEDHPVeaWDKVMNLNV------RGLFLlsqavakRSMIPRGYGRIINVASVAG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24640442  197 VIPNPLLSV----YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:PRK08213 153 LGGNPPEVMdtiaYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTR 205
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 52-243 9.93e-20

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: 86.67  E-value: 9.93e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKygveVRVIDVDFTGGDE---IYDKIREKTTGL 128
Cdd:cd05341   5 GKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDA----ARFFHLDVTDEDGwtaVVDTAREAFGRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 129 NVgvLVNNVGISYGHP--EYFLDCYkadppflRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVY 206
Cdd:cd05341  81 DV--LVNNAGILTGGTveTTTLEEW-------RRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAY 151

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24640442 207 SSTKAFVNKFSDD--LQTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd05341 152 NASKGAVRGLTKSaaLECATQGYGIRVNSVHPGYIYTPM 190
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 63-245 1.07e-19

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: 85.95  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442    63 GIGKAYAKELARRGLKLVLISRSlEKLNVVAKEIGDKYGVEVRVIDV-DFTGGDEIYDKIREKTTGLNVgvLVNNVGISY 141
Cdd:pfam13561   7 GIGWAIARALAEEGAEVVLTDLN-EALAKRVEELAEELGAAVLPCDVtDEEQVEALVAAAVEKFGRLDI--LVNNAGFAP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   142 GHPEYFLDCYKADppFLRnIVAANIHSVTHMTALFLPGMisQRRGVIINVSSTAGVIPNPLLSVYSSTKAFVNKFSDDLQ 221
Cdd:pfam13561  84 KLKGPFLDTSRED--FDR-ALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLA 158

                         170       180
                  ....*....|....*....|....
gi 24640442   222 TEYKEHGILIQSVQPGFVATNMSK 245
Cdd:pfam13561 159 VELGPRGIRVNAISPGPIKTLAAS 182
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 55-243 1.07e-19

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 86.70  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVL-ISRSLEKLNVVAKEIgDKYGVEVRVIDVDFT---GGDEIYDKIREKTTGLNV 130
Cdd:PRK06077   9 VVVTGSGRGIGRAIAVRLAKEGSLVVVnAKKRAEEMNETLKMV-KENGGEGIGVLADVStreGCETLAKATIDRYGVADI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 gvLVNNVGISYGHPeyFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMisQRRGVIINVSSTAGVIPNPLLSVYSSTK 210
Cdd:PRK06077  88 --LVNNAGLGLFSP--FLN---VDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSIYGAMK 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 24640442  211 AFVNKFSDDLQTEYKEHgILIQSVQPGFVATNM 243
Cdd:PRK06077 159 AAVINLTKYLALELAPK-IRVNAIAPGFVKTKL 190
PRK07201 PRK07201
SDR family oxidoreductase;
56-257 1.20e-19

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 89.63  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEIYDKIREKTTGL-NVGVLV 134
Cdd:PRK07201 375 LITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAK-GGTAHAYTCDLTDSAAVDHTVKDILAEHgHVDYLV 453

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  135 NNVG--------ISYGHpeyFLDcykadppFLRNIvAANIHSVTHMTALFLPGMISQRRGVIINVSStAGVIPN-PLLSV 205
Cdd:PRK07201 454 NNAGrsirrsveNSTDR---FHD-------YERTM-AVNYFGAVRLILGLLPHMRERRFGHVVNVSS-IGVQTNaPRFSA 521

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 24640442  206 YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM---SKIRKaSVFAPSPE 257
Cdd:PRK07201 522 YVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTPMiapTKRYN-NVPTISPE 575
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 52-245 1.31e-19

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


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 86.51  E-value: 1.31e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYG---VEVRVIDV-DFTGGDEIYDKIREKTTG 127
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGnakVEVIQLDLsSLASVRQFAEEFLARFPR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 128 LNvgVLVNNVGISYghpeyfldcykadPPFLRNI------VAANIHSVTHMTALFLPGMISQRRGVIINVSS---TAGVI 198
Cdd:cd05327  81 LD--ILINNAGIMA-------------PPRRLTKdgfelqFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSiahRAGPI 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24640442 199 PNPLLS-----------VYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:cd05327 146 DFNDLDlennkeyspykAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLR 203
PRK09242 PRK09242
SDR family oxidoreductase;
52-245 1.33e-19

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 86.34  E-value: 1.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKY-GVEVRVIDVDFT---GGDEIYDKIREKTTG 127
Cdd:PRK09242   9 GQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEFpEREVHGLAADVSddeDRRAILDWVEDHWDG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  128 LNVgvLVNNVG--ISYGHPEYFLDCYkadppflRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSV 205
Cdd:PRK09242  89 LHI--LVNNAGgnIRKAAIDYTEDEW-------RGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAP 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 24640442  206 YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:PRK09242 160 YGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTS 199
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 57-244 1.39e-19

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: 86.56  E-value: 1.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  57 VTGSTDGIGKAYAKELARRGLK-----LVLISRSLEKLNVVAKEigdkygvEVRVIDVDFTGGDEI---YDKIREKTTGL 128
Cdd:cd09805   5 ITGCDSGFGNLLAKKLDSLGFTvlagcLTKNGPGAKELRRVCSD-------RLRTLQLDVTKPEQIkraAQWVKEHVGEK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 129 NVGVLVNNVGISyGHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPgMISQRRGVIINVSSTAGVIPNPLLSVYSS 208
Cdd:cd09805  78 GLWGLVNNAGIL-GFGGDEELLPMDD---YRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRVPFPAGGAYCA 152

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24640442 209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMS 244
Cdd:cd09805 153 SKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGIT 188
PRK06949 PRK06949
SDR family oxidoreductase;
43-243 1.40e-19

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 86.35  E-value: 1.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   43 GSSVDLSkmGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIgDKYGVEVRVIDVDFTGGDEIYDKI- 121
Cdd:PRK06949   2 GRSINLE--GKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEI-EAEGGAAHVVSLDVTDYQSIKAAVa 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  122 REKTTGLNVGVLVNNVGISYghPEYFLDCYKADPPFLRN-------IVAANIHSVTHMTALFLPGMISQRRgvIINVSST 194
Cdd:PRK06949  79 HAETEAGTIDILVNNSGVST--TQKLVDVTPADFDFVFDtntrgafFVAQEVAKRMIARAKGAGNTKPGGR--IINIASV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 24640442  195 AGVIPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK06949 155 AGLRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEI 203
PRK07774 PRK07774
SDR family oxidoreductase;
55-245 1.73e-19

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 85.95  E-value: 1.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRViDVDFTGGD---EIYDKIREKTTGLNvg 131
Cdd:PRK07774   9 AIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAV-QVDVSDPDsakAMADATVSAFGGID-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  132 VLVNNVGISYGHPEYFLdcYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNpllSVYSSTKA 211
Cdd:PRK07774  86 YLVNNAAIYGGMKLDLL--ITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLYS---NFYGLAKV 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 24640442  212 FVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:PRK07774 161 GLNGLTQQLARELGGMNIRVNAIAPGPIDTEATR 194
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
51-243 2.05e-19

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 85.93  E-value: 2.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIdVDFTGGDEIY---DKIREKTTG 127
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVK-ADVSDRDQVFaavRQVVDTFGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  128 LNvgVLVNNVGISyghPEYFLDcyKADPPFLRNIVAANIHSVthmtalfLPGM---ISQRR-----GVIINVSSTAGVIP 199
Cdd:PRK08643  80 LN--VVVNNAGVA---PTTPIE--TITEEQFDKVYNINVGGV-------IWGIqaaQEAFKklghgGKIINATSQAGVVG 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 24640442  200 NPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK08643 146 NPELAVYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPM 189
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 55-241 2.38e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 86.90  E-value: 2.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDkYGVEVRVI--DV-DFTGGDEIYDKIREKTTGLNvg 131
Cdd:PRK07109  11 VVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRA-AGGEALAVvaDVaDAEAVQAAADRAEEELGPID-- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  132 VLVNNVGISyghpeYFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKA 211
Cdd:PRK07109  88 TWVNNAMVT-----VFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKH 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 24640442  212 FVNKFSDDLQTEYKEHG--ILIQSVQPGFVAT 241
Cdd:PRK07109 163 AIRGFTDSLRCELLHDGspVSVTMVQPPAVNT 194
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 48-244 2.53e-19

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: 85.46  E-value: 2.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  48 LSKMGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIYDKIRE--KT 125
Cdd:cd05352   4 FSLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQiqKD 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 126 TGlNVGVLVNNVGISYGHPeyFLDcYKADPpfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPN-PLLS 204
Cdd:cd05352  84 FG-KIDILIANAGITVHKP--ALD-YTYEQ--WNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVNrPQPQ 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 24640442 205 V-YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMS 244
Cdd:cd05352 158 AaYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLT 198
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 47-244 3.03e-19

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 84.97  E-value: 3.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   47 DLSkmGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKygveVRVIDVDFTGGDEIY---DKIRE 123
Cdd:PRK12936   3 DLS--GRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGER----VKIFPANLSDRDEVKalgQKAEA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  124 KTTGlnVGVLVNNVGISyghpeyfldcykADPPFLR-------NIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAG 196
Cdd:PRK12936  77 DLEG--VDILVNNAGIT------------KDGLFVRmsdedwdSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVG 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 24640442  197 VIPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMS 244
Cdd:PRK12936 143 VTGNPGQANYCASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMT 190
PRK08264 PRK08264
SDR family oxidoreductase;
55-267 4.94e-19

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 84.17  E-value: 4.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRG-LKLVLISRSLEKLnvvakeigDKYGVEVRVIDVDFTGGDEIYDKIREKTtglNVGVL 133
Cdd:PRK08264   9 VLVTGANRGIGRAFVEQLLARGaAKVYAAARDPESV--------TDLGPRVVPLQLDVTDPASVAAAAEAAS---DVTIL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  134 VNNVGIsYGHPEYFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFV 213
Cdd:PRK08264  78 VNNAGI-FRTGSLLLE---GDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAA 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 24640442  214 NKFSDDLQTEYKEHGILIQSVQPGFVATNMSkiRKASVFAPSPETYVRSALSTL 267
Cdd:PRK08264 154 WSLTQALRAELAPQGTRVLGVHPGPIDTDMA--AGLDAPKASPADVARQILDAL 205
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 52-243 5.19e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 84.38  E-value: 5.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDkygvevRVIDVDFTGGDEIYDKIREKTTglnVG 131
Cdd:PRK07060   9 GKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGC------EPLRLDVGDDAAIRAALAAAGA---FD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  132 VLVNNVGISYGHPEyfLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQ-RRGVIINVSSTAGVIPNPLLSVYSSTK 210
Cdd:PRK07060  80 GLVNCAGIASLESA--LDMTAEG---FDRVMAVNARGAALVARHVARAMIAAgRGGSIVNVSSQAALVGLPDHLAYCASK 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 24640442  211 AFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK07060 155 AALDAITRVLCVELGPHGIRVNSVNPTVTLTPM 187
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 55-267 7.54e-19

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: 83.88  E-value: 7.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRG-LKLVLISRSLEKLNVVAKEIGDkyGVEVRVIDVDFT-GGDEIYDKIREKTTGLNVGV 132
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAALGAS--HSRLHILELDVTdEIAESAEAVAERLGDAGLDV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 133 LVNNVGIsyGHPEYFLDcyKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIP-NPLLSVYS--ST 209
Cdd:cd05325  79 LINNAGI--LHSYGPAS--EVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSIGdNTSGGWYSyrAS 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24640442 210 KAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKiRKASVFAP-SPETYVRSALSTL 267
Cdd:cd05325 155 KAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGG-PFAKNKGPiTPEESVAGLLKVI 212
PRK06914 PRK06914
SDR family oxidoreductase;
55-242 8.53e-19

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 84.69  E-value: 8.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEK---LNVVAKEIGDKYGVEVRVIDV-DFTGGDEIYDKIREKTtglNV 130
Cdd:PRK06914   6 AIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKqenLLSQATQLNLQQNIKVQQLDVtDQNSIHNFQLVLKEIG---RI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 GVLVNNVGISYGH--PEYFLDCYkadppflRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSS 208
Cdd:PRK06914  83 DLLVNNAGYANGGfvEEIPVEEY-------RKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVS 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 24640442  209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATN 242
Cdd:PRK06914 156 SKYALEGFSESLRLELKPFGIDVALIEPGSYNTN 189
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 56-241 1.03e-18

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: 83.20  E-value: 1.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEIYD--KIREKTTGlNVGVL 133
Cdd:cd05360   4 VITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVREL-GGEAIAVVADVADAAQVERaaDTAVERFG-RIDTW 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 134 VNNVGIS-YGHPEyfldcyKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAF 212
Cdd:cd05360  82 VNNAGVAvFGRFE------DVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHA 155

                       170       180       190
                ....*....|....*....|....*....|.
gi 24640442 213 VNKFSDDLQTEYKEHG--ILIQSVQPGFVAT 241
Cdd:cd05360 156 VRGFTESLRAELAHDGapISVTLVQPTAMNT 186
PRK12743 PRK12743
SDR family oxidoreductase;
55-243 1.12e-18

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 83.93  E-value: 1.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEK-LNVVAKEIgDKYGVEVRVIDVDFT---GGDEIYDKIREKTTGLnv 130
Cdd:PRK12743   5 AIVTASDSGIGKACALLLAQQGFDIGITWHSDEEgAKETAEEV-RSHGVRAEIRQLDLSdlpEGAQALDKLIQRLGRI-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 GVLVNNVGIsyGHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQ-RRGVIINVSSTAGVIPNPLLSVYSST 209
Cdd:PRK12743  82 DVLVNNAGA--MTKAPFLDMDFDE---WRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHEHTPLPGASAYTAA 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 24640442  210 KAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK12743 157 KHALGGLTKAMALELVEHGILVNAVAPGAIATPM 190
PRK07035 PRK07035
SDR family oxidoreductase;
47-241 1.60e-18

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 83.14  E-value: 1.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   47 DLSkmGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYG----VEVRVIDVDFTggDEIYDKIR 122
Cdd:PRK07035   5 DLT--GKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGkaeaLACHIGEMEQI--DALFAHIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  123 EKTTGLNvgVLVNNVGisyGHPeYFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPL 202
Cdd:PRK07035  81 ERHGRLD--ILVNNAA---ANP-YFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDF 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 24640442  203 LSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK07035 155 QGIYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDT 193
PRK06484 PRK06484
short chain dehydrogenase; Validated
 55-243 1.66e-18

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 85.67  E-value: 1.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKlnvvAKEIGDKYGVEVRVIDVDFTggDEiyDKIREKTTGL-----N 129
Cdd:PRK06484   8 VLVTGAAGGIGRAACQRFARAGDQVVVADRNVER----ARERADSLGPDHHALAMDVS--DE--AQIREGFEQLhrefgR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VGVLVNNVGISYGHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGV-IINVSSTAGVIPNPLLSVYSS 208
Cdd:PRK06484  80 IDVLVNNAGVTDPTMTATLDTTLEE---FARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYSA 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 24640442  209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK06484 157 SKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQM 191
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 52-244 2.04e-18

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 82.91  E-value: 2.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKlnvVAKEIGDKyGVEvrVIDVDFTGGDEIYDKIRE--KTTGlN 129
Cdd:PRK06463   7 GKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAEN---EAKELREK-GVF--TIKCDVGNRDQVKKSKEVveKEFG-R 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VGVLVNNVGISYGHP-EYFldcykaDPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGV-IPNPLLSVYS 207
Cdd:PRK06463  80 VDVLVNNAGIMYLMPfEEF------DEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgTAAEGTTFYA 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 24640442  208 STKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMS 244
Cdd:PRK06463 154 ITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMT 190
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 52-245 3.14e-18

