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Conserved domains on  [gi|153792573|ref|NP_032317|]
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17-beta-hydroxysteroid dehydrogenase type 3 [Mus musculus]

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) ...
 44-280 1.36e-105

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: 307.61  E-value: 1.36e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFT-REDIYDHIKEHLEGLEIG 122
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSaGDDIYERIEKELEGLDIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ILVNNVGMLPSFfPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:cd05356   81 ILVNNVGISHSI-PEYFLETPEDElQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 202 YTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLN-NKMTKTADEFVKESLKYVTIGAESCGCLAHEIIAIILNRIPSRI 280
Cdd:cd05356  160 DFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKsSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARLVPEWI 239
 
Name Accession Description Interval E-value
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 44-280 1.36e-105

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: 307.61  E-value: 1.36e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFT-REDIYDHIKEHLEGLEIG 122
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSaGDDIYERIEKELEGLDIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ILVNNVGMLPSFfPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:cd05356   81 ILVNNVGISHSI-PEYFLETPEDElQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 202 YTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLN-NKMTKTADEFVKESLKYVTIGAESCGCLAHEIIAIILNRIPSRI 280
Cdd:cd05356  160 DFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKsSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARLVPEWI 239
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 45-236 5.52e-59

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 187.44  E-value: 5.52e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573   45 QWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTtGSCVKIVQADFTRED----IYDHIKEHLEGle 120
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAL-GGKALFIQGDVTDRAqvkaLVEQAVERLGR-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  121 IGILVNNVGMLPsFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAF 200
Cdd:pfam00106  78 LDILVNNAGITG-LGPFSELSDE-DWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAA 155

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 153792573  201 VYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLN 236
Cdd:pfam00106 156 VIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
43-255 1.62e-54

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 177.75  E-value: 1.62e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTRED----IYDHIKEHLEG 118
Cdd:COG0300    4 TGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAEL-RAAGARVEVVALDVTDPDavaaLAEAVLARFGP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 leIGILVNNVGMLPsffPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSAS 197
Cdd:COG0300   83 --IDVLVNNAGVGG---GGPFEELDLEDlRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAAS 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792573 198 KAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTK---TADEFVKESLKYVT 255
Cdd:COG0300  158 KAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRpllSPEEVARAILRALE 218
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 28-299 2.93e-49

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 166.19  E-value: 2.93e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  28 FLRfckalPSSFLRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSC-VKIVQADFTrE 106
Cdd:PLN02780  42 FLR-----PAKNLKKYGSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKTqIKTVVVDFS-G 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 107 DIYD---HIKEHLEGLEIGILVNNVGMlpSFFPSHFLSTSGES--QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISS 181
Cdd:PLN02780 116 DIDEgvkRIKETIEGLDVGVLINNVGV--SYPYARFFHEVDEEllKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGS 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 182 GAA--LRPWPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNK-MTKTADEFVKESLKYVTIGA 258
Cdd:PLN02780 194 GAAivIPSDPLYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMASIRRSSfLVPSSDGYARAALRWVGYEP 273

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 153792573 259 ESCGCLAHEIIAIILNRIPSRIFYSSTAQRFLLTRYSDYLK 299
Cdd:PLN02780 274 RCTPYWPHSLIWGLISALPESAVDSWRLKFCLQIRKKGQQK 314
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 47-232 1.05e-17

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: 80.73  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573   47 AVITGAGDGIGKAYSFELAR----HGLNVVLISRTLEKLQTIAEEIERTT-GSCVKIVQADFTRE-DIYDHIKEHLE--- 117
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIGAERsGLRVVRVSLDLGAEaGLEQLLKALRElpr 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  118 --GLEIGILVNNVGMLPSFFP-SHFLSTSGESQNLIHCNITSVVKMTQLVLKHMESRR--KGLILNISSGAALRPWPLYS 192
Cdd:TIGR01500  83 pkGLQRLLLINNAGTLGDVSKgFVDLSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPglNRTVVNISSLCAIQPFKGWA 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 153792573  193 LYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:TIGR01500 163 LYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQ 202
 
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) ...
 44-280 1.36e-105

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: 307.61  E-value: 1.36e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFT-REDIYDHIKEHLEGLEIG 122
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSaGDDIYERIEKELEGLDIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ILVNNVGMLPSFfPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:cd05356   81 ILVNNVGISHSI-PEYFLETPEDElQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 202 YTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLN-NKMTKTADEFVKESLKYVTIGAESCGCLAHEIIAIILNRIPSRI 280
Cdd:cd05356  160 DFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKsSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARLVPEWI 239
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 45-236 5.52e-59

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 187.44  E-value: 5.52e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573   45 QWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTtGSCVKIVQADFTRED----IYDHIKEHLEGle 120
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAL-GGKALFIQGDVTDRAqvkaLVEQAVERLGR-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  121 IGILVNNVGMLPsFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAF 200
Cdd:pfam00106  78 LDILVNNAGITG-LGPFSELSDE-DWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAA 155

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 153792573  201 VYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLN 236
Cdd:pfam00106 156 VIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
43-255 1.62e-54

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 177.75  E-value: 1.62e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTRED----IYDHIKEHLEG 118
Cdd:COG0300    4 TGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAEL-RAAGARVEVVALDVTDPDavaaLAEAVLARFGP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 leIGILVNNVGMLPsffPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSAS 197
Cdd:COG0300   83 --IDVLVNNAGVGG---GGPFEELDLEDlRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAAS 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792573 198 KAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTK---TADEFVKESLKYVT 255
Cdd:COG0300  158 KAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRpllSPEEVARAILRALE 218
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 28-299 2.93e-49

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 166.19  E-value: 2.93e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  28 FLRfckalPSSFLRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSC-VKIVQADFTrE 106
Cdd:PLN02780  42 FLR-----PAKNLKKYGSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKTqIKTVVVDFS-G 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 107 DIYD---HIKEHLEGLEIGILVNNVGMlpSFFPSHFLSTSGES--QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISS 181
Cdd:PLN02780 116 DIDEgvkRIKETIEGLDVGVLINNVGV--SYPYARFFHEVDEEllKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGS 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 182 GAA--LRPWPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNK-MTKTADEFVKESLKYVTIGA 258
Cdd:PLN02780 194 GAAivIPSDPLYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMASIRRSSfLVPSSDGYARAALRWVGYEP 273

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 153792573 259 ESCGCLAHEIIAIILNRIPSRIFYSSTAQRFLLTRYSDYLK 299
Cdd:PLN02780 274 RCTPYWPHSLIWGLISALPESAVDSWRLKFCLQIRKKGQQK 314
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 43-233 1.31e-44

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: 151.86  E-value: 1.31e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTtGSCVKIVQADFTRED----IYDHIKEHLEG 118
Cdd:COG1028    5 KGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAA-GGRALAVAADVTDEAaveaLVAAAVAAFGR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEIgiLVNNVGMLPsffPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSAS 197
Cdd:COG1028   84 LDI--LVNNAGITP---PGPLEELTEEDwDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAAS 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 153792573 198 KAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:COG1028  159 KAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTR 194
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 47-233 2.40e-44