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: 82.88  E-value: 3.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLE-KLNVVAKEIGDKYGVEVRVIdVDFTGGDEI---YDKIREKTTG 127
Cdd:cd09763   3 GKIALVTGASRGIGRGIALQLGEAGATVYITGRTILpQLPGTAEEIEARGGKCIPVR-CDHSDDDEVealFERVAREQQG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 128 lNVGVLVNNVGISYGhpeyfLDCYKADPPF---------------LRNIVAANIHSVthmtalflPGMISQRRGVIINVS 192
Cdd:cd09763  82 -RLDILVNNAYAAVQ-----LILVGVAKPFweepptiwddinnvgLRAHYACSVYAA--------PLMVKAGKGLIVIIS 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 24640442 193 STAGVipNPLLSV-YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:cd09763 148 STGGL--EYLFNVaYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVL 199
PRK05650 PRK05650
SDR family oxidoreductase;
56-243 3.81e-18

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 82.40  E-value: 3.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEI----GDKYGVEVRVIDV-DFTggdEIYDKIREKTTGLNV 130
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLreagGDGFYQRCDVRDYsQLT---ALAQACEEKWGGIDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 gvLVNNVGISYGhpEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTK 210
Cdd:PRK05650  81 --IVNNAGVASG--GFFEELSLED---WDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAK 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 24640442  211 AFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK05650 154 AGVVALSETLLVELADDEIGVHVVCPSFFQTNL 186
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 57-237 4.13e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 82.66  E-value: 4.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   57 VTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKygVEVRVIDVdfTGGDEIYDKIREKTTglNVG---VL 133
Cdd:PRK06180   9 ITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDR--ALARLLDV--TDFDAIDAVVADAEA--TFGpidVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  134 VNNVGisYGHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFV 213
Cdd:PRK06180  83 VNNAG--YGHEGAIEESPLAE---MRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFAL 157

                        170       180
                 ....*....|....*....|....
gi 24640442  214 NKFSDDLQTEYKEHGILIQSVQPG 237
Cdd:PRK06180 158 EGISESLAKEVAPFGIHVTAVEPG 181
PRK08267 PRK08267
SDR family oxidoreductase;
57-256 5.11e-18

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 81.91  E-value: 5.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   57 VTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVeVRVIDV-DFTGGDEIYDKIREKTTG-LNVgvLV 134
Cdd:PRK08267   6 ITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGNAW-TGALDVtDRAAWDAALADFAAATGGrLDV--LF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  135 NNVGISYGHPeyFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFVN 214
Cdd:PRK08267  83 NNAGILRGGP--FED---IPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVR 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 24640442  215 KFSDDLQTEYKEHGILIQSVQPGFVATNMSKIRKASVFAPSP 256
Cdd:PRK08267 158 GLTEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEVDAGST 199
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 55-237 6.92e-18

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 81.53  E-value: 6.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSlEKLNVVAKEIGDKyGVEVRVIDVD---FTGGDEIYDKIREKTTGLNVg 131
Cdd:PRK12823  11 VVVTGAAQGIGRGVALRAAAEGARVVLVDRS-ELVHEVAAELRAA-GGEALALTADletYAGAQAAMAAAVEAFGRIDV- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  132 vLVNNVGIS-----YGHpeyfldcYKADppflrNIVAANIHSVthMTALF-----LPGMISQRRGVIINVSS--TAGV-- 197
Cdd:PRK12823  88 -LINNVGGTiwakpFEE-------YEEE-----QIEAEIRRSL--FPTLWccravLPHMLAQGGGAIVNVSSiaTRGInr 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 24640442  198 IPnpllsvYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPG 237
Cdd:PRK12823 153 VP------YSAAKGGVNALTASLAFEYAEHGIRVNAVAPG 186
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 52-245 7.25e-18

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: 81.38  E-value: 7.25e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIgDKYGVEVRViDVdftgGDE-----IYDKIREKTT 126
Cdd:cd08944   3 GKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQI-AGGALALRV-DV----TDEqqvaaLFERAVEEFG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 127 GLNVgvLVNNVGISYGHPEYfldcykADPPF--LRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLS 204
Cdd:cd08944  77 GLDL--LVNNAGAMHLTPAI------IDTDLavWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYG 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 24640442 205 VYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:cd08944 149 AYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLL 189
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 55-242 7.96e-18

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 81.87  E-value: 7.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEI----GDKYGVEVRVIDVDFTggDEIYDKIREKTTGLNv 130
Cdd:PRK08277  13 AVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIkaagGEALAVKADVLDKESL--EQARQQILEDFGPCD- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 gVLVNNVG----------ISYGHPEYFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGviPN 200
Cdd:PRK08277  90 -ILINGAGgnhpkattdnEFHELIEPTKTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNA--FT 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 24640442  201 PLLSV--YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATN 242
Cdd:PRK08277 167 PLTKVpaYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE 210
PRK07832 PRK07832
SDR family oxidoreductase;
55-243 8.30e-18

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 81.63  E-value: 8.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYG--VEVRVIDVdftgGDeiYDKIREKTTGLN--- 129
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGtvPEHRALDI----SD--YDAVAAFAADIHaah 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 --VGVLVNNVGIS-------YGHPEYfldcykadppflRNIVAANIHSVTHMTALFLPGMISQRRG-VIINVSSTAGVIP 199
Cdd:PRK07832  77 gsMDVVMNIAGISawgtvdrLTHEQW------------RRMVDVNLMGPIHVIETFVPPMVAAGRGgHLVNVSSAAGLVA 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 24640442  200 NPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK07832 145 LPWHAAYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPL 188
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 51-243 8.83e-18

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: 81.27  E-value: 8.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEI---YDKIREKTTG 127
Cdd:cd05366   1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAGYNAVAVGADVTDKDDVealIDQAVEKFGS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 128 LNVgvLVNNVGISYGHPeyFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQ-RRGVIINVSSTAGVIPNPLLSVY 206
Cdd:cd05366  81 FDV--MVNNAGIAPITP--LLTITEED---LKKVYAVNVFGVLFGIQAAARQFKKLgHGGKIINASSIAGVQGFPNLGAY 153

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24640442 207 SSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd05366 154 SASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEM 190
PRK07063 PRK07063
SDR family oxidoreductase;
52-241 1.04e-17

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 81.25  E-value: 1.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKY-GVEVRVIDVDFTGGDEIYDKIREKTTGLN- 129
Cdd:PRK07063   7 GKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVaGARVLAVPADVTDAASVAAAVAAAEEAFGp 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VGVLVNNVGIS-YGHPeyfLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAG--VIPN--Plls 204
Cdd:PRK07063  87 LDVLVNNAGINvFADP---LAMTDED---WRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAfkIIPGcfP--- 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 24640442  205 vYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK07063 158 -YPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIET 193
PRK05693 PRK05693
SDR family oxidoreductase;
55-245 2.35e-17

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 80.61  E-value: 2.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEigdkyGVEVRVIDV-DFTGGDEIYDKIREKTTGLNVgvL 133
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAAA-----GFTAVQLDVnDGAALARLAEELEAEHGGLDV--L 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  134 VNNVGisYGHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPgMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFV 213
Cdd:PRK05693  77 INNAG--YGAMGPLLDGGVEA---MRRQFETNVFAVVGVTRALFP-LLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAV 150

                        170       180       190
                 ....*....|....*....|....*....|..
gi 24640442  214 NKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:PRK05693 151 HALSDALRLELAPFGVQVMEVQPGAIASQFAS 182
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 48-237 2.64e-17

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 80.06  E-value: 2.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   48 LSKMGEWAVVTGSTDGIGKAYAKELARRGLKLVLI-----SRSLEKLNVVAKEIGDKYGVEvrvidvdftggdEIYDKIR 122
Cdd:PRK06171   5 LNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNAdihggDGQHENYQFVPTDVSSAEEVN------------HTVAEII 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  123 EKTTGLNVgvLVNNVGISYghPEYFLDCYKADPPFLRN------IVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAG 196
Cdd:PRK06171  73 EKFGRIDG--LVNNAGINI--PRLLVDEKDPAGKYELNeaafdkMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAG 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 24640442  197 VIPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPG 237
Cdd:PRK06171 149 LEGSEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPG 189
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 52-243 3.39e-17

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 79.66  E-value: 3.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVL-ISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEIYDKIREKTTGL-N 129
Cdd:PRK12935   6 GKVAIVTGGAKGIGKAITVALAQEGAKVVInYNSSKEAAENLVNELGKE-GHDVYAVQADVSKVEDANRLVEEAVNHFgK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VGVLVNNVGISygHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSST 209
Cdd:PRK12935  85 VDILVNNAGIT--RDRTFKKLNRED---WERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAA 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 24640442  210 KAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK12935 160 KAGMLGFTKSLALELAKTNVTVNAICPGFIDTEM 193
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 57-243 3.39e-17

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: 79.03  E-value: 3.39e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  57 VTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVeVRVIDV-DFTGGDEIYDKIREKTTGlNVGVLVN 135
Cdd:cd08931   5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAENVV-AGALDVtDRAAWAAALADFAAATGG-RLDALFN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 136 NVGISYGHPeyFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFVNK 215
Cdd:cd08931  83 NAGVGRGGP--FEDVPLAA---HDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRG 157

                       170       180
                ....*....|....*....|....*...
gi 24640442 216 FSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd08931 158 LTEALDVEWARHGIRVADVWPWFVDTPI 185
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 56-245 4.36e-17

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 79.23  E-value: 4.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEI---YDKIREKTTGLNvgV 132
Cdd:PRK08217   9 VITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGAL-GTEVRGYAANVTDEEDVeatFAQIAEDFGQLN--G 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  133 LVNNVGIsyghpeyfldcykadppfLRN--IVAANIHSVTH--------------MTALFLPG------MI-SQRRGVII 189
Cdd:PRK08217  86 LINNAGI------------------LRDglLVKAKDGKVTSkmsleqfqsvidvnLTGVFLCGreaaakMIeSGSKGVII 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 24640442  190 NVSST--AGvipNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:PRK08217 148 NISSIarAG---NMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTA 202
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 52-243 5.45e-17

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: 78.86  E-value: 5.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVL-ISRSLEKLNVVAKEIGDKYGvevRVIDV-----DFTGGDEIYDKIREKT 125
Cdd:cd05362   3 GKVALVTGASRGIGRAIAKRLARDGASVVVnYASSKAAAEEVVAEIEAAGG---KAIAVqadvsDPSQVARLFDAAEKAF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 126 TGLNVgvLVNNVGISYGHPEYfldcyKADPPFLRNIVAANIHSVTHMTALFLPGMisQRRGVIINVSSTAGVIPNPLLSV 205
Cdd:cd05362  80 GGVDI--LVNNAGVMLKKPIA-----ETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPNYGA 150

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 24640442 206 YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd05362 151 YAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDM 188
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 52-241 6.05e-17

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 78.95  E-value: 6.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVvAKEIGDKYGVEVR--VIDV-DFTGGDEIYDKIrEKTTGL 128
Cdd:PRK07097  10 GKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDK-GLAAYRELGIEAHgyVCDVtDEDGVQAMVSQI-EKEVGV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  129 nVGVLVNNVGISYGHPeyFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSS 208
Cdd:PRK07097  88 -IDILVNNAGIIKRIP--MLEMSAED---FRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAA 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 24640442  209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK07097 162 AKGGLKMLTKNIASEYGEANIQCNGIGPGYIAT 194
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 52-243 6.98e-17

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: 78.65  E-value: 6.98e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVidvDFTGGDEIYDKIREKTT-GLNV 130
Cdd:cd05326   4 GKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFVHC---DVTVEADVRAAVDTAVArFGRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 131 GVLVNNVGISYGHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTK 210
Cdd:cd05326  81 DIMFNNAGVLGAPCYSILETSLEE---FERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASK 157

                       170       180       190
                ....*....|....*....|....*....|...
gi 24640442 211 AFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd05326 158 HAVLGLTRSAATELGEHGIRVNCVSPYGVATPL 190
PRK07775 PRK07775
SDR family oxidoreductase;
55-261 7.17e-17

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 79.03  E-value: 7.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNvvakEIGDKY---GVEVRVIDVDFTGGDEIYDKIREKTTGL-NV 130
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCE----ELVDKIradGGEAVAFPLDVTDPDSVKSFVAQAEEALgEI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 GVLVNNVGisyghPEYFLDCYKADPP-FLRNIvaaNIHSV--THMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYS 207
Cdd:PRK07775  89 EVLVSGAG-----DTYFGKLHEISTEqFESQV---QIHLVgaNRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 24640442  208 STKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKIRKASVFAPSPETYVR 261
Cdd:PRK07775 161 AAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGMGWSLPAEVIGPMLEDWAK 214
PRK08219 PRK08219
SDR family oxidoreductase;
55-243 1.12e-16

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 77.67  E-value: 1.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGlKLVLISRSLEKLNVVAKEIGDkygveVRVIDVDFTGgdeiYDKIREKTTGLN-VGVL 133
Cdd:PRK08219   6 ALITGASRGIGAAIARELAPTH-TLLLGGRPAERLDELAAELPG-----ATPFPVDLTD----PEAIAAAVEQLGrLDVL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  134 VNNVGISYGHPeyfldCYKADPPFLRNIVAANIHSVTHMTALFLPGMISqRRGVIINVSSTAGVIPNPLLSVYSSTKAFV 213
Cdd:PRK08219  76 VHNAGVADLGP-----VAESTVDEWRATLEVNVVAPAELTRLLLPALRA-AHGHVVFINSGAGLRANPGWGSYAASKFAL 149

                        170       180       190
                 ....*....|....*....|....*....|.
gi 24640442  214 NKFSDDLQTEykEHGIL-IQSVQPGFVATNM 243
Cdd:PRK08219 150 RALADALREE--EPGNVrVTSVHPGRTDTDM 178
PRK07326 PRK07326
SDR family oxidoreductase;
51-242 2.10e-16

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 76.97  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDV-DFTGGDEIYDKIREKTTGLN 129
Cdd:PRK07326   5 KGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNVLGLAADVrDEADVQRAVDAIVAAFGGLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 vgVLVNNVGIsyGHpeyFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMiSQRRGVIINVSSTAGVIPNPLLSVYSST 209
Cdd:PRK07326  85 --VLIANAGV--GH---FAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPAL-KRGGGYIINISSLAGTNFFAGGAAYNAS 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 24640442  210 KAFVNKFSDDLQTEYKEHGILIQSVQPGFVATN 242
Cdd:PRK07326 157 KFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATH 189
PRK07074 PRK07074
SDR family oxidoreductase;
55-241 2.61e-16

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 77.12  E-value: 2.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRvidVDFTGGDEIYDKIREKTTGLN-VGVL 133
Cdd:PRK07074   5 ALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARFVPVA---CDLTDAASLAAALANAAAERGpVDVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  134 VNNVGISYGhpeyfLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAG--VIPNPllsVYSSTKA 211
Cdd:PRK07074  82 VANAGAARA-----ASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGmaALGHP---AYSAAKA 153

                        170       180       190
                 ....*....|....*....|....*....|
gi 24640442  212 FVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK07074 154 GLIHYTKLLAVEYGRFGIRANAVAPGTVKT 183
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 52-241 2.88e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 77.25  E-value: 2.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSleklnvvakeIGDKYGVEVRVIDVDFT---GGDEIYDKIREKTTGL 128
Cdd:PRK06523   9 GKRALVTGGTKGIGAATVARLLEAGARVVTTARS----------RPDDLPEGVEFVAADLTtaeGCAAVARAVLERLGGV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  129 NVgvLVNNVGISYGHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNP-LLSVYS 207
Cdd:PRK06523  79 DI--LVHVLGGSSAPAGGFAALTDEE---WQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPeSTTAYA 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 24640442  208 STKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK06523 154 AAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIET 187
PRK07024 PRK07024
SDR family oxidoreductase;
56-243 3.05e-16

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 76.89  E-value: 3.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDV-----------DFTGGDEIYDkirek 124
Cdd:PRK07024   6 FITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAARVSVYAADVrdadalaaaaaDFIAAHGLPD----- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  125 ttglnvgVLVNNVGISYGhpeyFLDCYKADPPFLRNIVAANihsVTHMTALFLP---GMISQRRGVIINVSSTAGVIPNP 201
Cdd:PRK07024  81 -------VVIANAGISVG----TLTEEREDLAVFREVMDTN---YFGMVATFQPfiaPMRAARRGTLVGIASVAGVRGLP 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 24640442  202 LLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK07024 147 GAGAYSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPM 188
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 52-243 1.76e-15

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: 75.02  E-value: 1.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLI--SRSLEKLNVVAKEIgDKYGVEVRVIDVDFTGGD---EIYDKIREKTT 126
Cdd:cd05355  26 GKKALITGGDSGIGRAVAIAFAREGADVAINylPEEEDDAEETKKLI-EEEGRKCLLIPGDLGDESfcrDLVKEVVKEFG 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 127 GLNVgvLVNNVGisYGHPEYFLDcyKADPPFLRNIVAANIHSVTHMTALFLPGMisQRRGVIINVSSTAGVIPNPLLSVY 206
Cdd:cd05355 105 KLDI--LVNNAA--YQHPQESIE--DITTEQLEKTFRTNIFSMFYLTKAALPHL--KKGSSIINTTSVTAYKGSPHLLDY 176

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24640442 207 SSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd05355 177 AATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPL 213
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 52-243 1.90e-15

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 74.62  E-value: 1.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEI----GDKYGVEVRVIDVDFTggDEIYDKIREKTTG 127
Cdd:PRK12939   7 GKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALeaagGRAHAIAADLADPASV--QRFFDAAAAALGG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  128 LNVgvLVNNVGISYGHpeyflDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYS 207
Cdd:PRK12939  85 LDG--LVNNAGITNSK-----SATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYV 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 24640442  208 STKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK12939 158 ASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEA 193
PRK06172 PRK06172
SDR family oxidoreductase;
52-243 2.05e-15

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 74.40  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSL---EKLNVVAKEIGDkygvEVRVIDVDFTGGDEIyDKIREKTTGL 128
Cdd:PRK06172   7 GKVALVTGGAAGIGRATALAFAREGAKVVVADRDAaggEETVALIREAGG----EALFVACDVTRDAEV-KALVEQTIAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  129 nVGVL---VNNVGISYGHP---EYFLDCYKAdppflrnIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPL 202
Cdd:PRK06172  82 -YGRLdyaFNNAGIEIEQGrlaEGSEAEFDA-------IMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPK 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 24640442  203 LSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK06172 154 MSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDM 194
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
55-252 2.18e-15

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 74.28  E-value: 2.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVL----ISRSLEKLNVVAKEIG-DKYGVEVRVIDVDFTggDEIYDKIREKTTglN 129
Cdd:PRK12938   6 AYVTGGMGGIGTSICQRLHKDGFKVVAgcgpNSPRRVKWLEDQKALGfDFIASEGNVGDWDST--KAAFDKVKAEVG--E 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VGVLVNNVGISygHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSST 209
Cdd:PRK12938  82 IDVLVNNAGIT--RDVVFRKMTRED---WTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 24640442  210 KAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKIRKASVF 252
Cdd:PRK12938 157 KAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVL 199
PRK06139 PRK06139
SDR family oxidoreductase;
56-241 2.22e-15

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 75.53  E-value: 2.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEIYDKIRE-KTTGLNVGVLV 134
Cdd:PRK06139  11 VITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRAL-GAEVLVVPTDVTDADQVKALATQaASFGGRIDVWV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  135 NNVGIsyGHPEYF----LDCYKAdppflrnIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTK 210
Cdd:PRK06139  90 NNVGV--GAVGRFeetpIEAHEQ-------VIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASK 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 24640442  211 AFVNKFSDDLQTEYKEH-GILIQSVQPGFVAT 241
Cdd:PRK06139 161 FGLRGFSEALRGELADHpDIHVCDVYPAFMDT 192
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 52-258 3.13e-15

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 74.11  E-value: 3.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVrVIDVDFTGGDEIYDKIREKTTGL-NV 130
Cdd:PRK06113  11 GKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAF-ACRCDITSEQELSALADFALSKLgKV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 GVLVNNVGisYGHPEYFldcykaDPPFLRNIVA--ANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSS 208
Cdd:PRK06113  90 DILVNNAG--GGGPKPF------DMPMADFRRAyeLNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYAS 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 24640442  209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMskirKASVFAPSPET 258
Cdd:PRK06113 162 SKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDA----LKSVITPEIEQ 207
PRK07069 PRK07069
short chain dehydrogenase; Validated
 55-243 3.35e-15

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 73.98  E-value: 3.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEK-LNVVAKEIGDKYGVEVR---VIDV-DFTGGDEIYDKIREKTTGLN 129
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAgLDAFAAEINAAHGEGVAfaaVQDVtDEAQWQALLAQAADAMGGLS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VgvLVNNVGI-SYGHPEyflDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSS 208
Cdd:PRK07069  82 V--LVNNAGVgSFGAIE---QIELDE---WRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNA 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 24640442  209 TKAFVNKFSDDLQTEYKEHGILIQ--SVQPGFVATNM 243
Cdd:PRK07069 154 SKAAVASLTKSIALDCARRGLDVRcnSIHPTFIRTGI 190
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 52-241 3.49e-15

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: 73.96  E-value: 3.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRS-LEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEI---YDKIREKTTG 127
Cdd:cd05358   3 GKVALVTGASSGIGKAIAIRLATAGANVVVNYRSkEDAAEEVVEEIKAV-GGKAIAVQADVSKEEDVvalFQSAIKEFGT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 128 LNVgvLVNNVGIsyghpeyfldcyKADPPFLrNIVAANIHSV--THMTALFLPG-------MISQRRGVIINVSSTAGVI 198
Cdd:cd05358  82 LDI--LVNNAGL------------QGDASSH-EMTLEDWNKVidVNLTGQFLCAreaikrfRKSKIKGKIINMSSVHEKI 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24640442 199 PNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:cd05358 147 PWPGHVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINT 189
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 57-257 3.50e-15

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 74.30  E-value: 3.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   57 VTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNvvakEIGDKYGVEVRVIDVDFTGGDEIYDKIreKTTGLNVG---VL 133
Cdd:PRK08263   8 ITGASRGFGRAWTEAALERGDRVVATARDTATLA----DLAEKYGDRLLPLALDVTDRAAVFAAV--ETAVEHFGrldIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  134 VNNVGisYGHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFV 213
Cdd:PRK08263  82 VNNAG--YGLFGMIEEVTESE---ARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWAL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 24640442  214 NKFSDDLQTEYKEHGILIQSVQPGFVATNMSKIrKASVFAPSPE 257
Cdd:PRK08263 157 EGMSEALAQEVAEFGIKVTLVEPGGYSTDWAGT-SAKRATPLDA 199
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
52-243 3.67e-15

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 73.91  E-value: 3.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDK-YGVEVRVIDVDFTggDEIYDKIREKTTGLNv 130
Cdd:PRK07067   6 GKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAaIAVSLDVTRQDSI--DRIVAAAVERFGGID- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 gVLVNNVGISYGHPeyFLDCYKADppFLRnIVAANIHSVTHMTALFLPGMISQRRG-VIINVSSTAGVIPNPLLSVYSST 209
Cdd:PRK07067  83 -ILFNNAALFDMAP--ILDISRDS--YDR-LFAVNVKGLFFLMQAVARHMVEQGRGgKIINMASQAGRRGEALVSHYCAT 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 24640442  210 KAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK07067 157 KAAVISYTQSAALALIRHGINVNAIAPGVVDTPM 190
PRK06194 PRK06194
hypothetical protein; Provisional
 52-244 6.32e-15

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 73.51  E-value: 6.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEV--RVIDVDFTGGDEIYDKIREKTTGlN 129
Cdd:PRK06194   6 GKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQ-GAEVlgVRTDVSDAAQVEALADAALERFG-A 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VGVLVNNVGISYGHPeyfldCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQ------RRGVIINVSSTAGVIPNPLL 203
Cdd:PRK06194  84 VHLLFNNAGVGAGGL-----VWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAaekdpaYEGHIVNTASMAGLLAPPAM 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 24640442  204 SVYSSTKAFVNKFSDDLQTEYK-EHGILIQSVQ-PGFVATNMS 244
Cdd:PRK06194 159 GIYNVSKHAVVSLTETLYQDLSlVTDQVGASVLcPYFVPTGIW 201
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 47-241 6.95e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 73.15  E-value: 6.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   47 DLSKMGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIYDKIREKTT 126
Cdd:PRK06125   2 DLHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVDVAVHALDLSSPEAREQLAAEAGD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  127 glnVGVLVNNVGisyGHPEYFLDcyKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVY 206
Cdd:PRK06125  82 ---IDILVNNAG---AIPGGGLD--DVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAGENPDADYICG 153

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 24640442  207 SSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK06125 154 SAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVAT 188
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 52-250 8.07e-15

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: 72.95  E-value: 8.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSlEKLNVVAKEIGDKyGVEVRVIDVD---FTGGDEIYDKIREKTTGL 128
Cdd:cd08937   4 GKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRS-ELVHEVLAEILAA-GDAAHVHTADletYAGAQGVVRAAVERFGRV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 129 NVgvLVNNVGISYGHPeyFLDCYKADPpflrniVAANIHSvTHMTAL-----FLPGMISQRRGVIINVSSTA--GVIPNP 201
Cdd:cd08937  82 DV--LINNVGGTIWAK--PYEHYEEEQ------IEAEIRR-SLFPTLwccraVLPHMLERQQGVIVNVSSIAtrGIYRIP 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 24640442 202 llsvYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKIRKAS 250
Cdd:cd08937 151 ----YSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPRNA 195
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 55-245 1.95e-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: 71.94  E-value: 1.95e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAkeigdKYGVEVRVIDVDFTGGDEIYDKIRE-KTTGLNVGVL 133
Cdd:cd05371   5 AVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVA-----KLGDNCRFVPVDVTSEKDVKAALALaKAKFGRLDIV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 134 VNNVGISYGHPEYFLDCYKADPPFL-RNIVAANIHSVTHMTALFLPGMISQ------RRGVIINVSSTAGVIPNPLLSVY 206
Cdd:cd05371  80 VNCAGIAVAAKTYNKKGQQPHSLELfQRVINVNLIGTFNVIRLAAGAMGKNepdqggERGVIINTASVAAFEGQIGQAAY 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24640442 207 SSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:cd05371 160 SASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLA 198
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 51-246 2.81e-14

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: 71.21  E-value: 2.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIyDKIREKTTGLN- 129
Cdd:cd08930   1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVIALELDITSKESI-KELIESYLEKFg 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 130 -VGVLVNNVGISYghPEYFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVI---------P 199
Cdd:cd08930  80 rIDILINNAYPSP--KVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIapdfriyenT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 24640442 200 NPLLSV-YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKI 246
Cdd:cd08930 158 QMYSPVeYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNNQPSE 205
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 56-239 3.25e-14

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 71.14  E-value: 3.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEI---YDKIREKTTGlnVGV 132
Cdd:PRK07890   9 VVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDL-GRRALAVPTDITDEDQCanlVALALERFGR--VDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  133 LVNNvgiSYGHPeYFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMiSQRRGVIINVSSTAGVIPNPLLSVYSSTKAF 212
Cdd:PRK07890  86 LVNN---AFRVP-SMKPLADADFAHWRAVIELNVLGTLRLTQAFTPAL-AESGGSIVMINSMVLRHSQPKYGAYKMAKGA 160

                        170       180
                 ....*....|....*....|....*..
gi 24640442  213 VNKFSDDLQTEYKEHGILIQSVQPGFV 239
Cdd:PRK07890 161 LLAASQSLATELGPQGIRVNSVAPGYI 187
PRK08589 PRK08589
SDR family oxidoreductase;
55-241 3.75e-14

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 71.35  E-value: 3.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKlVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEI---YDKIREKTTglNVG 131
Cdd:PRK08589   9 AVITGASTGIGQASAIALAQEGAY-VLAVDIAEAVSETVDKIKSN-GGKAKAYHVDISDEQQVkdfASEIKEQFG--RVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  132 VLVNNVGISYG----HpEYFLDCYKadppflrNIVAANIHSVTHMTALFLPGMISQrRGVIINVSSTAGVIPNPLLSVYS 207
Cdd:PRK08589  85 VLFNNAGVDNAagriH-EYPVDVFD-------KIMAVDMRGTFLMTKMLLPLMMEQ-GGSIINTSSFSGQAADLYRSGYN 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 24640442  208 STKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK08589 156 AAKGAVINFTKSIAIEYGRDGIRANAIAPGTIET 189
PRK05867 PRK05867
SDR family oxidoreductase;
47-243 3.84e-14

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 70.83  E-value: 3.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   47 DLSkmGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGdKYGVEVRVIDVDFTGGDEIYDKIREKTT 126
Cdd:PRK05867   6 DLH--GKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIG-TSGGKVVPVCCDVSQHQQVTSMLDQVTA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  127 GL-NVGVLVNNVGISYGHPeyFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQ-RRGVIINVSSTAGVIPN--PL 202
Cdd:PRK05867  83 ELgGIDIAVCNAGIITVTP--MLDMPLEE---FQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTASMSGHIINvpQQ 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 24640442  203 LSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK05867 158 VSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTEL 198
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 55-259 7.25e-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: 70.18  E-value: 7.25e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRS-LEKLNVVAKEIgDKYGVEVRVIDVDF---TGGDEIYDKIREKTTGLNv 130
Cdd:cd05337   4 AIVTGASRGIGRAIATELAARGFDIAINDLPdDDQATEVVAEV-LAAGRRAIYFQADIgelSDHEALLDQAWEDFGRLD- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 131 gVLVNNVGISyghPEYFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRR------GVIINVSSTAGVIPNPLLS 204
Cdd:cd05337  82 -CLVNNAGIA---VRPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDrfdgphRSIIFVTSINAYLVSPNRG 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24640442 205 VYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSkirkasvfAPSPETY 259
Cdd:cd05337 158 EYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMT--------APVKEKY 204
PRK06138 PRK06138
SDR family oxidoreductase;
52-274 9.16e-14

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 69.80  E-value: 9.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDE-IYDKIREKTTGLNv 130
Cdd:PRK06138   5 GRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAGGRAFARQGDVGSAEAVEaLVDFVAARWGRLD- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 gVLVNNVGISYGHpeyflDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTK 210
Cdd:PRK06138  84 -VLVNNAGFGCGG-----TVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASK 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24640442  211 AFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMskIRKASVFAPSPETY-----VRSALSTLGIATQTA 274
Cdd:PRK06138 158 GAIASLTRAMALDHATDGIRVNAVAPGTIDTPY--FRRIFARHADPEALrealrARHPMNRFGTAEEVA 224
PRK06484 PRK06484
short chain dehydrogenase; Validated
 48-241 1.14e-13

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 71.42  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   48 LSKMGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYgVEVRVIDVDFTGGDEIYDKIREKTTG 127
Cdd:PRK06484 265 LAESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEH-LSVQADITDEAAVESAFAQIQARWGR 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  128 LNVgvLVNNVGISyghpEYFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQrrGVIINVSSTAGVIPNPLLSVYS 207
Cdd:PRK06484 344 LDV--LVNNAGIA----EVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG--GVIVNLGSIASLLALPPRNAYC 415