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: 150.90  E-value: 2.40e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERttGSCVKIVQADFTRED----IYDHIKEHLEGleIG 122
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEAL--GGNAVAVQADVSDEEdveaLVEEALEEFGR--LD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ILVNNVGMLPSFFPSHFlsTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVY 202
Cdd:cd05233   77 ILVNNAGIARPGPLEEL--TDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALE 154

                        170       180       190
                 ....*....|....*....|....*....|.
gi 153792573 203 TFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:cd05233  155 GLTRSLALELAPYGIRVNAVAPGLVDTPMLA 185
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 44-232 2.57e-42

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: 145.71  E-value: 2.57e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIerttGSCVKIVQADFTRED----IYDHIKEHLEGL 119
Cdd:COG4221    5 GKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAEL----GGRALAVPLDVTDEAaveaAVAAAVAEFGRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIgiLVNNVGMLPsffPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASK 198
Cdd:COG4221   81 DV--LVNNAGVAL---LGPLEELDPEDwDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATK 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:COG4221  156 AAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFL 189
PRK07454 PRK07454
SDR family oxidoreductase;
38-231 2.20e-38

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 135.47  E-value: 2.20e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  38 SFLRSMgQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTR-EDIYDHIKEHL 116
Cdd:PRK07454   1 MSLNSM-PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAEL-RSTGVKAAAYSIDLSNpEAIAPGIAELL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 117 E-GLEIGILVNNVGMLpsfFPSHFLSTS-GESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLY 194
Cdd:PRK07454  79 EqFGCPDVLINNAGMA---YTGPLLEMPlSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAY 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK07454 156 CVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPL 192
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 44-252 1.60e-37

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 133.28  E-value: 1.60e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTtGSCVKIVQADFTREDIYDHIKEHLEGL--EI 121
Cdd:PRK07666   7 GKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAY-GVKVVIATADVSDYEEVTAAIEQLKNElgSI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMlpSFFPSHFLSTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:PRK07666  86 DILINNAGI--SKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFGV 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153792573 202 YTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLN------NKMTKTAD--EFVKESLK 252
Cdd:PRK07666 164 LGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGltdgnpDKVMQPEDlaEFIVAQLK 222
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 44-257 6.06e-35

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: 127.00  E-value: 6.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTREDIYDHI-KEHLEGL-EI 121
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASEL-RAGGAGVLAVVADLTDPEDIDRLvEKAGDAFgRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMLPsffPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAF 200
Cdd:cd05344   80 DILVNNAGGPP---PGPFAELTDEDwLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAG 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792573 201 VYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTK----TADEFVKESLKYVTIG 257
Cdd:cd05344  157 LIGLVKTLSRELAPDGVTVNSVLPGYIDTERVRRLLEARAEkegiSVEEAEKEVASQIPLG 217
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
43-243 3.81e-34

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 124.50  E-value: 3.81e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVkIVQADFTRED----IYDHIKEHLEG 118
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEAR-VLVFDVSDEAavraLIEAAVEAFGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEIgiLVNNVGMLPsFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASK 198
Cdd:PRK05653  83 LDI--LVNNAGITR-DALLPRMSEE-DWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAK 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTKTA 243
Cdd:PRK05653 159 AGVIGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEI 203
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 41-237 1.84e-32

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 120.33  E-value: 1.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  41 RSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRT-LEKLQTIAEEIERTTGSCVkIVQADFTRED----IYDHIKEH 115
Cdd:PRK05565   2 KLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDInEEAAQELLEEIKEEGGDAI-AVKADVSSEEdvenLVEQIVEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 116 LEGLEigILVNNVGMlpSFFPSHFLSTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYS 195
Cdd:PRK05565  81 FGKID--ILVNNAGI--SNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYS 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 153792573 196 ASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNN 237
Cdd:PRK05565 157 ASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSE 198
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 47-239 1.54e-30

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: 114.95  E-value: 1.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERtTGSCVKIVQADFT-REDIYDHIKEHLEGL-EIGIL 124
Cdd:cd05333    3 ALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKA-LGGNAAALEADVSdREAVEALVEKVEAEFgPVDIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 VNNVG-----MLPSFFPSHFlstsgesQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:cd05333   82 VNNAGitrdnLLMRMSEEDW-------DAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKM 239
Cdd:cd05333  155 GVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKV 194
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 44-245 4.71e-30

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


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 113.79  E-value: 4.71e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIErTTGSCVKIVQADFTREDIYDHI----KEHLEGL 119
Cdd:cd08934    3 GKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELE-AEGGKALVLELDVTDEQQVDAAvertVEALGRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIgiLVNNVG-MLpsFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASK 198
Cdd:cd08934   82 DI--LVNNAGiML--LGPVEDADTT-DWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATK 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTKTADE 245
Cdd:cd08934  157 FGVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTITKEAYE 203
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 48-294 5.99e-30

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: 113.84  E-value: 5.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTR-EDIYDHIKEHLEGL-EIGILV 125
Cdd:cd05332    7 IITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVPLDMSDlEDAEQVVEEALKLFgGLDILI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 126 NNVGMlpsFFPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYTF 204
Cdd:cd05332   87 NNAGI---SMRSLFHDTSIDVdRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHALQGF 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 205 SKALSVEYRDKGIIIQVLTPYSISTPMT-KYLNNKMTKTADEFVKESLKYvtiGAESCgclAHEIIAIILNRIPSrIFYS 283
Cdd:cd05332  164 FDSLRAELSEPNISVTVVCPGLIDTNIAmNALSGDGSMSAKMDDTTANGM---SPEEC---ALEILKAIALRKRE-VFYA 236

                        250
                 ....*....|.
gi 153792573 284 StaQRFLLTRY 294
Cdd:cd05332  237 R--QVPLLAVY 245
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 47-217 2.55e-29

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: 111.99  E-value: 2.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTREDiydHIKEHLEGL-----EI 121
Cdd:cd05346    3 VLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVKVLPLQLDVSDRE---SIEAALENLpeefrDI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMLPSFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:cd05346   80 DILVNNAGLALGLDPAQEADLE-DWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAV 158

                        170
                 ....*....|....*.
gi 153792573 202 YTFSKALSVEYRDKGI 217
Cdd:cd05346  159 RQFSLNLRKDLIGTGI 174
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 44-233 1.19e-28

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: 110.55  E-value: 1.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRT-LEKLQTIAEEIERTTGSCVkIVQADFTRED----IYDHIKEHLEG 118
Cdd:cd05358    3 GKVALVTGASSGIGKAIAIRLATAGANVVVNYRSkEDAAEEVVEEIKAVGGKAI-AVQADVSKEEdvvaLFQSAIKEFGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEIgiLVNNVGMLPSFfPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHM-ESRRKGLILNISSGAALRPWPLYSLYSAS 197
Cdd:cd05358   82 LDI--LVNNAGLQGDA-SSHEMTLE-DWNKVIDVNLTGQFLCAREAIKRFrKSKIKGKIINMSSVHEKIPWPGHVNYAAS 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 153792573 198 KAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:cd05358  158 KGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINA 193
FabG-like PRK07231
SDR family oxidoreductase;
44-233 1.27e-28

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 110.30  E-value: 1.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIErtTGSCVKIVQADFTREDiydHIKEHLE-GLE-- 120
Cdd:PRK07231   5 GKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEIL--AGGRAIAVAADVSDEA---DVEAAVAaALErf 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 --IGILVNNVGMLPSFFPshFLSTS-GESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSAS 197
Cdd:PRK07231  80 gsVDILVNNAGTTHRNGP--LLDVDeAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNAS 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 153792573 198 KAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:PRK07231 158 KGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLE 193
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 44-252 4.73e-28

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


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 108.16  E-value: 4.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIerttgSCVKIVQADFTR-EDIYDHIKEHL-EGLEI 121
Cdd:cd05370    5 GNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKEL-----PNIHTIVLDVGDaESVEALAEALLsEYPNL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMLPSFFPSHFLSTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:cd05370   80 DILINNAGIQRPIDLRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKAAL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153792573 202 YTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTK-----TADEFVKESLK 252
Cdd:cd05370  160 HSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGGtprkmPLDEFVDEVVA 215
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 43-240 4.91e-28

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 108.74  E-value: 4.91e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKL-QTIAEEIERTTGSCVkIVQADFTRED----IYDHIKEHLE 117
Cdd:PRK05557   4 EGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGaEALVAEIGALGGKAL-AVQGDVSDAEsverAVDEAKAEFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 118 GLEIgiLVNNVG---------MLPSFFpshflstsgesQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPW 188
Cdd:PRK05557  83 GVDI--LVNNAGitrdnllmrMKEEDW-----------DRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGN 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153792573 189 PLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMT 240
Cdd:PRK05557 150 PGQANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVK 201
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 48-248 5.72e-28

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: 108.14  E-value: 5.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELAR--HGLNVVLISRTLEKLQTIAEEIerTTGSCVKIVQADFTREDIYDHIKEHL--EGLEIGI 123
Cdd:cd05367    3 ILTGASRGIGRALAEELLKrgSPSVVVLLARSEEPLQELKEEL--RPGLRVTTVKADLSDAAGVEQLLEAIrkLDGERDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 124 LVNNVGMLPSFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESRR-KGLILNISSGAALRPWPLYSLYSASKAFVY 202
Cdd:cd05367   81 LINNAGSLGPVSKIEFIDLD-ELQKYFDLNLTSPVCLTSTLLRAFKKRGlKKTVVNVSSGAAVNPFKGWGLYCSSKAARD 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 153792573 203 TFSKALSVEYRDkgiiIQVLT--PYSISTPMTKYL--NNKMTKTADEFVK 248
Cdd:cd05367  160 MFFRVLAAEEPD----VRVLSyaPGVVDTDMQREIreTSADPETRSRFRS 205
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 43-257 5.81e-28

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 108.42  E-value: 5.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISR-TLEKLQTIAEEIErTTGSCVKIVQADFT-REDIYDHIKEHLEGL- 119
Cdd:PRK12825   5 MGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAVE-ALGRRAQAVQADVTdKAALEAAVAAAVERFg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIGILVNNVGMlpsfFPSHFLS--TSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSAS 197
Cdd:PRK12825  84 RIDILVNNAGI----FEDKPLAdmSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 198 KAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMtkylnnkMTKTADEFVKESLKYVTIG 257
Cdd:PRK12825 160 KAGLVGLTKALARELAEYGITVNMVAPGDIDTDM-------KEATIEEAREAKDAETPLG 212
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 44-231 1.99e-27

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: 106.57  E-value: 1.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIE---RTTGSCVKIVQADFT-REDIYDHIKE-HLEG 118
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEaeaNASGQKVSYISADLSdYEEVEQAFAQaVEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEIGILVNNVGM-LPSFF----PSHFlstsgesQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSL 193
Cdd:cd08939   81 GPPDLVVNCAGIsIPGLFedltAEEF-------ERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSA 153

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 153792573 194 YSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:cd08939  154 YCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTPG 191
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
43-231 5.20e-27

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 106.00  E-value: 5.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTR-EDIYDHIKEHLEGLE- 120
Cdd:PRK12824   1 MKKIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAKDWFEEYGFTEDQVRLKELDVTDtEECAEALAEIEEEEGp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 IGILVNNVGMLPSffpSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:PRK12824  81 VDILVNNAGITRD---SVFKRMSHQEwNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKA 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK12824 158 GMIGFTKALASEGARYGITVNCIAPGYIATPM 189
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 44-250 9.69e-27

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: 105.05  E-value: 9.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVL-ISRTLEKLQTIAEEIERTTGSCVkIVQADFTRED----IYDHIKEHLEG 118
Cdd:cd05362    3 GKVALVTGASRGIGRAIAKRLARDGASVVVnYASSKAAAEEVVAEIEAAGGKAI-AVQADVSDPSqvarLFDAAEKAFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEIgiLVNNVGMLPSffpSHFLSTSGESQNLIH-CNITSVVKMTQLVLKHMesRRKGLILNISSGAALRPWPLYSLYSAS 197
Cdd:cd05362   82 VDI--LVNNAGVMLK---KPIAETSEEEFDRMFtVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPNYGAYAGS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153792573 198 KAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMtkYLNNKMTKTADEFVKES 250
Cdd:cd05362  155 KAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDM--FYAGKTEEAVEGYAKMS 205
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 44-233 5.53e-26

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: 103.21  E-value: 5.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTtGSCVKIVQADFTREDIYDHIKEHL--EGLEI 121
Cdd:cd05347    5 GKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKE-GVEATAFTCDVSDEEAIKAAVEAIeeDFGKI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMlpSFFPSHFLSTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:cd05347   84 DILVNNAGI--IRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGV 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 153792573 202 YTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:cd05347  162 AGLTKALATEWARHGIQVNAIAPGYFATEMTE 193
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 47-281 6.69e-26

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: 103.08  E-value: 6.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEiertTGSCVKIVQADFTRED-IYDHIKEHLE-GLEIGIL 124
Cdd:cd05374    3 VLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGEL----LNDNLEVLELDVTDEEsIKAAVKEVIErFGRIDVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 VNNVGMlPSFFPshFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYT 203
Cdd:cd05374   79 VNNAGY-GLFGP--LEETSIEEvRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 204 FSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTKT--------ADEFVKESLKYVTIGAESCGCLAHEIIAIILNR 275
Cdd:cd05374  156 LSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGSALEDpeispyapERKEIKENAAGVGSNPGDPEKVADVIVKALTSE 235


                 ....*..
gi 153792573 276 -IPSRIF 281
Cdd:cd05374  236 sPPLRYF 242
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 47-234 9.58e-26