                        170       180       190
                 ....*....|....*....|....*....|....
gi 24640442  208 STKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK06484 416 ASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 52-261 2.01e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 68.99  E-value: 2.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGdkyGVEVRVIDVDFTGGDEIYDKIREkTTGlNVG 131
Cdd:PRK06057   7 GRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVG---GLFVPTDVTDEDAVNALFDTAAE-TYG-SVD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  132 VLVNNVGISYGHPEYFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSV-YSSTK 210
Cdd:PRK06057  82 IAFNNAGISPPEDDSILN---TGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSQIsYTASK 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24640442  211 AFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKirkaSVFAPSPETYVR 261
Cdd:PRK06057 159 GGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQ----ELFAKDPERAAR 205
PRK07577 PRK07577
SDR family oxidoreductase;
55-243 2.04e-13

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 68.60  E-value: 2.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSleklnvvakEIGDKYG--VEVRVIDVDFTggDEIYDKIREKTTglnVGV 132
Cdd:PRK07577   6 VLVTGATKGIGLALSLRLANLGHQVIGIARS---------AIDDFPGelFACDLADIEQT--AATLAQINEIHP---VDA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  133 LVNNVGISYGHPeyfldCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAgVIPNPLLSVYSSTKAF 212
Cdd:PRK07577  72 IVNNVGIALPQP-----LGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRA-IFGALDRTSYSAAKSA 145

                        170       180       190
                 ....*....|....*....|....*....|.
gi 24640442  213 VNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK07577 146 LVGCTRTWALELAEYGITVNAVAPGPIETEL 176
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
53-250 2.24e-13

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 68.56  E-value: 2.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   53 EWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEK-LNVVAKEIGDKYG-VEVRVIDVDFTGGD--EIYDKIREKttgl 128
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKeLTKLAEQYNSNLTfHSLDLQDVHELETNfnEILSSIQED---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  129 NVG--VLVNNVG-------ISYGHPEYFLDCYKAdppflrNIVAANI--HSVTHMTALFlpgmisQRRGVIINVSSTAGV 197
Cdd:PRK06924  78 NVSsiHLINNAGmvapikpIEKAESEELITNVHL------NLLAPMIltSTFMKHTKDW------KVDKRVINISSGAAK 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 24640442  198 IPNPLLSVYSSTKAFVNKFSD--DLQTEYKEHGILIQSVQPGFVATNM-SKIRKAS 250
Cdd:PRK06924 146 NPYFGWSAYCSSKAGLDMFTQtvATEQEEEEYPVKIVAFSPGVMDTNMqAQIRSSS 201
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 55-256 2.25e-13

(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: 68.50  E-value: 2.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVL---------ISRSLEKLNVVAKEIGDKYGVEVRVIDvDFTGGDEIYDKIREKT 125
Cdd:cd05353   8 VLVTGAGGGLGRAYALAFAERGAKVVVndlggdrkgSGKSSSAADKVVDEIKAAGGKAVANYD-SVEDGEKIVKTAIDAF 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 126 TGlnVGVLVNNVGIsyghpeyfldcykadppfLRNIVAAN--------IHSVtHMTALFL------PGMISQRRGVIINV 191
Cdd:cd05353  87 GR--VDILVNNAGI------------------LRDRSFAKmseedwdlVMRV-HLKGSFKvtraawPYMRKQKFGRIINT 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24640442 192 SSTAGVIPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGfVATNMSKirkaSVFAPSP 256
Cdd:cd05353 146 SSAAGLYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA-AGSRMTE----TVMPEDL 205
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 52-243 2.30e-13

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 68.67  E-value: 2.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKL-NVVAKEIGDkyGVEVRVIDV-DFTGGDEIYDKIREKTTGLN 129
Cdd:PRK12828   7 GKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLsQTLPGVPAD--ALRIGGIDLvDPQAARRAVDEVNRQFGRLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VgvLVNNVGI-SYGHPEyfldcyKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSS 208
Cdd:PRK12828  85 A--LVNIAGAfVWGTIA------DGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAA 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 24640442  209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK12828 157 AKAGVARLTEALAAELLDRGITVNAVLPSIIDTPP 191
PRK06398 PRK06398
aldose dehydrogenase; Validated
 55-210 2.52e-13

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 68.71  E-value: 2.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSleklnvvakeigDKYGVEVRVIDVDFTGGDEIYDKIREKTTGL-NVGVL 133
Cdd:PRK06398   9 AIVTGGSQGIGKAVVNRLKEEGSNVINFDIK------------EPSYNDVDYFKVDVSNKEQVIKGIDYVISKYgRIDIL 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24640442  134 VNNVGI-SYGHPEyfldcyKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTK 210
Cdd:PRK06398  77 VNNAGIeSYGAIH------AVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSK 148
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 55-259 3.63e-13

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 67.88  E-value: 3.63e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLnvvakeigDKYGVEVRVIDVDFTGG---DEIYDKIREKTTGLNVg 131
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLL--------LEYGDPLRLTPLDVADAaavREVCSRLLAEHGPIDA- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 132 vLVNNVGISygHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKA 211
Cdd:cd05331  72 -LVNCAGVL--RPGATDPLSTED---WEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKA 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 24640442 212 FVNKFSDDLQTEYKEHGILIQSVQPGFVATNM------SKIRKASVFAPSPETY 259
Cdd:cd05331 146 ALASLSKCLGLELAPYGVRCNVVSPGSTDTAMqrtlwhDEDGAAQVIAGVPEQF 199
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 55-251 4.44e-13

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: 68.02  E-value: 4.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442    55 AVVTGSTDGIGKAYAKELARR----GLKLVLISRSLEKLNVVAKEIGDKYG---VEVRVIDVDFTGGDEIYDKIRE---K 124
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAERSglrVVRVSLDLGAEAGLEQLLKALRelpR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   125 TTGLNVGVLVNNVGISYGHPEYFLDCykADPPFLRNIVAANIHSVTHMTALFL---PGMISQRRgVIINVSSTAGVIPNP 201
Cdd:TIGR01500  83 PKGLQRLLLINNAGTLGDVSKGFVDL--SDSTQVQNYWALNLTSMLCLTSSVLkafKDSPGLNR-TVVNISSLCAIQPFK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 24640442   202 LLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM-SKIRKASV 251
Cdd:TIGR01500 160 GWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMqQQVREESV 210
PRK07023 PRK07023
SDR family oxidoreductase;
55-250 4.64e-13

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 67.73  E-value: 4.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEklnvvaKEIGDKYGVEVRVIDVD---------FTGGDEIYDKIREKT 125
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPGIAVLGVARSRH------PSLAAAAGERLAEVELDlsdaaaaaaWLAGDLLAAFVDGAS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  126 TGLnvgvLVNNVGISygHPEYFLDCYkaDPPFLRNIVAANIHSVTHMTALFLPGMI--SQRRgvIINVSSTAGVIPNPLL 203
Cdd:PRK07023  78 RVL----LINNAGTV--EPIGPLATL--DAAAIARAVGLNVAAPLMLTAALAQAASdaAERR--ILHISSGAARNAYAGW 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 24640442  204 SVYSSTKAFVNKFSDDLQTEyKEHGILIQSVQPGFVATNM-SKIRKAS 250
Cdd:PRK07023 148 SVYCATKAALDHHARAVALD-ANRALRIVSLAPGVVDTGMqATIRATD 194
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 55-245 4.83e-13

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 67.86  E-value: 4.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEIYDKIR--EKTTGlNVGV 132
Cdd:PRK08085  12 ILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQE-GIKAHAAPFNVTHKQEVEAAIEhiEKDIG-PIDV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  133 LVNNVGISYGHPeyFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAF 212
Cdd:PRK08085  90 LINNAGIQRRHP--FTEFPEQE---WNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAASKGA 164

                        170       180       190
                 ....*....|....*....|....*....|...
gi 24640442  213 VNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:PRK08085 165 VKMLTRGMCVELARHNIQVNGIAPGYFKTEMTK 197
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 52-243 5.40e-13

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: 67.64  E-value: 5.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIG-DKYGVEVRVIDVDFTggDEIYDKIREKTTGLNV 130
Cdd:cd05363   3 GKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGpAACAISLDVTDQASI--DRCVAALVDRWGSIDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 131 gvLVNNVGISYGHP--EYFLDCYKadppflrNIVAANIHSVTHMTALFLPGMISQRRG-VIINVSSTAGVIPNPLLSVYS 207
Cdd:cd05363  81 --LVNNAALFDLAPivDITRESYD-------RLFAINVSGTLFMMQAVARAMIAQGRGgKIINMASQAGRRGEALVGVYC 151

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24640442 208 STKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd05363 152 ATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEH 187
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
52-247 6.40e-13

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 67.45  E-value: 6.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVvaKEIGDKYGVEVRVIDVDFTGGDEIYDKIRE--KTTGlN 129
Cdd:PRK06935  15 GKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDET--RRLIEKEGRKVTFVQVDLTKPESAEKVVKEalEEFG-K 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VGVLVNNVGISYGHPeyFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSS----TAGV-IPNPLLS 204
Cdd:PRK06935  92 IDILVNNAGTIRRAP--LLEYKDED---WNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASmlsfQGGKfVPAYTAS 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 24640442  205 ---VYSSTKAFVNkfsddlqtEYKEHGILIQSVQPGFVAT-NMSKIR 247
Cdd:PRK06935 167 khgVAGLTKAFAN--------ELAAYNIQVNAIAPGYIKTaNTAPIR 205
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-243 1.37e-12

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 67.94  E-value: 1.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   23 QVFRkvlpwiyanvVGPKVFGSSVDLSK--MGEWAVVTGSTDGIGKAYAKELARRGLKLVL--ISRSLEKLNVVAKEIGd 98
Cdd:PRK08261 189 QVVR----------VGAADAAPPADWDRplAGKVALVTGAARGIGAAIAEVLARDGAHVVCldVPAAGEALAAVANRVG- 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   99 kyGVEVrVIDV-DFTGGDEIYDKIREKTTGLNvgVLVNNVGISYghpeyflDCYKA--DPPFLRNIVAANIHSVTHMTAL 175
Cdd:PRK08261 258 --GTAL-ALDItAPDAPARIAEHLAERHGGLD--IVVHNAGITR-------DKTLAnmDEARWDSVLAVNLLAPLRITEA 325

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24640442  176 FLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK08261 326 LLAAGALGDGGRIVGVSSISGIAGNRGQTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQM 393
PRK06114 PRK06114
SDR family oxidoreductase;
52-245 1.47e-12

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 66.34  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLIS-RSLEKLNVVAKEIgDKYGVEVRVIDVDFTGGDEIYDKIREKTTGLN- 129
Cdd:PRK06114   8 GQVAFVTGAGSGIGQRIAIGLAQAGADVALFDlRTDDGLAETAEHI-EAAGRRAIQIAADVTSKADLRAAVARTEAELGa 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VGVLVNNVGISYGHP--EYFLDCYKadppflrnivaaNIHSVtHMTALFLP------GMISQRRGVIINVSSTAGVIPNP 201
Cdd:PRK06114  87 LTLAVNAAGIANANPaeEMEEEQWQ------------TVMDI-NLTGVFLScqaearAMLENGGGSIVNIASMSGIIVNR 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 24640442  202 LL--SVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:PRK06114 154 GLlqAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNT 199
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 55-257 1.49e-12

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: 65.99  E-value: 1.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDkyGVEVRVIDV-DFTGGDEIYDKIREKTTGLNvgVL 133
Cdd:cd08929   3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELE--GVLGLAGDVrDEADVRRAVDAMEEAFGGLD--AL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 134 VNNVGIsyGHpeyFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFV 213
Cdd:cd08929  79 VNNAGV--GV---MKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGL 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 24640442 214 NKFSDDLQTEYKEHGILIQSVQPGFVATNmskirkasvFAPSPE 257
Cdd:cd08929 154 LGLSEAAMLDLREANIRVVNVMPGSVDTG---------FAGSPE 188
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 55-243 1.59e-12

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 66.14  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLIS-RSLEKLNVVAKEIGDKyGVEVRVI--DV-DFTGGDEIYDKIREKTTGLNv 130
Cdd:PRK12745   5 ALVTGGRRGIGLGIARALAAAGFDLAINDrPDDEELAATQQELRAL-GVEVIFFpaDVaDLSAHEAMLDAAQAAWGRID- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 gVLVNNVGISYGHPEYFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRR------GVIINVSSTAGVIPNPLLS 204
Cdd:PRK12745  83 -CLVNNAGVGVKVRGDLLD---LTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVSSVNAIMVSPNRG 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 24640442  205 VYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK12745 159 EYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDM 197
PRK06124 PRK06124
SDR family oxidoreductase;
52-241 1.64e-12

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 66.27  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKL-NVVAKEIGDKYGVEVRVIDV-DFTGGDEIYDKIREKTTGLN 129
Cdd:PRK06124  11 GQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLeAAVAALRAAGGAAEALAFDIaDEEAVAAAFARIDAEHGRLD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 vgVLVNNVGISYGHPeyFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSST 209
Cdd:PRK06124  91 --ILVNNVGARDRRP--LAE---LDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAA 163

                        170       180       190
                 ....*....|....*....|....*....|..
gi 24640442  210 KAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK06124 164 KQGLTGLMRALAAEFGPHGITSNAIAPGYFAT 195
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 51-254 1.78e-12

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 65.75  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKlvlisrsleklnVVAKEIGDKYGVE--VRVIDVDFTGG-DEIYDKIRekttg 127
Cdd:PRK06550   4 MTKTVLITGAASGIGLAQARAFLAQGAQ------------VYGVDKQDKPDLSgnFHFLQLDLSDDlEPLFDWVP----- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  128 lNVGVLVNNVGIsyghpeyfLDCYKadpPFL-------RNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPN 200
Cdd:PRK06550  67 -SVDILCNTAGI--------LDDYK---PLLdtsleewQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAG 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 24640442  201 PLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSkirkASVFAP 254
Cdd:PRK06550 135 GGGAAYTASKHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMT----AADFEP 184
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 47-245 1.89e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 66.22  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   47 DLSkmGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDkygvEVRVIDVDFTGGDEIYDKIREKTT 126
Cdd:PRK06841  12 DLS--GKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGG----NAKGLVCDVSDSQSVEAAVAAVIS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  127 GL-NVGVLVNNVGISYGHP--EYFLDCYKAdppflrnIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLL 203
Cdd:PRK06841  86 AFgRIDILVNSAGVALLAPaeDVSEEDWDK-------TIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERH 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 24640442  204 SVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:PRK06841 159 VAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGK 200
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 52-267 3.35e-12

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: 65.11  E-value: 3.35e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLE--------KLNVVAKEIGDKY---GVEVRVIDVDFTGGDEI--- 117
Cdd:cd05338   3 GKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASegdngsakSLPGTIEETAEEIeaaGGQALPIVVDVRDEDQVral 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 118 YDKIREKTTGLNVgvLVNNVGISyghpeyFLDCYKADPP--FLRnIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTA 195
Cdd:cd05338  83 VEATVDQFGRLDI--LVNNAGAI------WLSLVEDTPAkrFDL-MQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPL 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24640442 196 GVIPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFV-----ATNMSKIRKASVfAPSPETYVRSALSTL 267
Cdd:cd05338 154 SLRPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAietpaATELSGGSDPAR-ARSPEILSDAVLAIL 229
PRK08340 PRK08340
SDR family oxidoreductase;
56-234 3.79e-12