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: 102.41  E-value: 9.58e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGScVKIVQADFTREDI----YDHIKEHLEGLEIG 122
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPS-VEVEILDVTDEERnqlvIAELEAELGGLDLV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ILVNNVGMlpsffPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:cd05350   80 IINAGVGK-----GTSLGDLSFKAfRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAAL 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 153792573 202 YTFSKALSVEYRDKGIIIQVLTPYSISTPMTKY 234
Cdd:cd05350  155 SSLAESLRYDVKKRGIRVTVINPGFIDTPLTAN 187
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 49-252 1.39e-25

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: 102.16  E-value: 1.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  49 ITGAGDGIGkaysFELAR--HGL-NVVLIS-RTLEKLQTIAEEIERttgscVKIVQADFTREDI----YDHIKEHLEGLe 120
Cdd:COG3967   10 ITGGTSGIG----LALAKrlHARgNTVIITgRREEKLEEAAAANPG-----LHTIVLDVADPASiaalAEQVTAEFPDL- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 iGILVNNVGMLPsffPSHFLSTSGESQNL---IHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSAS 197
Cdd:COG3967   80 -NVLINNAGIMR---AEDLLDEAEDLADAereITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSAT 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153792573 198 KAFVYTFSKALSVEYRDKGI-IIQVLTPYsISTPMTKYLN---NKMtkTADEFVKESLK 252
Cdd:COG3967  156 KAALHSYTQSLRHQLKDTSVkVIELAPPA-VDTDLTGGQGgdpRAM--PLDEFADEVMA 211
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 47-249 1.43e-25

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: 101.99  E-value: 1.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTlEKLQTIAEEIERTTGSCVKIVQADFTR----EDIYDHIKEHLEGLEIg 122
Cdd:cd05323    3 AIITGGASGIGLATAKLLLKKGAKVAILDRN-ENPGAAAELQAINPKVKATFVQCDVTSweqlAAAFKKAIEKFGRVDI- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 iLVNNVGMLPSffPSHFLSTSGESQN--LIHCNITSVVKMTQLVLKHM---ESRRKGLILNISSGAALRPWPLYSLYSAS 197
Cdd:cd05323   81 -LINNAGILDE--KSYLFAGKLPPPWekTIDVNLTGVINTTYLALHYMdknKGGKGGVIVNIGSVAGLYPAPQFPVYSAS 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153792573 198 KAFVYTFSKALSVEYRDK-GIIIQVLTPYSISTPMtkyLNNKMTKTADEFVKE 249
Cdd:cd05323  158 KHGVVGFTRSLADLLEYKtGVRVNAICPGFTNTPL---LPDLVAKEAEMLPSA 207
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 55-237 1.62e-25

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: 101.35  E-value: 1.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573   55 GIGKAYSFELARHGLNVVLISRTlEKLQTIAEEIERTTGScvKIVQADFTRED----IYDHIKEHLEGLEIgiLVNNVGM 130
Cdd:pfam13561   7 GIGWAIARALAEEGAEVVLTDLN-EALAKRVEELAEELGA--AVLPCDVTDEEqveaLVAAAVEKFGRLDI--LVNNAGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  131 LPSFFpSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMesRRKGLILNISSGAALRPWPLYSLYSASKAFVYTFSKALS 209
Cdd:pfam13561  82 APKLK-GPFLDTSREDfDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLA 158

                         170       180
                  ....*....|....*....|....*...
gi 153792573  210 VEYRDKGIIIQVLTPYSISTPMTKYLNN 237
Cdd:pfam13561 159 VELGPRGIRVNAISPGPIKTLAASGIPG 186
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 44-231 2.07e-25

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 102.11  E-value: 2.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEK-LQTIAEEIERTTGSCVkIVQADFTRED----IYDHIKEHLEG 118
Cdd:PRK08936   7 GKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEeANDVAEEIKKAGGEAI-AVKGDVTVESdvvnLIQTAVKEFGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEIgiLVNNVGM-LPSffPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHM-ESRRKGLILNISSGAALRPWPLYSLYSA 196
Cdd:PRK08936  86 LDV--MINNAGIeNAV--PSHEMSLE-DWNKVINTNLTGAFLGSREAIKYFvEHDIKGNIINMSSVHEQIPWPLFVHYAA 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 197 SKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK08936 161 SKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPI 195
PRK12826 PRK12826
SDR family oxidoreductase;
43-233 3.08e-25

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 101.15  E-value: 3.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGScVKIVQADFT-REDIYDHIKEHLEGL-E 120
Cdd:PRK12826   5 EGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGK-ARARQVDVRdRAALKAAVAAGVEDFgR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 IGILVNNVGMLPsffPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALR-PWPLYSLYSASK 198
Cdd:PRK12826  84 LDILVANAGIFP---LTPFAEMDDEQwERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRvGYPGLAHYAASK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:PRK12826 161 AGLVGFTRALALELAARNITVNSVHPGGVDTPMAG 195
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 47-237 8.05e-25

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: 99.73  E-value: 8.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISR-TLEKLQTIAEEIERTTGSCVkIVQADFTR----EDIYDHIKEHLEGLEI 121
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVINYRkSKDAAAEVAAEIEELGGKAV-VVRADVSQpqdvEEMFAAVKERFGRLDV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 giLVNNVGmlPSFF-------PSHF-LSTSGESQNLIHCnitsvvkmTQLVLKHMESRRKGLILNISSGAALRPWPLYSL 193
Cdd:cd05359   80 --LVSNAA--AGAFrplseltPAHWdAKMNTNLKALVHC--------AQQAAKLMRERGGGRIVAISSLGSIRALPNYLA 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 153792573 194 YSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNN 237
Cdd:cd05359  148 VGTAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDALAHFPN 191
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 47-232 8.51e-25

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: 100.01  E-value: 8.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFT-REDIY---DHIKEhlEGLEIG 122
Cdd:cd05339    2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNV-RKAGGKVHYYKCDVSkREEVYeaaKKIKK--EVGDVT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ILVNNVGMLPSFfpsHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:cd05339   79 ILINNAGVVSGK---KLLELPDEEiEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAA 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 153792573 202 YTFSKALSVE---YRDKGIIIQVLTPYSISTPMT 232
Cdd:cd05339  156 VGFHESLRLElkaYGKPGIKTTLVCPYFINTGMF 189
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 47-249 1.03e-24

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 99.80  E-value: 1.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVL-ISRTLEKLQTIAEEIERTTGSCVkIVQADF-TREDIYDHIKEHLEGL-EIGI 123
Cdd:PRK06077   9 VVVTGSGRGIGRAIAVRLAKEGSLVVVnAKKRAEEMNETLKMVKENGGEGI-GVLADVsTREGCETLAKATIDRYgVADI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 124 LVNNVGmLPSFFPshFLSTSGE-SQNLIHCNITSVVKMTQLVLKHMesRRKGLILNISSGAALRPWPLYSLYSASKAFVY 202
Cdd:PRK06077  88 LVNNAG-LGLFSP--FLNVDDKlIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSIYGAMKAAVI 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153792573 203 TFSKALSVEYRDKgIIIQVLTPYSISTPMTKYLNNKMTKTADEFVKE 249
Cdd:PRK06077 163 NLTKYLALELAPK-IRVNAIAPGFVKTKLGESLFKVLGMSEKEFAEK 208
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 41-240 1.55e-24