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 65.21  E-value: 3.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDkYGvEVRVIDVDFTGGDEIYDKIREKTTGLN-VGVLV 134
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKE-YG-EVYAVKADLSDKDDLKNLVKEAWELLGgIDALV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  135 NNVGISYGHPeyfldCYKADPPFLRNIVAANIHSVT--HMTALFLPGMISQR-RGVIINVSSTAGVIPNPLLSVYSSTKA 211
Cdd:PRK08340  82 WNAGNVRCEP-----CMLHEAGYSDWLEAALLHLVApgYLTTLLIQAWLEKKmKGVLVYLSSVSVKEPMPPLVLADVTRA 156

                        170       180
                 ....*....|....*....|...
gi 24640442  212 FVNKFSDDLQTEYKEHGILIQSV 234
Cdd:PRK08340 157 GLVQLAKGVSRTYGGKGIRAYTV 179
PRK07856 PRK07856
SDR family oxidoreductase;
45-244 5.37e-12

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 64.57  E-value: 5.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   45 SVDLSkmGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSleklnvvAKEIGDKYGVEVRVIDV-DFTGGDEIYDKIRE 123
Cdd:PRK07856   1 NLDLT--GRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRR-------APETVDGRPAEFHAADVrDPDQVAALVDAIVE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  124 KTTGLNvgVLVNNVGisyGHPeyFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQ-RRGVIINVSSTAGVIPNPL 202
Cdd:PRK07856  72 RHGRLD--VLVNNAG---GSP--YALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQpGGGSIVNIGSVSGRRPSPG 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 24640442  203 LSVYSSTKAFVNKFSDDLQTEYKEHgILIQSVQPGFVATNMS 244
Cdd:PRK07856 145 TAAYGAAKAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQS 185
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 52-246 6.49e-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: 6.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLN-VVAKEIGDKYGVEVRVIDVdftGGDEIYDKIREKTTGLNV 130
Cdd:cd08936  10 NKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDrAVATLQGEGLSVTGTVCHV---GKAEDRERLVATAVNLHG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 131 GV--LVNNVGISyghpEYFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSS 208
Cdd:cd08936  87 GVdiLVSNAAVN----PFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNV 162

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 24640442 209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKI 246
Cdd:cd08936 163 SKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSA 200
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
52-236 8.21e-12

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 66.02  E-value: 8.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDftggDEiyDKIRE--KTTGLN 129
Cdd:PRK08324 422 GKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPDRALGVACDVT----DE--AAVQAafEEAALA 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VG---VLVNNVGISygHPEYFLDCYKADppfLRNIVAANIhsvthmTALFL------PGMISQ-RRGVIINVSSTAGVIP 199
Cdd:PRK08324 496 FGgvdIVVSNAGIA--ISGPIEETSDED---WRRSFDVNA------TGHFLvareavRIMKAQgLGGSIVFIASKNAVNP 564

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 24640442  200 NPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQP 236
Cdd:PRK08324 565 GPNFGAYGAAKAAELHLVRQLALELGPDGIRVNGVNP 601
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 52-237 9.28e-12

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 64.04  E-value: 9.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGST--DGIGKAYAKELARRGLKLVLI-----SRSLEKLN------VVAKEIgDKYGVEVRVIDVDFT---GGD 115
Cdd:PRK12859   6 NKVAVVTGVSrlDGIGAAICKELAEAGADIFFTywtayDKEMPWGVdqdeqiQLQEEL-LKNGVKVSSMELDLTqndAPK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  116 EIYDKIREKttglnVG---VLVNNVgisyghpeyfldCYKADPPFlRNIVAA--------NIHSVTHMTALFLPGMISQR 184
Cdd:PRK12859  85 ELLNKVTEQ-----LGyphILVNNA------------AYSTNNDF-SNLTAEeldkhymvNVRATTLLSSQFARGFDKKS 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24640442  185 RGVIINVSSTAGVIPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPG 237
Cdd:PRK12859 147 GGRIINMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPG 199
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 56-243 1.10e-11

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: 63.75  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDF-TGGDEIYDKIREKTT---GLNVG 131
Cdd:cd05340   8 LVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFILDLlTCTSENCQQLAQRIAvnyPRLDG 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 132 VLvNNVGISYGH-PEYFLdcykaDPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTK 210
Cdd:cd05340  88 VL-HNAGLLGDVcPLSEQ-----NPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSK 161

                       170       180       190
                ....*....|....*....|....*....|...
gi 24640442 211 AFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd05340 162 FATEGL*QVLADEYQQRNLRVNCINPGGTRTAM 194
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 52-280 2.02e-11

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 63.44  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVL-------ISRSLEKLNvvaKEIGDKYGV--EVRVIDVDFTGGDEIYdkir 122
Cdd:PRK05876   6 GRGAVITGGASGIGLATGTEFARRGARVVLgdvdkpgLRQAVNHLR---AEGFDVHGVmcDVRHREEVTHLADEAF---- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  123 eKTTGlNVGVLVNNVGISYGHPeyFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRR-GVIINVSSTAGVIPNP 201
Cdd:PRK05876  79 -RLLG-HVDVVFSNAGIVVGGP--IVEMTHDD---WRWVIDVDLWGSIHTVEAFLPRLLEQGTgGHVVFTASFAGLVPNA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  202 LLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM----SKIRKA------SVFAPSPETYVRSALSTLGIAT 271
Cdd:PRK05876 152 GLGAYGVAKYGVVGLAETLAREVTADGIGVSVLCPMVVETNLvansERIRGAacaqssTTGSPGPLPLQDDNLGVDDIAQ 231

                        250
                 ....*....|....*..
gi 24640442  272 QTAG--------YLPHA 280
Cdd:PRK05876 232 LTADailanrlyVLPHA 248
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 52-244 2.03e-11

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 63.17  E-value: 2.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGlKLVLI------SRSLEKLNVVAKEIGDKYGVEVRVIDVDftGGDEIYD----KI 121
Cdd:PRK12747   4 GKVALVTGASRGIGRAIAKRLANDG-ALVAIhygnrkEEAEETVYEIQSNGGSAFSIGANLESLH--GVEALYSsldnEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  122 REKTTGLNVGVLVNNVGISyghPEYFLDcyKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRgvIINVSSTAGVIPNP 201
Cdd:PRK12747  81 QNRTGSTKFDILINNAGIG---PGAFIE--ETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNSR--IINISSAATRISLP 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 24640442  202 LLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMS 244
Cdd:PRK12747 154 DFIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMN 196
PRK07814 PRK07814
SDR family oxidoreductase;
52-211 2.40e-11

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 62.87  E-value: 2.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGD---EIYDKIREKTTGL 128
Cdd:PRK07814  10 DQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAA-GRRAHVVAADLAHPEataGLAGQAVEAFGRL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  129 NvgVLVNNVGISYghPEYFLDcykADPPFLRNIVAANIHSVTHMTALFLPGMISQR-RGVIINVSSTAGVIPNPLLSVYS 207
Cdd:PRK07814  89 D--IVVNNVGGTM--PNPLLS---TSTKDLADAFTFNVATAHALTVAAVPLMLEHSgGGSVINISSTMGRLAGRGFAAYG 161


                 ....
gi 24640442  208 STKA 211
Cdd:PRK07814 162 TAKA 165
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 52-236 2.97e-11

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: 62.41  E-value: 2.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGdkYGVEVRVIDVDFTGGDEIYDKIreKTTGLNVG 131
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQ--GGPRALGVQCDVTSEAQVQSAF--EQAVLEFG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 132 ---VLVNNVGISYGHPeyFLDCYKADppFLRNIvaaNIHSVTHMTAL--FLPGMISQRR-GVIINVSSTAGVIPNPLLSV 205
Cdd:cd08943  77 gldIVVSNAGIATSSP--IAETSLED--WNRSM---DINLTGHFLVSreAFRIMKSQGIgGNIVFNASKNAVAPGPNAAA 149

                       170       180       190
                ....*....|....*....|....*....|.
gi 24640442 206 YSSTKAFVNKFSDDLQTEYKEHGILIQSVQP 236
Cdd:cd08943 150 YSAAKAAEAHLARCLALEGGEDGIRVNTVNP 180
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 49-243 3.47e-11

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 62.43  E-value: 3.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   49 SKMGEWAVVTGSTDGIGKAYAKELARRGLKLVLIS----RSLEKLNVVAKEIGDKYG-VEVRVIDV-DFTGGDEIYDKIR 122
Cdd:PRK12827   3 SLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDihpmRGRAEADAVAAGIEAAGGkALGLAFDVrDFAATRAALDAGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  123 EKTTGLNVgvLVNNVGISygHPEYFLDCYKADppfLRNIVAANIHSVTHMT-ALFLPGMISQRRGVIINVSSTAGVIPNP 201
Cdd:PRK12827  83 EEFGRLDI--LVNNAGIA--TDAAFAELSIEE---WDDVIDVNLDGFFNVTqAALPPMIRARRGGRIVNIASVAGVRGNR 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 24640442  202 LLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK12827 156 GQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPM 197
PRK07102 PRK07102
SDR family oxidoreductase;
57-243 4.49e-11

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 61.86  E-value: 4.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   57 VTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRV--IDV-DFTGGDEIYDKIREK--TTGLNVG 131
Cdd:PRK07102   6 IIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAVAVSTheLDIlDTASHAAFLDSLPALpdIVLIAVG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  132 VLVNNVgisyghpeyflDCyKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKA 211
Cdd:PRK07102  86 TLGDQA-----------AC-EADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKA 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 24640442  212 FVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK07102 154 ALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPM 185
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 52-241 4.77e-11

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 62.05  E-value: 4.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEK-LNVVAKEIgDKYGVEVRVIDVDFTGGDEIYDKIR--EKTTGl 128
Cdd:PRK08936   7 GKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEeANDVAEEI-KKAGGEAIAVKGDVTVESDVVNLIQtaVKEFG- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  129 NVGVLVNNVGISYGHP--EYFLDCYkadppflrNIVAAnihsvTHMTALFLPGMISQR-------RGVIINVSSTAGVIP 199
Cdd:PRK08936  85 TLDVMINNAGIENAVPshEMSLEDW--------NKVIN-----TNLTGAFLGSREAIKyfvehdiKGNIINMSSVHEQIP 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 24640442  200 NPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK08936 152 WPLFVHYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINT 193
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 55-243 5.16e-11

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 61.68  E-value: 5.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVL-ISRSLEKLNVVAKEIGDKYGVEVRV-IDV-DFTGGDEIYDKIREKTTGLNVg 131
Cdd:PRK12937   8 AIVTGASRGIGAAIARRLAADGFAVAVnYAGSAAAADELVAEIEAAGGRAIAVqADVaDAAAVTRLFDAAETAFGRIDV- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  132 vLVNNVGIsyghpeyfLDCYKADP----PFLRnIVAANIHSVTHMTALFLPGMisQRRGVIINVSSTAGVIPNPLLSVYS 207
Cdd:PRK12937  87 -LVNNAGV--------MPLGTIADfdleDFDR-TIATNLRGAFVVLREAARHL--GQGGRIINLSTSVIALPLPGYGPYA 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 24640442  208 STKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK12937 155 ASKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 55-252 5.92e-11

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: 61.70  E-value: 5.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVL-ISRSLEKLNVVAKEIGDKygveVRVIDVDFTGGDEIYDKIREKTTGLN-VGV 132
Cdd:cd05349   3 VLVTGASRGLGAAIARSFAREGARVVVnYYRSTESAEAVAAEAGER----AIAIQADVRDRDQVQAMIEEAKNHFGpVDT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 133 LVNNVGISYghPEYFLDCYKADP----PFLRNIVAAnIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSS 208
Cdd:cd05349  79 IVNNALIDF--PFDPDQRKTFDTidweDYQQQLEGA-VKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTT 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 24640442 209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFV-ATNMSKIRKASVF 252
Cdd:cd05349 156 AKAALLGFTRNMAKELGPYGITVNMVSGGLLkVTDASAATPKEVF 200
PRK09730 PRK09730
SDR family oxidoreductase;
55-243 7.43e-11

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 61.40  E-value: 7.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKL-VLISRSLEKLNVVAKEIgDKYGVEVRVIDVDFTGGDEI---YDKIREKTTGLnv 130
Cdd:PRK09730   4 ALVTGGSRGIGRATALLLAQEGYTVaVNYQQNLHAAQEVVNLI-TQAGGKAFVLQADISDENQVvamFTAIDQHDEPL-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 GVLVNNVGIsyghpeYFLDCYkadppfLRNIVAANIHSV--THMTALFLPGMISQRR---------GVIINVSSTAGVIP 199
Cdd:PRK09730  81 AALVNNAGI------LFTQCT------VENLTAERINRVlsTNVTGYFLCCREAVKRmalkhggsgGAIVNVSSAASRLG 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 24640442  200 NPLLSV-YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK09730 149 APGEYVdYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEM 193
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 52-243 7.93e-11

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: 61.34  E-value: 7.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGdKYGvEVRVIDVDFT---GGDEIYDKIREKTTGL 128
Cdd:cd08942   6 GKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELS-AYG-ECIAIPADLSseeGIEALVARVAERSDRL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 129 NvgVLVNNVGISYGHPeyfLDCYKADPpfLRNIVAANIHSVTHMTALFLPGMisqRRGV-------IINVSSTAGVIPNP 201
Cdd:cd08942  84 D--VLVNNAGATWGAP---LEAFPESG--WDKVMDINVKSVFFLTQALLPLL---RAAAtaenparVINIGSIAGIVVSG 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24640442 202 LLS-VYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd08942 154 LENySYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKM 196
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 52-269 8.59e-11

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 61.05  E-value: 8.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLnvvakeigDKYGVEVRVIDV-DFTGGDEIYDKIrEKTTGLnV 130
Cdd:PRK08220   8 GKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQ--------EDYPFATFVLDVsDAAAVAQVCQRL-LAETGP-L 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 GVLVNNVGI-SYGH-----PEYFLDCYkadppflrnivAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLS 204
Cdd:PRK08220  78 DVLVNAAGIlRMGAtdslsDEDWQQTF-----------AVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMA 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640442  205 VYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM------SKIRKASVFAPSPETYvrsalsTLGI 269
Cdd:PRK08220 147 AYGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMqrtlwvDEDGEQQVIAGFPEQF------KLGI 211
PRK08251 PRK08251
SDR family oxidoreductase;
56-262 9.16e-11

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 61.10  E-value: 9.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKY---GVEVRVIDVdfTGGDEIYDKIREKTTGLnvGV 132
Cdd:PRK08251   6 LITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARYpgiKVAVAALDV--NDHDQVFEVFAEFRDEL--GG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  133 L---VNNVGISYGHP--EYFLDCYKAdpPFLRNIVAANIHSVTHMtALFLpgmiSQRRGVIINVSSTAGVIPNP-LLSVY 206
Cdd:PRK08251  82 LdrvIVNAGIGKGARlgTGKFWANKA--TAETNFVAALAQCEAAM-EIFR----EQGSGHLVLISSVSAVRGLPgVKAAY 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 24640442  207 SSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKIRKASVFAPSPETYVRS 262
Cdd:PRK08251 155 AASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNAKAKSTPFMVDTETGVKA 210
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 56-241 1.13e-10

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 60.94  E-value: 1.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  56 VVTGSTDGIGKAYAKELAR---RGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIyDKIREKTTGLNVGV 132
Cdd:cd09806   4 LITGCSSGIGLHLAVRLASdpsKRFKVYATMRDLKKKGRLWEAAGALAGGTLETLQLDVCDSKSV-AAAVERVTERHVDV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 133 LVNNVGISYGHPeyfLDCYKADPpfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAF 212
Cdd:cd09806  83 LVCNAGVGLLGP---LEALSEDA--MASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFA 157