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: 99.39  E-value: 1.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  41 RSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIerttGSCVKIVQADFTREDIYDHIKEHL--EG 118
Cdd:cd05345    2 RLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADI----GEAAIAIQADVTKRADVEAMVEAAlsKF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEIGILVNNVGMlpSFFPSHFLSTSGESQNLI-HCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSAS 197
Cdd:cd05345   78 GRLDILVNNAGI--THRNKPMLEVDEEEFDRVfAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNAS 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 153792573 198 KAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMT 240
Cdd:cd05345  156 KGWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFMGEDT 198
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 47-233 1.76e-24

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: 99.41  E-value: 1.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKI--VQADFTREDIYDHI-KEHLEGL-EIG 122
Cdd:cd05364    6 AIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSEKKIllVVADLTEEEGQDRIiSTTLAKFgRLD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ILVNNVGMLpsfFPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMeSRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:cd05364   86 ILVNNAGIL---AKGGGEDQDIEEyDKVMNLNLRAVIYLTKLAVPHL-IKTKGEIVNVSSVAGGRSFPGVLYYCISKAAL 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 153792573 202 YTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:cd05364  162 DQFTRCTALELAPKGVRVNSVSPGVIVTGFHR 193
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 44-229 4.74e-24

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: 98.04  E-value: 4.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADfTR--EDIYDHIKEHLEGL-E 120
Cdd:cd05369    3 GKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGRAHPIQCD-VRdpEAVEAAVDETLKEFgK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 IGILVNNVGmlpsffpSHFLS-TSGESQN----LIHCNITSVVKMTQLVLKH-MESRRKGLILNISSGAALRPWPLYSLY 194
Cdd:cd05369   82 IDILINNAA-------GNFLApAESLSPNgfktVIDIDLNGTFNTTKAVGKRlIEAKHGGSILNISATYAYTGSPFQVHS 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGIIIQVLTPYSIST 229
Cdd:cd05369  155 AAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPT 189
PRK09072 PRK09072
SDR family oxidoreductase;
48-231 1.48e-23

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 96.93  E-value: 1.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIerTTGSCVKIVQADFTREDIYDHIKEH-LEGLEIGILVN 126
Cdd:PRK09072   9 LLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARL--PYPGRHRWVVADLTSEAGREAVLARaREMGGINVLIN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 127 NVGMlpsffpSHF--LSTSGESQ--NLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVY 202
Cdd:PRK09072  87 NAGV------NHFalLEDQDPEAieRLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFALR 160

                        170       180
                 ....*....|....*....|....*....
gi 153792573 203 TFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK09072 161 GFSEALRRELADTGVRVLYLAPRATRTAM 189
PRK09242 PRK09242
SDR family oxidoreductase;
44-237 1.68e-23

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 96.74  E-value: 1.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTI-----AEEIERTTGSCVKIVQADFTREDIYDHIKEHLEG 118
Cdd:PRK09242   9 GQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQArdelaEEFPEREVHGLAADVSDDEDRRAILDWVEDHWDG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEigILVNNVGMLPSFFPSHFlsTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASK 198
Cdd:PRK09242  89 LH--ILVNNAGGNIRKAAIDY--TEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTK 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK-YLNN 237
Cdd:PRK09242 165 AALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSgPLSD 204
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 44-232 4.49e-23

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: 95.14  E-value: 4.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIerttGSCVKIVQADFTRED----IYDHIKEHLEGL 119
Cdd:cd05341    5 GKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAEL----GDAARFFHLDVTDEDgwtaVVDTAREAFGRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIgiLVNNVGMLPSFFPSHflSTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:cd05341   81 DV--LVNNAGILTGGTVET--TTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKG 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLT--PYSISTPMT 232
Cdd:cd05341  157 AVRGLTKSAALECATQGYGIRVNSvhPGYIYTPMT 191
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 45-241 1.06e-22

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: 93.99  E-value: 1.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  45 QWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVkIVQADFTREDIYDHIKEHLE---GlEI 121
Cdd:cd05360    1 QVVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAI-AVVADVADAAQVERAADTAVerfG-RI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMlpSFFpSHFLSTS-GESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAF 200
Cdd:cd05360   79 DTWVNNAGV--AVF-GRFEDVTpEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 153792573 201 VYTFSKALSVEYRDKG--IIIQVLTPYSISTPMTKYLNNKMTK 241
Cdd:cd05360  156 VRGFTESLRAELAHDGapISVTLVQPTAMNTPFFGHARSYMGK 198
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 44-243 1.20e-22

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


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 94.12  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTRED----IYDHIKEHLEGl 119
Cdd:cd05343    6 GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLFPYQCDLSNEEqilsMFSAIRTQHQG- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 eIGILVNNVGMLpsfFPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRR--KGLILNISS--GAALRPWPLYSLY 194
Cdd:cd05343   85 -VDVCINNAGLA---RPEPLLSGKTEGwKEMFDVNVLALSICTREAYQSMKERNvdDGHIININSmsGHRVPPVSVFHFY 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGIIIQV--LTPYSISTP-MTKYLNNKMTKTA 243
Cdd:cd05343  161 AATKHAVTALTEGLRQELREAKTHIRAtsISPGLVETEfAFKLHDNDPEKAA 212
PRK07201 PRK07201
SDR family oxidoreductase;
48-245 1.29e-22

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 97.71  E-value: 1.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTREDIYDHIKEHLEGlEIG---IL 124
Cdd:PRK07201 375 LITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEI-RAKGGTAHAYTCDLTDSAAVDHTVKDILA-EHGhvdYL 452

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 VNNVGMlpSFFPSHFLST--SGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVY 202
Cdd:PRK07201 453 VNNAGR--SIRRSVENSTdrFHDYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSIGVQTNAPRFSAYVASKAALD 530

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 153792573 203 TFSKALSVEYRDKGIIIQVLTPYSISTPM---TKYLNNKMTKTADE 245
Cdd:PRK07201 531 AFSDVAASETLSDGITFTTIHMPLVRTPMiapTKRYNNVPTISPEE 576
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 47-255 2.45e-22

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: 93.13  E-value: 2.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLN-VVLISR---TLEKLQTIAEEIERttgscVKIVQADFTRE--DIYDHIKEHLEGLE 120
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGNNtVIATCRdpsAATELAALGASHSR-----LHILELDVTDEiaESAEAVAERLGDAG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 IGILVNNVGMLPSFfpSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAA----LRPWPLYSlYS 195
Cdd:cd05325   76 LDVLINNAGILHSY--GPASEVDSEDlLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGsigdNTSGGWYS-YR 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792573 196 ASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKY-LNNKMTKTADEFVKESLKYVT 255
Cdd:cd05325  153 ASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPfAKNKGPITPEESVAGLLKVID 213
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 44-231 3.65e-22