                       170       180
                ....*....|....*....|....*....
gi 24640442 213 VNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:cd09806 158 LEGLCESLAVQLLPFNVHLSLIECGPVHT 186
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 52-241 1.35e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 61.20  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVI--DVdftgGDEIY-DKIREKTT-- 126
Cdd:PRK06701  46 GKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDANETKQRVEKEGVKCLLIpgDV----SDEAFcKDAVEETVre 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  127 --GLNVgvLVNNVGISYgHPEYFLDCykADPPFLRNIvAANIHSVTHMTALFLPGMisQRRGVIINVSSTAGVIPNPLLS 204
Cdd:PRK06701 122 lgRLDI--LVNNAAFQY-PQQSLEDI--TAEQLDKTF-KTNIYSYFHMTKAALPHL--KQGSAIINTGSITGYEGNETLI 193

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 24640442  205 VYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK06701 194 DYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWT 230
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 45-242 4.76e-10

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 59.10  E-value: 4.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   45 SVDLSkmGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIYDKIREk 124
Cdd:PRK08339   3 KIDLS--GKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSYIVADLTKREDLERTVKE- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  125 ttglnvgvlVNNVG------ISYGHPE--YFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAG 196
Cdd:PRK08339  80 ---------LKNIGepdiffFSTGGPKpgYFMEMSMED---WEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAI 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 24640442  197 VIPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATN 242
Cdd:PRK08339 148 KEPIPNIALSNVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTD 193
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 52-241 6.60e-10

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: 58.75  E-value: 6.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIYDKIRE--KTTGLn 129
Cdd:cd05369   3 GKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDEtlKEFGK- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 130 VGVLVNNVGISYGHPEYFLdcykaDPPFLRNIVAANIHSVTHMTALFLPGMISQRR-GVIINVSSTAGVIPNPLLSVYSS 208
Cdd:cd05369  82 IDILINNAAGNFLAPAESL-----SPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHgGSILNISATYAYTGSPFQVHSAA 156

                       170       180       190
                ....*....|....*....|....*....|...
gi 24640442 209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:cd05369 157 AKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPT 189
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 55-211 6.61e-10

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 59.93  E-value: 6.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVeVRVIDVDFTGGDEIYDKIREKTTGLNVGVLV 134
Cdd:COG3347 428 ALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGA-DAVDATDVDVTAEAAVAAAFGFAGLDIGGSD 506

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 135 NNVGISyghpeyfldCYKADPPFLRNIVAANIHSVTH-MTALFLP---GMISQRRGVIINVSSTAGViPNPLLSVYSSTK 210
Cdd:COG3347 507 IGVANA---------GIASSSPEEETRLSFWLNNFAHlSTGQFLVaraAFQGTGGQGLGGSSVFAVS-KNAAAAAYGAAA 576


                .
gi 24640442 211 A 211
Cdd:COG3347 577 A 577
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 56-243 8.78e-10

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: 58.30  E-value: 8.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  56 VVTGSTDGIGKAYAKELARRGLKLVLI---SRSLEKLNVVAKEIGDKygVEVRVIDVDFTGGDEIYDKIREKTTGL-NVG 131
Cdd:cd05330   7 LITGGGSGLGLATAVRLAKEGAKLSLVdlnEEGLEAAKAALLEIAPD--AEVLLIKADVSDEAQVEAYVDATVEQFgRID 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 132 VLVNNVGISyGHPEYFLDcYKADPpfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKA 211
Cdd:cd05330  85 GFFNNAGIE-GKQNLTED-FGADE--FDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKH 160

                       170       180       190
                ....*....|....*....|....*....|..
gi 24640442 212 FVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd05330 161 GVVGLTRNSAVEYGQYGIRINAIAPGAILTPM 192
PLN02253 PLN02253
xanthoxin dehydrogenase
 51-244 1.14e-09

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 58.30  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGV-----EVRVID-----VDFTGgdeiydk 120
Cdd:PLN02253  17 LGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVcffhcDVTVEDdvsraVDFTV------- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  121 irEKTTGLNvgVLVNNVGISyGHPeyFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPN 200
Cdd:PLN02253  90 --DKFGTLD--IMVNNAGLT-GPP--CPDIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGG 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 24640442  201 PLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMS 244
Cdd:PLN02253 163 LGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALA 206
PRK08017 PRK08017
SDR family oxidoreductase;
51-241 1.42e-09

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 57.79  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISR---SLEKLNVVAKEigdkyGVEvrvIDVDFTGG-DEIYDKIREKTT 126
Cdd:PRK08017   1 MQKSVLITGCSSGIGLEAALELKRRGYRVLAACRkpdDVARMNSLGFT-----GIL---LDLDDPESvERAADEVIALTD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  127 GLNVGvLVNNVGIS-YGhPEYFLDCYKADPPFlrnivAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSV 205
Cdd:PRK08017  73 NRLYG-LFNNAGFGvYG-PLSTISRQQMEQQF-----STNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGA 145

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 24640442  206 YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK08017 146 YAASKYALEAWSDALRMELRHSGIKVSLIEPGPIRT 181
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 56-243 1.55e-09

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: 57.54  E-value: 1.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIYDKIREKTTGL-NVGVLV 134
Cdd:cd08933  13 IVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKFVPCDVTKEEDIKTLISVTVERFgRIDCLV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 135 NNVGisYGHPEYFLDCYKADPpfLRNIVAANIHSVTHMTALFLPgMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFVN 214
Cdd:cd08933  93 NNAG--WHPPHQTTDETSAQE--FRDLLNLNLISYFLASKYALP-HLRKSQGNIINLSSLVGSIGQKQAAPYVATKGAIT 167

                       170       180
                ....*....|....*....|....*....
gi 24640442 215 KFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd08933 168 AMTKALAVDESRYGVRVNCISPGNIWTPL 196
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 55-258 3.48e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 56.48  E-value: 3.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVI-DVdftgGDEIY-----DKIREKTTGL 128
Cdd:PRK07478   9 AIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALAgDV----RDEAYakalvALAVERFGGL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  129 NVGvlVNNVGISyghpeyfldcykADPPFLRNIVAANIHSV--THMTALFL------PGMISQRRGVIINVSS----TAG 196
Cdd:PRK07478  85 DIA--FNNAGTL------------GEMGPVAEMSLEGWRETlaTNLTSAFLgakhqiPAMLARGGGSLIFTSTfvghTAG 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24640442  197 VipnPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMskirkASVFAPSPET 258
Cdd:PRK07478 151 F---PGMAAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPM-----GRAMGDTPEA 204
PRK06482 PRK06482
SDR family oxidoreductase;
57-270 3.67e-09

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 56.66  E-value: 3.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   57 VTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNvvakEIGDKYGVEVRVIDVDFTGGDEIYDKIREKTTGL-NVGVLVN 135
Cdd:PRK06482   7 ITGASSGFGRGMTERLLARGDRVAATVRRPDALD----DLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALgRIDVVVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  136 NVGIS-YGHPEYFLDCYkadppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFVN 214
Cdd:PRK06482  83 NAGYGlFGAAEELSDAQ------IRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIE 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  215 KFSDDLQTEYKEHGILIQSVQPGFVATNM-SKIRKAS---VFAPSPETYVRSALSTLGIA 270
Cdd:PRK06482 157 GFVEAVAQEVAPFGIEFTIVEPGPARTNFgAGLDRGApldAYDDTPVGDLRRALADGSFA 216
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 52-211 3.92e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 56.55  E-value: 3.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLK-LVLISRSLEKLNVVAKEIgDKYGVEVRVIDVDFTGGDEIYDKIREKTTGLN- 129
Cdd:PRK06198   6 GKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAEL-EALGAKAVFVQADLSDVEDCRRVVAAADEAFGr 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VGVLVNNVGI-SYGHpeyFLDcykADPPFLRNIVAANIHS--------VTHMTALFLPGMISQrrgvIINVSSTAGVipn 200
Cdd:PRK06198  85 LDALVNAAGLtDRGT---ILD---TSPELFDRHFAVNVRApfflmqeaIKLMRRRKAEGTIVN----IGSMSAHGGQ--- 151

                        170
                 ....*....|.
gi 24640442  201 PLLSVYSSTKA 211
Cdd:PRK06198 152 PFLAAYCASKG 162
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 48-241 4.12e-09

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 56.24  E-value: 4.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   48 LSKMGEWAVVTGST--DGIGKAYAKELARRGLKLVL------------ISRSLEKLnVVAKEIGDkYGVEVRVIDVDFTG 113
Cdd:PRK12748   1 LPLMKKIALVTGASrlNGIGAAVCRRLAAKGIDIFFtywspydktmpwGMHDKEPV-LLKEEIES-YGVRCEHMEIDLSQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  114 GD---EIYDKIREKTTGLNVgvLVNNVGISyGHPEYfldcYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIIN 190
Cdd:PRK12748  79 PYapnRVFYAVSERLGDPSI--LINNAAYS-THTRL----EELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIIN 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24640442  191 VSSTAGVIPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK12748 152 LTSGQSLGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDT 202
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 52-237 5.07e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 56.17  E-value: 5.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKygveVRVIDVDFTGGDEIYDKIRE--KTTGlN 129
Cdd:PRK08265   6 GKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGER----ARFIATDITDDAAIERAVATvvARFG-R 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VGVLVNNvGISYGHPEyfLDCYKADppFLR----NIVAANIhsvthMTALFLPGMISqRRGVIINVSSTAGVIPNPLLSV 205
Cdd:PRK08265  81 VDILVNL-ACTYLDDG--LASSRAD--WLAaldvNLVSAAM-----LAQAAHPHLAR-GGGAIVNFTSISAKFAQTGRWL 149

                        170       180       190
                 ....*....|....*....|....*....|..
gi 24640442  206 YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPG 237
Cdd:PRK08265 150 YPASKAAIRQLTRSMAMDLAPDGIRVNSVSPG 181
PRK07062 PRK07062
SDR family oxidoreductase;
52-241 6.16e-09

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 55.82  E-value: 6.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGvEVRVIDV--DFTGGDEIYDKIREKTTGL- 128
Cdd:PRK07062   8 GRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFP-GARLLAArcDVLDEADVAAFAAAVEARFg 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  129 NVGVLVNNVGISYGHPeyFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSS 208
Cdd:PRK07062  87 GVDMLVNNAGQGRVST--FADTTDDA---WRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATSA 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 24640442  209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK07062 162 ARAGLLNLVKSLATELAPKGVRVNSILLGLVES 194
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 55-241 7.46e-09

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: 54.84  E-value: 7.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDkygvevRVIDVDFTGGDEIYDKIREKTTglnVGVLV 134
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGA------LARPADVAAELEVWALAQELGP---LDLLV 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 135 NNVGISYGHPeyfldCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTagVIPNPLLSVYSSTKAFVN 214
Cdd:cd11730  72 YAAGAILGKP-----LARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFLGAYPE--LVMLPGLSAYAAAKAALE 144

                       170       180
                ....*....|....*....|....*..
gi 24640442 215 KFSDDLQTEYKehGILIQSVQPGFVAT 241
Cdd:cd11730 145 AYVEVARKEVR--GLRLTLVRPPAVDT 169
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 52-243 1.30e-08

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: 55.17  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEI-GDKYGVEVRVIDVDFTGGDEIYDKIRE-KTTGLN 129
Cdd:cd09807   1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIrRDTLNHEVIVRHLDLASLKSIRAFAAEfLAEEDR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 130 VGVLVNNVGIsyghpeyfLDCykadpPFLRNIVAANIH-SVTHM-----TALFLPGMISQRRGVIINVSS---TAGVIPN 200
Cdd:cd09807  81 LDVLINNAGV--------MRC-----PYSKTEDGFEMQfGVNHLghfllTNLLLDLLKKSAPSRIVNVSSlahKAGKINF 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 24640442 201 PLLSV---YSSTKAFVNK------FSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd09807 148 DDLNSeksYNTGFAYCQSklanvlFTRELARRLQGTGVTVNALHPGVVRTEL 199
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 51-241 1.57e-08

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 54.71  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVL-ISRSLEKLNVVAKEIGDKygveVRVIDVDFTGGDEIYDKIREKT--TG 127
Cdd:PRK08642   4 SEQTVLVTGGSRGLGAAIARAFAREGARVVVnYHQSEDAAEALADELGDR----AIALQADVTDREQVQAMFATATehFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  128 LNVGVLVNNVgisyghpeyfLDCYKADP---PFLRNIVAAN--------IHSVTHMTALFLPGMISQRRGVIINVSSTag 196
Cdd:PRK08642  80 KPITTVVNNA----------LADFSFDGdarKKADDITWEDfqqqlegsVKGALNTIQAALPGMREQGFGRIINIGTN-- 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 24640442  197 VIPNPLLSV--YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK08642 148 LFQNPVVPYhdYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRT 194
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
51-242 1.74e-08

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 54.34  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLI-SRSLEKLNVVAKEIgDKYGVEVRVIDVDFtgGD-----EIYDKIREK 124
Cdd:PRK08063   3 SGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEI-EALGRKALAVKANV--GDvekikEMFAQIDEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  125 TTGLNvgVLVNNVGISYGHPEYFLDCYKADppFLRNIVA-ANIHSVTHMTALflpgMISQRRGVIINVSSTAG--VIPNp 201
Cdd:PRK08063  80 FGRLD--VFVNNAASGVLRPAMELEESHWD--WTMNINAkALLFCAQEAAKL----MEKVGGGKIISLSSLGSirYLEN- 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 24640442  202 LLSVYSStKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATN 242
Cdd:PRK08063 151 YTTVGVS-KAALEALTRYLAVELAPKGIAVNAVSGGAVDTD 190
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
47-106 3.76e-08

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 54.08  E-value: 3.76e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24640442  47 DLSKmGEWAVV--TGStdgIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRV 106
Cdd:COG5322 148 DLKK-ATVAVVgaTGS---IGSVCARLLAREVKRLTLVARNLERLEELAEEILRNPGGKVTI 205
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 55-229 4.29e-08

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: 53.16  E-value: 4.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEI---YDKIREKTTGLNVg 131
Cdd:cd05373   2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVialFDLIEEEIGPLEV- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 132 vLVNNVGisyghpeyfldcykADPPF-LRNIVAANIHSVTHMTAL--FLPG------MISQRRGVIINVSSTAGVIPNPL 202
Cdd:cd05373  81 -LVYNAG--------------ANVWFpILETTPRVFEKVWEMAAFggFLAAreaakrMLARGRGTIIFTGATASLRGRAG 145

                       170       180
                ....*....|....*....|....*..
gi 24640442 203 LSVYSSTKAFVNKFSDDLQTEYKEHGI 229
Cdd:cd05373 146 FAAFAGAKFALRALAQSMARELGPKGI 172
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 57-283 6.16e-08

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: 52.88  E-value: 6.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  57 VTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVrvidVDFTGGDEIYDKIREKTTGLNVGVLVNN 136
Cdd:cd08951  12 ITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLI----GDLSSLAETRKLADQVNAIGRFDAVIHN 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 137 VGISYGhPEYFLDCYKADPPFLRNIVAANIhsvthMTALFLPgmiSQRrgvIINVSST-------------AGVIPNPLL 203
Cdd:cd08951  88 AGILSG-PNRKTPDTGIPAMVAVNVLAPYV-----LTALIRR---PKR---LIYLSSGmhrggnaslddidWFNRGENDS 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 204 SVYSSTKAFVNKFSDDLQTEYKEhgILIQSVQPGFVATNMSkirkaSVFAPSP-----ETYVRSALSTLGIATQTAGYLP 278
Cdd:cd08951 156 PAYSDSKLHVLTLAAAVARRWKD--VSSNAVHPGWVPTKMG-----GAGAPDDleqghLTQVWLAESDDPQALTSGGYFY 228