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: 92.53  E-value: 3.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQtiaeEIERTTGscVKIVQADFT-REDIYDHIKEhlEGlEIG 122
Cdd:cd05368    2 GKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLK----ELERGPG--ITTRVLDVTdKEQVAALAKE--EG-RID 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ILVNNVGMLPSffpSHFLSTSGESQNL-IHCNITSVVKMTQLVLKHMESRRKGLILNISSGAA-LRPWPLYSLYSASKAF 200
Cdd:cd05368   73 VLFNCAGFVHH---GSILDCEDDDWDFaMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASsIKGVPNRFVYSTTKAA 149

                        170       180       190
                 ....*....|....*....|....*....|.
gi 153792573 201 VYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:cd05368  150 VIGLTKSVAADFAQQGIRCNAICPGTVDTPS 180
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 44-238 1.16e-21

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 91.52  E-value: 1.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIerttGSCVKIVQADFTRED----IYDHIKEHLEGL 119
Cdd:PRK12936   6 GRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAEL----GERVKIFPANLSDRDevkaLGQKAEADLEGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIgiLVNNVGMLPSFFpshFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASK 198
Cdd:PRK12936  82 DI--LVNNAGITKDGL---FVRMSDEDwDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASK 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNK 238
Cdd:PRK12936 157 AGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDK 196
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 44-241 1.94e-21

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: 90.85  E-value: 1.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTREDIYDH----IKEHLEgl 119
Cdd:cd05352    8 GKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKtfkqIQKDFG-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIGILVNNVGMlpSFFPSHFLSTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRP-WPL-YSLYSAS 197
Cdd:cd05352   86 KIDILIANAGI--TVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVnRPQpQAAYNAS 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 153792573 198 KAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTK 241
Cdd:cd05352  164 KAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRK 207
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 47-231 3.22e-21

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 90.73  E-value: 3.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEeierttgscVKIVQADFTRED-----IYDHIKEhlEGlEI 121
Cdd:PRK06179   7 ALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIPG---------VELLELDVTDDAsvqaaVDEVIAR--AG-RI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMlpSFFPSHFLSTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:PRK06179  75 DVLVNNAGV--GLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHAV 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 153792573 202 YTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK06179 153 EGYSESLDHEVRQFGIRVSLVEPAYTKTNF 182
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 43-257 3.22e-21

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 90.50  E-value: 3.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIErttGSCVKIVQADFTR----EDIYDHIKEHLEG 118
Cdd:PRK12829  10 DGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLP---GAKVTATVADVADpaqvERVFDTAVERFGG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEIgiLVNNVGMlpsFFPSHFLS--TSGESQNLIHCNITSVVKMTQLVLKHM-ESRRKGLILNISSGAALRPWPLYSLYS 195
Cdd:PRK12829  87 LDV--LVNNAGI---AGPTGGIDeiTPEQWEQTLAVNLNGQFYFARAAVPLLkASGHGGVIIALSSVAGRLGYPGRTPYA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792573 196 ASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYL----NNKMTKTADEFVKESLKYVTIG 257
Cdd:PRK12829 162 ASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRViearAQQLGIGLDEMEQEYLEKISLG 227
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 48-232 6.29e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 90.00  E-value: 6.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVkivqaDFTREDIYDHIKEHLEGL--EIGILV 125
Cdd:PRK07825   9 AITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGLVVGGPL-----DVTDPASFAAFLDAVEADlgPIDVLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 126 NNVGMLPSffpSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYTF 204
Cdd:PRK07825  84 NNAGVMPV---GPFLDEPDAVtRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKHAVVGF 160

                        170       180
                 ....*....|....*....|....*...
gi 153792573 205 SKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:PRK07825 161 TDAARLELRGTGVHVSVVLPSFVNTELI 188
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 44-233 6.93e-21

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: 89.43  E-value: 6.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFT----REDIYDHIKEHLEGl 119
Cdd:cd05329    6 GKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEW-REKGFKVEGSVCDVSsrseRQELMDTVASHFGG- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIGILVNNVGMLPSFFPSHFlsTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:cd05329   84 KLNILVNNAGTNIRKEAKDY--TEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKG 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:cd05329  162 ALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVE 195
PRK06181 PRK06181
SDR family oxidoreductase;
44-224 8.24e-21

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 89.65  E-value: 8.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTRED----IYDHIKEHLEGL 119
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQEL-ADHGGEALVVPTDVSDAEacerLIEAAVARFGGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EigILVNNVGMLPSffpSHFLSTSGES--QNLIHCNITSVVKMTQLVLKHMESRRkGLILNISSGAALRPWPLYSLYSAS 197
Cdd:PRK06181  80 D--ILVNNAGITMW---SRFDELTDLSvfERVMRVNYLGAVYCTHAALPHLKASR-GQIVVVSSLAGLTGVPTRSGYAAS 153

                        170       180
                 ....*....|....*....|....*..
gi 153792573 198 KAFVYTFSKALSVEYRDKGIIIQVLTP 224
Cdd:PRK06181 154 KHALHGFFDSLRIELADDGVAVTVVCP 180
PRK07774 PRK07774
SDR family oxidoreductase;
47-252 9.11e-21

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 89.03  E-value: 9.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKiVQADFTRED----IYDHIKEHLEGLEig 122
Cdd:PRK07774   9 AIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIA-VQVDVSDPDsakaMADATVSAFGGID-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ILVNN----VGMLPSffpshFLSTS--GESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAAlrpWPLYSLYSA 196
Cdd:PRK07774  86 YLVNNaaiyGGMKLD-----LLITVpwDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAA---WLYSNFYGL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153792573 197 SKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKylnnkmTKTADEFVKESLK 252
Cdd:PRK07774 158 AKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATR------TVTPKEFVADMVK 207
PRK06949 PRK06949
SDR family oxidoreductase;
44-235 1.76e-20

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 88.67  E-value: 1.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGScVKIVQADFTRediYDHIKEHLEGLE--- 120
Cdd:PRK06949   9 GKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGA-AHVVSLDVTD---YQSIKAAVAHAEtea 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 --IGILVNNVGmlpsffpshfLSTSGESQN--------LIHCNITSVVKMTQLVLKHMESRRKGL--------ILNISSG 182
Cdd:PRK06949  85 gtIDILVNNSG----------VSTTQKLVDvtpadfdfVFDTNTRGAFFVAQEVAKRMIARAKGAgntkpggrIINIASV 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153792573 183 AALRPWPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYL 235
Cdd:PRK06949 155 AGLRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHH 207
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 44-211 2.37e-20

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 89.60  E-value: 2.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVqADFTRED----IYDHIKEHLEGL 119
Cdd:PRK07109   8 RQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVV-ADVADAEavqaAADRAEEELGPI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIGIlvnNVGMLPSFfpSHFLSTS-GESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASK 198
Cdd:PRK07109  87 DTWV---NNAMVTVF--GPFEDVTpEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAK 161