                ....*
gi 24640442 279 HALLQ 283
Cdd:cd08951 229 HRRLQ 233
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 57-243 7.66e-08

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 52.57  E-value: 7.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   57 VTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGG-----DEIYDKIREKTTGLNvG 131
Cdd:PRK08945  17 VTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIPLDLLTAtpqnyQQLADTIEEQFGRLD-G 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  132 VLvNNVGI-------SYGHPEYFLDcykadppflrnIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLS 204
Cdd:PRK08945  96 VL-HNAGLlgelgpmEQQDPEVWQD-----------VMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANWG 163

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 24640442  205 VYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK08945 164 AYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAM 202
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 51-237 7.79e-08

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 52.34  E-value: 7.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGvEVRVIDVDFTGGDE-----IYDKIREKT 125
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYG-EGMAYGFGADATSEqsvlaLSRGVDEIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  126 TGLNvgVLVNNVGISYGHP--EYFLDCYKadppflrNIVAANihsvthMTALFLPG------MISQR-RGVIINVSSTAG 196
Cdd:PRK12384  80 GRVD--LLVYNAGIAKAAFitDFQLGDFD-------RSLQVN------LVGYFLCArefsrlMIRDGiQGRIIQINSKSG 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 24640442  197 VIPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPG 237
Cdd:PRK12384 145 KVGSKHNSGYSAAKFGGVGLTQSLALDLAEYGITVHSLMLG 185
PRK06101 PRK06101
SDR family oxidoreductase;
57-241 9.17e-08

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 52.18  E-value: 9.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   57 VTGSTDGIGKAYAKELARRGLKLVLISRSLEklnvVAKEIGDKYGvEVRVIDVDFTGGDEIYDKIREKTTGLNVGVLvnn 136
Cdd:PRK06101   6 ITGATSGIGKQLALDYAKQGWQVIACGRNQS----VLDELHTQSA-NIFTLAFDVTDHPGTKAALSQLPFIPELWIF--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  137 vgiSYGHPEYfLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIinVSSTAGVIPNPLLSVYSSTKAFVNKF 216
Cdd:PRK06101  78 ---NAGDCEY-MDDGKVDATLMARVFNVNVLGVANCIEGIQPHLSCGHRVVI--VGSIASELALPRAEAYGASKAAVAYF 151

                        170       180
                 ....*....|....*....|....*
gi 24640442  217 SDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK06101 152 ARTLQLDLRPKGIEVVTVFPGFVAT 176
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
52-242 2.25e-07

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 51.03  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLI-----SRSLEKLNVVAKEIGDkygvevrvIDVDFTGGDEIYDKIREKTT 126
Cdd:PRK08993  10 GKVAVVTGCDTGLGQGMALGLAEAGCDIVGInivepTETIEQVTALGRRFLS--------LTADLRKIDGIPALLERAVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  127 GL-NVGVLVNNVGISygHPEYFLDCYKADPPFLRNIvaaNIHSVTHMTALFLPGMISQRRG-VIINVSSTAGVIPNPLLS 204
Cdd:PRK08993  82 EFgHIDILVNNAGLI--RREDAIEFSEKDWDDVMNL---NIKSVFFMSQAAAKHFIAQGNGgKIINIASMLSFQGGIRVP 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 24640442  205 VYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATN 242
Cdd:PRK08993 157 SYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATN 194
PRK12742 PRK12742
SDR family oxidoreductase;
52-243 2.95e-07

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 50.53  E-value: 2.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLI-SRSLEKLNVVAKEIGdkygveVRVIDVDFTGGDEIYDKIREKTTglnV 130
Cdd:PRK12742   6 GKKVLVLGGSRGIGAAIVRRFVTDGANVRFTyAGSKDAAERLAQETG------ATAVQTDSADRDAVIDVVRKSGA---L 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 GVLVNNVGISYghpeyFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINvSSTAGVIPNPLLSVYSSTK 210
Cdd:PRK12742  77 DILVVNAGIAV-----FGDALELDADDIDRLFKINIHAPYHASVEAARQMPEGGRIIIIG-SVNGDRMPVAGMAAYAASK 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 24640442  211 AFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK12742 151 SALQGMARGLARDFGPRGITINVVQPGPIDTDA 183
PRK06500 PRK06500
SDR family oxidoreductase;
51-241 3.39e-07

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 50.34  E-value: 3.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDkygvEVRVIDVDftGGD-----EIYDKIREKT 125
Cdd:PRK06500   5 QGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGE----SALVIRAD--AGDvaaqkALAQALAEAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  126 TGLNVGVLvnNVGISYGHP-----EYFLDcykadppflrNIVAANIHSVTHMTALFLPgMISQRRGVIINVSSTAGvIPN 200
Cdd:PRK06500  79 GRLDAVFI--NAGVAKFAPledwdEAMFD----------RSFNTNVKGPYFLIQALLP-LLANPASIVLNGSINAH-IGM 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 24640442  201 PLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK06500 145 PNSSVYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQT 185
PRK05993 PRK05993
SDR family oxidoreductase;
50-318 4.15e-07

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 50.41  E-value: 4.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   50 KMGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEigdkyGVEvrVIDVDFTGGDEI---YDKIREKTT 126
Cdd:PRK05993   2 DMKRSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEAE-----GLE--AFQLDYAEPESIaalVAQVLELSG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  127 GlNVGVLVNNvGiSYGHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVY 206
Cdd:PRK05993  75 G-RLDALFNN-G-AYGQPGAVEDLPTEA---LRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAY 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  207 SSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATN-----MSKIRKASVFAPSP--ETYVRSALSTLGIATQTAGYLP- 278
Cdd:PRK05993 149 NASKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETRfranaLAAFKRWIDIENSVhrAAYQQQMARLEGGGSKSRFKLGp 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24640442  279 --------HALL--QLVIHFTEAVFGEQFArniVMKNILGTR--KRALRRLA 318
Cdd:PRK05993 229 eavyavllHALTapRPRPHYRVTTPAKQGA---LLKRLLPARwlYRLLRKAA 277
PRK07041 PRK07041
SDR family oxidoreductase;
56-109 8.78e-07

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 49.27  E-value: 8.78e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDV 109
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGAPVRTAALDI 54
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 55-243 1.01e-06

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: 48.28  E-value: 1.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGL-KLVLISRSleklnvvakeigdkygvevrvidvdftggdeiydkirekttglnvGVL 133
Cdd:cd02266   1 VLVTGGSGGIGGAIARWLASRGSpKVLVVSRR---------------------------------------------DVV 35

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 134 VNNVGISYGHPEYFLDCYKADPpFLRnivaANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFV 213
Cdd:cd02266  36 VHNAAILDDGRLIDLTGSRIER-AIR----ANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAAL 110

                       170       180       190
                ....*....|....*....|....*....|
gi 24640442 214 NKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd02266 111 DGLAQQWASEGWGNGLPATAVACGTWAGSG 140
PRK06947 PRK06947
SDR family oxidoreductase;
56-243 1.56e-06

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 48.65  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKL-VLISRSLEKLNVVAKEIGDKyGVEVRVIDVDFTGGDEI---YDKIREKTTGLNvg 131
Cdd:PRK06947   6 LITGASRGIGRATAVLAAARGWSVgINYARDAAAAEETADAVRAA-GGRACVVAGDVANEADViamFDAVQSAFGRLD-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  132 VLVNNVGISygHPEYFLdcykADPPF--LRNIVAANIHSVthmtalFLPGMISQRR---------GVIINVSSTAGVIPN 200
Cdd:PRK06947  83 ALVNNAGIV--APSMPL----ADMDAarLRRMFDTNVLGA------YLCAREAARRlstdrggrgGAIVNVSSIASRLGS 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 24640442  201 PLLSV-YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK06947 151 PNEYVdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
PRK06128 PRK06128
SDR family oxidoreductase;
52-241 1.79e-06

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 48.70  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLisrsleklNVVAKEIGDKYGVeVRVIDVD-----FTGGD--------EIY 118
Cdd:PRK06128  55 GRKALITGADSGIGRATAIAFAREGADIAL--------NYLPEEEQDAAEV-VQLIQAEgrkavALPGDlkdeafcrQLV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  119 DKIREKTTGLNVgvLVNNVG-------ISYGHPEYFLDCYKADPPFLRNIVAAnihSVTHMTalflPGmisqrrGVIINV 191
Cdd:PRK06128 126 ERAVKELGGLDI--LVNIAGkqtavkdIADITTEQFDATFKTNVYAMFWLCKA---AIPHLP----PG------ASIINT 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 24640442  192 SSTAGVIPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK06128 191 GSIQSYQPSPTLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWT 240
PRK08628 PRK08628
SDR family oxidoreductase;
56-241 2.40e-06

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 48.03  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKlNVVAKEIgDKYGVEVRVIDVDFTGGDEIYDKIRE--KTTGlNVGVL 133
Cdd:PRK08628  11 IVTGGASGIGAAISLRLAEEGAIPVIFGRSAPD-DEFAEEL-RALQPRAEFVQVDLTDDAQCRDAVEQtvAKFG-RIDGL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  134 VNNVGISYG-----HPEYFLDCYKadppflRNIvaanIHSVThMTALFLPgMISQRRGVIINVSSTAGVIPNPLLSVYSS 208
Cdd:PRK08628  88 VNNAGVNDGvgleaGREAFVASLE------RNL----IHYYV-MAHYCLP-HLKASRGAIVNISSKTALTGQGGTSGYAA 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 24640442  209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT 241
Cdd:PRK08628 156 AKGAQLALTREWAVALAKDGVRVNAVIPAEVMT 188
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 56-237 3.69e-06

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 47.37  E-value: 3.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIgDKYGVEVRVIDVDFTGGDEIYDKIRE--KTTGlNVGVL 133
Cdd:PRK07677   5 IITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEI-EQFPGQVLTVQMDVRNPEDVQKMVEQidEKFG-RIDAL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  134 VNNVGISYGHP--EYFLDCYKAdppfLRNIVaanIHSVTHMTALFLPGMISQ-RRGVIINVSST------AGVIPNplls 204
Cdd:PRK07677  83 INNAAGNFICPaeDLSVNGWNS----VIDIV---LNGTFYCSQAVGKYWIEKgIKGNIINMVATyawdagPGVIHS---- 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 24640442  205 vySSTKAFVNKFSDDLQTEY-KEHGILIQSVQPG 237
Cdd:PRK07677 152 --AAAKAGVLAMTRTLAVEWgRKYGIRVNAIAPG 183
PRK08416 PRK08416
enoyl-ACP reductase;
51-275 4.32e-06

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 47.46  E-value: 4.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKL-NVVAKEIGDKYGVEVRVIDVDFTGGD---EIYDKIREKTT 126
Cdd:PRK08416   7 KGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVEEaNKIAEDLEQKYGIKAKAYPLNILEPEtykELFKKIDEDFD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  127 glNVGVLVNNvGISYGHPEY--FLDCYKADPPFLRNIVAANIHSvthmtalFLPG-------MISQRRGVIINVSSTAGV 197
Cdd:PRK08416  87 --RVDFFISN-AIISGRAVVggYTKFMRLKPKGLNNIYTATVNA-------FVVGaqeaakrMEKVGGGSIISLSSTGNL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  198 IPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVAT-------NMSKIRKasvfapspETYVRSALSTLGIA 270
Cdd:PRK08416 157 VYIENYAGHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTdalkaftNYEEVKA--------KTEELSPLNRMGQP 228


                 ....*
gi 24640442  271 TQTAG 275
Cdd:PRK08416 229 EDLAG 233
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 56-261 5.46e-06

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 46.68  E-value: 5.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGdKYGvEVRVIDVDFTGGDEIYDKIREKTTGLN-VGVLV 134
Cdd:PRK05786   9 AIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLS-KYG-NIHYVVGDVSSTESARNVIEKAAKVLNaIDGLV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  135 NNVGisyGHPEYFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGmisqrrGVIINVSSTAGV-IPNPLLSVYSSTKAFV 213
Cdd:PRK05786  87 VTVG---GYVEDTVEEFSGLEEMLTNHIKIPLYAVNASLRFLKEG------SSIVLVSSMSGIyKASPDQLSYAVAKAGL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 24640442  214 NKFSDDLQTEYKEHGILIQSVQPGFVA------TNMSKIRKASVFAPSPETYVR 261
Cdd:PRK05786 158 AKAVEILASELLGRGIRVNGIAPTTISgdfepeRNWKKLRKLGDDMAPPEDFAK 211
PRK08703 PRK08703
SDR family oxidoreductase;
56-127 7.00e-06

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 46.46  E-value: 7.00e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDF-TGGDEIYDK----IREKTTG 127
Cdd:PRK08703  10 LVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPEPFAIRFDLmSAEEKEFEQfaatIAEATQG 86
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 52-110 9.72e-06

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 45.46  E-value: 9.72e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVD 110
Cdd:cd01078  28 GKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAADSLRARFGEGVGAVETS 86
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 56-193 1.42e-05

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 45.66  E-value: 1.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYG-VEVRVIDVDFTGGDEIYDKIRE-KTTGLNVGVL 133
Cdd:cd09808   5 LITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETESGnQNIFLHIVDMSDPKQVWEFVEEfKEEGKKLHVL 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 134 VNNVGISYGHPEYFLDCYKADppflrniVAANIHSVTHMTALFLPGMISQRRGVIINVSS 193
Cdd:cd09808  85 INNAGCMVNKRELTEDGLEKN-------FATNTLGTYILTTHLIPVLEKEEDPRVITVSS 137
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
59-245 1.49e-05

decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 45.47  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   59 GSTDGIGKAYAKELARRG-LKLVLISRSLE-KLNVVAKEIGDKYGVEVRVIDVDFTGGDEIYDKIREKTTGLNVGVLVNN 136
Cdd:PRK07904  15 GGTSEIGLAICERYLKNApARVVLAALPDDpRRDAAVAQMKAAGASSVEVIDFDALDTDSHPKVIDAAFAGGDVDVAIVA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  137 VGISYGHPEYFLDCYKAdppflrnIVAANIHSVTHMTALFLPG--MISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFVN 214
Cdd:PRK07904  95 FGLLGDAEELWQNQRKA-------VQIAEINYTAAVSVGVLLGekMRAQGFGQIIAMSSVAGERVRRSNFVYGSTKAGLD 167

                        170       180       190
                 ....*....|....*....|....*....|.
gi 24640442  215 KFSDDLQTEYKEHGILIQSVQPGFVATNMSK 245
Cdd:PRK07904 168 GFYLGLGEALREYGVRVLVVRPGQVRTRMSA 198
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 52-141 1.67e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 45.79  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEI-GDKYGVEVRVIDVDFTGgdeiYDKIREKTTGL-- 128
Cdd:PRK06197  16 GRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARItAATPGADVTLQELDLTS----LASVRAAADALra 91

                         90
                 ....*....|....*.
gi 24640442  129 ---NVGVLVNNVGISY 141
Cdd:PRK06197  92 aypRIDLLINNAGVMY 107
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 56-133 1.93e-05

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: 45.82  E-value: 1.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  56 VVTGSTDGIGKAYAKELARR-GLKLVLISRS----LEKLNVVAKEIGDKYGVEVRVIDVDFTGGD---EIYDKIREKTTG 127
Cdd:cd08953 209 LVTGGAGGIGRALARALARRyGARLVLLGRSplppEEEWKAQTLAALEALGARVLYISADVTDAAavrRLLEKVRERYGA 288