                        170
                 ....*....|...
gi 153792573 199 AFVYTFSKALSVE 211
Cdd:PRK07109 162 HAIRGFTDSLRCE 174
PRK05855 PRK05855
SDR family oxidoreductase;
44-233 3.05e-20

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 90.81  E-value: 3.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGscvkivQADFTREDIYDHikEHLEGL---- 119
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGA------VAHAYRVDVSDA--DAMEAFaewv 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 --EIG---ILVNN--VGMLPSffpshFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRK-GLILNISSGAALRPWPL 190
Cdd:PRK05855 387 raEHGvpdIVVNNagIGMAGG-----FLDTSAEDwDRVLDVNLWGVIHGCRLFGRQMVERGTgGHIVNVASAAAYAPSRS 461

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 153792573 191 YSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:PRK05855 462 LPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVA 504
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 43-244 3.24e-20

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: 87.82  E-value: 3.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAE-EIERTTGSCVKIVqADFT-REDIYDHIKEHLEGL- 119
Cdd:cd05366    1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIqEISEAGYNAVAVG-ADVTdKDDVEALIDQAVEKFg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIGILVNNVGMLPSffpSHFLS-TSGESQNLIHCNITSVVKMTQLVLKHM-ESRRKGLILNISSGAALRPWPLYSLYSAS 197
Cdd:cd05366   80 SFDVMVNNAGIAPI---TPLLTiTEEDLKKVYAVNVFGVLFGIQAAARQFkKLGHGGKIINASSIAGVQGFPNLGAYSAS 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153792573 198 KAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTKTAD 244
Cdd:cd05366  157 KFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVGEIAG 203
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 44-255 3.43e-20

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: 87.45  E-value: 3.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEK---------LQTI---AEEIERTTGSCVKIvQADFTRED-IYD 110
Cdd:cd05338    3 GKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEgdngsakslPGTIeetAEEIEAAGGQALPI-VVDVRDEDqVRA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 111 HIKEHLEGL-EIGILVNNVGMLpsfFPSHFLSTSGESQNLI---HCNITSVVkmTQLVLKHMESRRKGLILNISSGAALR 186
Cdd:cd05338   82 LVEATVDQFgRLDILVNNAGAI---WLSLVEDTPAKRFDLMqrvNLRGTYLL--SQAALPHMVKAGQGHILNISPPLSLR 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 187 PWPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTP-YSISTPMTkylnNKMTKTADEFVKESLKYVT 255
Cdd:cd05338  157 PARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPsTAIETPAA----TELSGGSDPARARSPEILS 222
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
41-231 4.09e-20

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 87.39  E-value: 4.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  41 RSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIerttGSCVKIVQADFTREDIYDHIKEHLEGL- 119
Cdd:PRK07067   3 RLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEI----GPAAIAVSLDVTRQDSIDRIVAAAVERf 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 -EIGILVNNVGMlpsFFPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHM-ESRRKGLILNISSGAALRPWPLYSLYSA 196
Cdd:PRK07067  79 gGIDILFNNAAL---FDMAPILDISRDSyDRLFAVNVKGLFFLMQAVARHMvEQGRGGKIINMASQAGRRGEALVSHYCA 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 153792573 197 SKAFV--YTFSKALS-VEYrdkGIIIQVLTPYSISTPM 231
Cdd:PRK07067 156 TKAAVisYTQSAALAlIRH---GINVNAIAPGVVDTPM 190
PRK05866 PRK05866
SDR family oxidoreductase;
44-245 4.29e-20

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 88.26  E-value: 4.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGScVKIVQADFTREDIYDHIKEHLEGlEIG- 122
Cdd:PRK05866  40 GKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGD-AMAVPCDLSDLDAVDALVADVEK-RIGg 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 --ILVNNVGmlpsffpSHFLSTSGESQNLIH-------CNITSVVKMTQLVLKHMESRRKGLILNISS-GAALRPWPLYS 192
Cdd:PRK05866 118 vdILINNAG-------RSIRRPLAESLDRWHdvertmvLNYYAPLRLIRGLAPGMLERGDGHIINVATwGVLSEASPLFS 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 153792573 193 LYSASKAFVYTFSKALSVEYRDKGiiIQVLTPYS--ISTPM---TKYLNNKMTKTADE 245
Cdd:PRK05866 191 VYNASKAALSAVSRVIETEWGDRG--VHSTTLYYplVATPMiapTKAYDGLPALTADE 246
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 44-231 4.73e-20

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: 87.35  E-value: 4.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLI--SRTLEKLQTIAEEIERTTGSCV----KIVQADFTREDIYDHIKEHle 117
Cdd:cd05355   26 GKKALITGGDSGIGRAVAIAFAREGADVAINylPEEEDDAEETKKLIEEEGRKCLlipgDLGDESFCRDLVKEVVKEF-- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 118 GlEIGILVNNVGMlpsFFPSHFLSTSGESQ--NLIHCNITSVVKMTQLVLKHMEsrRKGLILNISSGAALRPWPLYSLYS 195
Cdd:cd05355  104 G-KLDILVNNAAY---QHPQESIEDITTEQleKTFRTNIFSMFYLTKAALPHLK--KGSSIINTTSVTAYKGSPHLLDYA 177

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 153792573 196 ASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:cd05355  178 ATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPL 213
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
38-302 6.45e-20

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 87.10  E-value: 6.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  38 SFLRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRT--LEKLQTIAEEIERTtgscVKIVQADFTR-EDIYDHIKE 114
Cdd:PRK06935   9 DFFSLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGtnWDETRRLIEKEGRK----VTFVQVDLTKpESAEKVVKE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 115 HLEGL-EIGILVNNVGMLPSffpSHFLSTSGESQN-LIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYS 192
Cdd:PRK06935  85 ALEEFgKIDILVNNAGTIRR---APLLEYKDEDWNaVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 193 LYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTKTADefvkeslkyvtigaescgclaheiiaiI 272
Cdd:PRK06935 162 AYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIRADKNRNDE---------------------------I 214

                        250       260       270
                 ....*....|....*....|....*....|....
gi 153792573 273 LNRIPSR----IFYSSTAQRFLLTRYSDYLKRNI 302
Cdd:PRK06935 215 LKRIPAGrwgePDDLMGAAVFLASRASDYVNGHI 248
PRK06484 PRK06484
short chain dehydrogenase; Validated
 47-231 1.19e-19

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 88.75  E-value: 1.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIerttGSCVKIVQADFTREDIYDHIKEHLEGL--EIGIL 124
Cdd:PRK06484   8 VLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSL----GPDHHALAMDVSDEAQIREGFEQLHREfgRIDVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 VNNVGMLPSFfPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGL-ILNISSGAALRPWPLYSLYSASKAFVY 202
Cdd:PRK06484  84 VNNAGVTDPT-MTATLDTTLEEfARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYSASKAAVI 162

                        170       180
                 ....*....|....*....|....*....
gi 153792573 203 TFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK06484 163 SLTRSLACEWAAKGIRVNAVLPGYVRTQM 191
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 44-233 1.65e-19