                ....*.
gi 24640442 128 LNvGVL 133
Cdd:cd08953 289 ID-GVI 293
PRK06123 PRK06123
SDR family oxidoreductase;
55-243 2.12e-05

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 45.15  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVL-ISRSLEKLNVVAKEIGDKYGVEVRV-IDVDFTGGDEIYDKIREKTTGlNVGV 132
Cdd:PRK06123   5 MIITGASRGIGAATALLAAERGYAVCLnYLRNRDAAEAVVQAIRRQGGEALAVaADVADEADVLRLFEAVDRELG-RLDA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  133 LVNNVGISygHPEYFLDcyKADPPFLRNIVAANI--------HSVTHMTALFlpgmiSQRRGVIINVSSTAGVIPNPLLS 204
Cdd:PRK06123  84 LVNNAGIL--EAQMRLE--QMDAARLTRIFATNVvgsflcarEAVKRMSTRH-----GGRGGAIVNVSSMAARLGSPGEY 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 24640442  205 V-YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK06123 155 IdYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEI 194
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 52-258 2.25e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 44.95  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRV-IDV-DFTGGDEIYDKIREKTTGLN 129
Cdd:PRK07576   9 GKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVsADVrDYAAVEAAFAQIADEFGPID 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VGV-------LVNNVGISYGHPEYFLD--------CYKADPPFLRNivaanihsvthmtalflPGmisqrrGVIINVSST 194
Cdd:PRK07576  89 VLVsgaagnfPAPAAGMSANGFKTVVDidllgtfnVLKAAYPLLRR-----------------PG------ASIIQISAP 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24640442  195 AGVIPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVA--TNMSKIrkasvfAPSPET 258
Cdd:PRK07576 146 QAFVPMPMQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPGPIAgtEGMARL------APSPEL 205
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 51-237 3.41e-05

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


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 44.38  E-value: 3.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  51 MGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIYDKIREKTTGLN- 129
Cdd:cd05322   1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKr 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 130 VGVLVNNVGISYGHP--EYFLDCYKadppflrNIVAANihsvthMTALFLPG------MISQ-RRGVIINVSSTAGVIPN 200
Cdd:cd05322  81 VDLLVYSAGIAKSAKitDFELGDFD-------RSLQVN------LVGYFLCArefsklMIRDgIQGRIIQINSKSGKVGS 147

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24640442 201 PLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPG 237
Cdd:cd05322 148 KHNSGYSAAKFGGVGLTQSLALDLAEHGITVNSLMLG 184
PRK12746 PRK12746
SDR family oxidoreductase;
52-244 3.64e-05

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 44.64  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRG-LKLVLISRSLEKLNVVAKEI----GDKYGVEVRVIDVDFTGG--DEIYDKIREK 124
Cdd:PRK12746   6 GKVALVTGASRGIGRAIAMRLANDGaLVAIHYGRNKQAADETIREIesngGKAFLIEADLNSIDGVKKlvEQLKNELQIR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  125 TTGLNVGVLVNNVGI-SYGHPEyfldcyKADPPFLRNIVAANIHSVTHMTALFLPgmISQRRGVIINVSSTAGVIPNPLL 203
Cdd:PRK12746  86 VGTSEIDILVNNAGIgTQGTIE------NTTEEIFDEIMAVNIKAPFFLIQQTLP--LLRAEGRVINISSAEVRLGFTGS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 24640442  204 SVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMS 244
Cdd:PRK12746 158 IAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDIN 198
COG3268 COG3268
Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];
56-144 3.90e-05

Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];


Pssm-ID: 442499 [Multi-domain]  Cd Length: 368  Bit Score: 44.83  E-value: 3.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKyGVEVRVIDVDftggDEiyDKIREKTTGlnVGVLVN 135
Cdd:COG3268   9 VVYGATGYTGRLVAEYLARRGLRPALAGRNAAKLEAVAAELGAA-DLPLRVADLD----DP--ASLAALLAG--TRVVLN 79

                        90
                ....*....|.
gi 24640442 136 NVG--ISYGHP 144
Cdd:COG3268  80 TVGpfARTGEP 90
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 56-243 4.15e-05

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: 44.41  E-value: 4.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  56 VVTGSTDGIGKAYAKELARRGLKLVLISRsleKLNVVAKEIGDKYGVevrvidvdftggDEIYDKIREKTTGLnVGVLVN 135
Cdd:cd05328   3 VITGAASGIGAATAELLEDAGHTVIGIDL---READVIADLSTPEGR------------AAAIADVLARCSGV-LDGLVN 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 136 NVGISYghpeyfldcykadPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPN--------------- 200
Cdd:cd05328  67 CAGVGG-------------TTVAGLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAGWAqdklelakalaagte 133

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24640442 201 ------------PLLSVYSSTKAFVNKFSDDL-QTEYKEHGILIQSVQPGFVATNM 243
Cdd:cd05328 134 aravalaehagqPGYLAYAGSKEALTVWTRRRaATWLYGAGVRVNTVAPGPVETPI 189
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 55-139 6.66e-05

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 44.05  E-value: 6.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  55 AVVTGSTDGIGKAYAKELARRGL-KLVLISRSLEKLNVVAKEIGDKYGvEVRVIDVDFTGGDEIYDKIRE-KTTGLNVGV 132
Cdd:cd09810   4 VVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVGMPKD-SYSVLHCDLASLDSVRQFVDNfRRTGRPLDA 82


                ....*..
gi 24640442 133 LVNNVGI 139
Cdd:cd09810  83 LVCNAAV 89
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
52-249 7.50e-05

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 43.35  E-value: 7.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLIS-RSLEKLNVVAKEIGDKYgvevRVIDVDFTGGDEIYDKIREKTTGL-N 129
Cdd:PRK12481   8 GKVAIITGCNTGLGQGMAIGLAKAGADIVGVGvAEAPETQAQVEALGRKF----HFITADLIQQKDIDSIVSQAVEVMgH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  130 VGVLVNNVGISygHPEYFLDCYKADPPFLRNIvaaNIHSVTHMTALFLPGMISQRR-GVIINVSSTAGVIPNPLLSVYSS 208
Cdd:PRK12481  84 IDILINNAGII--RRQDLLEFGNKDWDDVINI---NQKTVFFLSQAVAKQFVKQGNgGKIINIASMLSFQGGIRVPSYTA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 24640442  209 TKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNMSKIRKA 249
Cdd:PRK12481 159 SKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALRA 199
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 43-139 1.71e-04

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 42.85  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   43 GSSVDLSkmGEWAVVTGSTDGIGKAYAKELARRGLKLVL--ISRSLEKLNVVAkEIGDKYGVEVRVI-DV-DFTGGDEIY 118
Cdd:PRK07792   5 TNTTDLS--GKVAVVTGAAAGLGRAEALGLARLGATVVVndVASALDASDVLD-EIRAAGAKAVAVAgDIsQRATADELV 81

                         90       100
                 ....*....|....*....|..
gi 24640442  119 dkirEKTTGL-NVGVLVNNVGI 139
Cdd:PRK07792  82 ----ATAVGLgGLDIVVNNAGI 99
PRK06196 PRK06196
oxidoreductase; Provisional
 46-139 1.98e-04

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 42.36  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   46 VDLSkmGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGdkyGVEVRVIDV-DFTGGDEIYDKIREK 124
Cdd:PRK06196  22 HDLS--GKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGID---GVEVVMLDLaDLESVRAFAERFLDS 96

                         90
                 ....*....|....*
gi 24640442  125 TTGLNvgVLVNNVGI 139
Cdd:PRK06196  97 GRRID--ILINNAGV 109
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 56-216 2.23e-04

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 41.39  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442    56 VVTGSTDGIGKAYAKELARRGLK-LVLISRSLEKLNVVAKEIGD--KYGVEVRVIDVDFTGGDEI---YDKIREKTTGLN 129
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARhLVLLSRSAAPRPDAQALIAEleARGVEVVVVACDVSDPDAVaalLAEIKAEGPPIR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   130 vGVlVNNVGISygHPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQrrgvIINVSSTAGVIPNPLLSVYSST 209
Cdd:pfam08659  84 -GV-IHAAGVL--RDALLENMTDED---WRRVLAPKVTGTWNLHEATPDEPLDF----FVLFSSIAGLLGSPGQANYAAA 152


                  ....*..
gi 24640442   210 KAFVNKF 216
Cdd:pfam08659 153 NAFLDAL 159
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 56-175 4.55e-04

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 40.60  E-value: 4.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEigdkyGVEVRVIDVDftggDEiyDKIREKTTGlnVGVLVN 135
Cdd:COG0702   3 LVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAALAAA-----GVEVVQGDLD----DP--ESLAAALAG--VDAVFL 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 24640442 136 NVGISYGHPeyFLDCYKADPPFLRNIVAANIHSVTHMTAL 175
Cdd:COG0702  70 LVPSGPGGD--FAVDVEGARNLADAAKAAGVKRIVYLSAL 107
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 52-254 6.34e-04

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


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 40.64  E-value: 6.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIG-DKYGVEVRVIDVDFTGGDEIydKIREKTTGLNv 130
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGpNLFFVHGDVADETLVKFVVY--AMLEKLGRID- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 131 gVLVNNVGI---------SYGHPEYfldcykadppflrnIVAANIHSVTHMTALFLPGMISQrRGVIINVSSTAGVIPNP 201
Cdd:cd09761  78 -VLVNNAARgskgilsslLLEEWDR--------------ILSVNLTGPYELSRYCRDELIKN-KGRIINIASTRAFQSEP 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 24640442 202 LLSVYSSTKAFVNKFSDDLQTEYKEHgILIQSVQPGFVATNMSKIRKASVFAP 254
Cdd:cd09761 142 DSEAYAASKGGLVALTHALAMSLGPD-IRVNCISPGWINTTEQQEFTAAPLTQ 193
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 56-243 7.01e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 40.56  E-value: 7.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGV-EVRVIDVDFTGGDEIydkIREKTTGLNVGVLV 134
Cdd:PRK05875  11 LVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEALKGAgAVRYEPADVTDEDQV---ARAVDAATAWHGRL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  135 NNVGISYGHPEYFLDCYKADPPFLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFVN 214
Cdd:PRK05875  88 HGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVTKSAVD 167

                        170       180
                 ....*....|....*....|....*....
gi 24640442  215 KFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK05875 168 HLMKLAADELGPSWVRVNSIRPGLIRTDL 196
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
 57-110 7.18e-04

triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical 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: 187578 [Multi-domain]  Cd Length: 272  Bit Score: 40.72  E-value: 7.18e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24640442  57 VTGSTDGIGKAYAKELARRGLKLVLISRSLEKlnvvAKEIGDKyGVEVRVIDVD 110
Cdd:cd05269   3 VTGATGKLGTAVVELLLAKVASVVALVRNPEK----AKAFAAD-GVEVRQGDYD 51
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 52-210 1.15e-03

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 39.94  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   52 GEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKygVEVRVIDV-DFTGGDEIYDKIREKTTGLNv 130
Cdd:PRK06200   6 GQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDH--VLVVEGDVtSYADNQRAVDQTVDAFGKLD- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  131 gVLVNNVGI-SYGHPEYFLDCYKADPPFLRnIVAANIHSVTHMTALFLPGMIsQRRGVIINVSSTAGVIPNPLLSVYSST 209
Cdd:PRK06200  83 -CFVGNAGIwDYNTSLVDIPAETLDTAFDE-IFNVNVKGYLLGAKAALPALK-ASGGSMIFTLSNSSFYPGGGGPLYTAS 159


                 .
gi 24640442  210 K 210
Cdd:PRK06200 160 K 160
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 59-100 1.29e-03

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 40.36  E-value: 1.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 24640442   59 GSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKY 100
Cdd:PRK08655   7 GGTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKELGVEY 48
PRK08177 PRK08177
SDR family oxidoreductase;
55-243 1.32e-03

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 39.63  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   55 AVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKlnvvAKEIGDKYGVEVRVIDVDFTggdEIYDKIREKTTGLNVGVLV 134
Cdd:PRK08177   4 ALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQ----DTALQALPGVHIEKLDMNDP---ASLDQLLQRLQGQRFDLLF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  135 NNVGISYGHPEyflDCYKADPP-----FLRNIVAA-NIhsvthmtALFLPGMISQRRGVIINVSSTAGVIPNPL---LSV 205
Cdd:PRK08177  77 VNAGISGPAHQ---SAADATAAeigqlFLTNAIAPiRL-------ARRLLGQVRPGQGVLAFMSSQLGSVELPDggeMPL 146

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 24640442  206 YSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFVATNM 243
Cdd:PRK08177 147 YKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDM 184
PRK05854 PRK05854
SDR family oxidoreductase;
47-139 1.74e-03

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 39.66  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   47 DLSkmGEWAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKY-GVEVRVIDVDFTGGDEIY---DKIR 122
Cdd:PRK05854  11 DLS--GKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTAVpDAKLSLRALDLSSLASVAalgEQLR 88

                         90
                 ....*....|....*..
gi 24640442  123 EKttGLNVGVLVNNVGI 139
Cdd:PRK05854  89 AE--GRPIHLLINNAGV 103
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 172-239 1.78e-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: 39.10  E-value: 1.78e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24640442 172 MTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKAFVNKFSDDLQTEYKEHGILIQSVQPGFV 239
Cdd:cd05361 111 LLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFF 178
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 56-110 2.54e-03

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 38.23  E-value: 2.54e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24640442     56 VVTGSTDGIGKAYAKELARRG-LKLVLISRSLEKLNVVAKEIGD--KYGVEVRVIDVD 110
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGaRRLVLLSRSGPDAPGAAALLAEleAAGARVTVVACD 61
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 54-211 2.54e-03

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: 38.80  E-value: 2.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442  54 WAVVTGSTDGIGKAYAKELARRGLKLVLISRSLEKLNVVAKEIGDKYGVEVRVIDVDFTGGDEIYDKIR--EKTTGlNVG 131
Cdd:cd05357   2 VALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDELNALRNSAVLVQADLSDFAACADLVAaaFRAFG-RCD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442 132 VLVNNVGISYghPEYFLDCYKADppfLRNIVAANIHSVTHMTALFLPGMISQRRGVIINVSSTAGVIPNPLLSVYSSTKA 211
Cdd:cd05357  81 VLVNNASAFY--PTPLGQGSEDA---WAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKA 155
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 54-112 4.81e-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: 38.52  E-value: 4.81e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640442  54 WAVVTGSTDGIGKAYAKELARRGLK-LVLISRSLEKLNVVAKEIGDK-YGVEVRVIDVDFT 112
Cdd:cd05274 152 TYLITGGLGGLGLLVARWLAARGARhLVLLSRRGPAPRAAARAALLRaGGARVSVVRCDVT 212
PLN00015 PLN00015
protochlorophyllide reductase
 56-141 5.02e-03

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 38.15  E-value: 5.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640442   56 VVTGSTDGIGKAYAKELARRGLKLVLIS-RSLEKLNVVAKEIG---DKYgvevRVIDVDFTGGDEIYDKIRE-KTTGLNV 130
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGKWHVVMAcRDFLKAERAAKSAGmpkDSY----TVMHLDLASLDSVRQFVDNfRRSGRPL 76

                         90
                 ....*....|.
gi 24640442  131 GVLVNNVGISY 141
Cdd:PLN00015  77 DVLVCNAAVYL 87
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
 57-111 5.06e-03

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: 37.98  E-value: 5.06e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24640442  57 VTGSTDGIGKAYAKELARRGLK-LVLISRSLEKLNVVAKEIGDKY-GVEVRVIDVDF 111
Cdd:cd05237   7 VTGGAGSIGSELVRQILKFGPKkLIVFDRDENKLHELVRELRSRFpHDKLRFIIGDV 63
 
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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