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: 85.62  E-value: 1.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCvkivQADFTRE----DIYDHIKEHLEGL 119
Cdd:cd08944    3 GKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALAL----RVDVTDEqqvaALFERAVEEFGGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIgiLVNNVGMLPsfFPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASK 198
Cdd:cd08944   79 DL--LVNNAGAMH--LTPAIIDTDLAVwDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASK 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:cd08944  155 AAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLL 189
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 44-233 2.20e-19

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 85.38  E-value: 2.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTtGSCVKIVQADFTRE-DIYDHIKEHLEGL-EI 121
Cdd:PRK08213  12 GKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEAL-GIDALWIAADVADEaDIERLAEETLERFgHV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGmlpsffpshflSTSGES---------QNLIHCNITSVVKMTQLVLKH-MESRRKGLILNISSGAALRPWPLY 191
Cdd:PRK08213  91 DILVNNAG-----------ATWGAPaedhpveawDKVMNLNVRGLFLLSQAVAKRsMIPRGYGRIINVASVAGLGGNPPE 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 153792573 192 SL----YSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:PRK08213 160 VMdtiaYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTR 205
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 44-217 2.34e-19

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 85.72  E-value: 2.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTREDIYDHIKEHLEGL--EI 121
Cdd:PRK08277  10 GKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEI-KAAGGEALAVKADVLDKESLEQARQQILEDfgPC 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVG-------------MLP----SFFPshfLSTSGESQ--NLihcNITSVVKMTQLVLKHMESRRKGLILNISSG 182
Cdd:PRK08277  89 DILINGAGgnhpkattdnefhELIeptkTFFD---LDEEGFEFvfDL---NLLGTLLPTQVFAKDMVGRKGGNIINISSM 162

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 183 AALRPWPLYSLYSASKAFVYTFSKALSVEYRDKGI 217
Cdd:PRK08277 163 NAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGI 197
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 44-231 2.41e-19

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 84.85  E-value: 2.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTL----EKLQTIAEEIERTTGscVKIVQADFTREDIyDHIKEHLEGL 119
Cdd:PRK12828   7 GKVVAITGGFGGLGRATAAWLAARGARVALIGRGAaplsQTLPGVPADALRIGG--IDLVDPQAARRAV-DEVNRQFGRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIgiLVNNVGMlpsfFPSHFL--STSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSAS 197
Cdd:PRK12828  84 DA--LVNIAGA----FVWGTIadGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAA 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 153792573 198 KAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK12828 158 KAGVARLTEALAAELLDRGITVNAVLPSIIDTPP 191
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 43-255 3.57e-19

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: 84.69  E-value: 3.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFT-REDIYDHIKEHLEGL-E 120
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVIALELDITsKESIKELIESYLEKFgR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 IGILVNNVGMLPSFFPSHFLSTSGESQNL-IHCNITSVVKMTQLVLKHMESRRKGLILNISS--GAALRPWPLYS----- 192
Cdd:cd08930   81 IDILINNAYPSPKVWGSRFEEFPYEQWNEvLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASiyGVIAPDFRIYEntqmy 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 193 ---LYSASKAFVYTFSKALSVEYRDKGIIIQVLTP--------------YSISTPMTKYLNNKMTKTADEFVKESL-KYV 254
Cdd:cd08930  161 spvEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPggilnnqpseflekYTKKCPLKRMLNPEDLRGAIIFLLSDAsSYV 240


                 .
gi 153792573 255 T 255
Cdd:cd08930  241 T 241
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 44-248 4.13e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 84.60  E-value: 4.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKI---VQADFTREDIYDHIKEHLEGLE 120
Cdd:PRK07478   6 GKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALagdVRDEAYAKALVALAVERFGGLD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 IGIlvNNVGMLPSFFPSHFLSTSGeSQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISS----GAALrpwPLYSLYSA 196
Cdd:PRK07478  86 IAF--NNAGTLGEMGPVAEMSLEG-WRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTfvghTAGF---PGMAAYAA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 153792573 197 SKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTkylnNKMTKTAD--EFVK 248
Cdd:PRK07478 160 SKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMG----RAMGDTPEalAFVA 209
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 47-245 4.59e-19

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: 83.83  E-value: 4.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLN-VVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFT----REDIYDHIKEHLEGLEi 121
Cdd:cd05324    3 ALVTGANRGIGFEIVRQLAKSGPGtVILTARDVERGQAAVEKL-RAEGLSVRFHQLDVTddasIEAAADFVEEKYGGLD- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 gILVNNVGmlpsFFPSHFLSTSGESQNL---IHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPlyslYSASK 198
Cdd:cd05324   81 -ILVNNAG----IAFKGFDDSTPTREQAretMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLTSA----YGVSK 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYlnnKMTKTADE 245
Cdd:cd05324  152 AALNALTRILAKELKETGIKVNACCPGWVKTDMGGG---KAPKTPEE 195
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 44-235 4.72e-19

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 84.43  E-value: 4.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVqadFtreDIYDH--IKEHLEGLE- 120
Cdd:PRK07523  10 GRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALA---F---DVTDHdaVRAAIDAFEa 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 ----IGILVNNVGM-----LPSFFPSHFlstsgesQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLY 191
Cdd:PRK07523  84 eigpIDILVNNAGMqfrtpLEDFPADAF-------ERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGI 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 153792573 192 SLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYL 235
Cdd:PRK07523 157 APYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAAL 200
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 47-229 5.68e-19

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


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 84.16  E-value: 5.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIvQADFTRE-DIYDHIKEHLEGL-EIGIL 124
Cdd:cd05365    2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGL-ECNVTSEqDLEAVVKATVSQFgGITIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 VNNVG----------MLPSFFPSHFlstsgesqnliHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLY 194
Cdd:cd05365   81 VNNAGgggpkpfdmpMTEEDFEWAF-----------KLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAY 149

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGIIIQVLTPYSIST 229
Cdd:cd05365  150 GSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKT 184
PRK05650 PRK05650
SDR family oxidoreductase;
48-224 5.70e-19

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 84.71  E-value: 5.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTRED----IYDHIKEHLEGleIGI 123
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLL-REAGGDGFYQRCDVRDYSqltaLAQACEEKWGG--IDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 124 LVNNVGMLPSFFpshFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVY 202
Cdd:PRK05650  81 IVNNAGVASGGF---FEELSLEDwDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVV 157

                        170       180
                 ....*....|....*....|..
gi 153792573 203 TFSKALSVEYRDKGIIIQVLTP 224
Cdd:PRK05650 158 ALSETLLVELADDEIGVHVVCP 179
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 40-233 7.29e-19

(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: 83.91  E-value: 7.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  40 LRSMGQWAVITGAGDGIGKAYSFELARHGLNVVL---------ISRTLEKLQTIAEEIERTTGSCV----------KIVQ 100
Cdd:cd05353    1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVndlggdrkgSGKSSSAADKVVDEIKAAGGKAVanydsvedgeKIVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 101 A---DFTREDiydhikehlegleigILVNNVGMLPSffpSHFLSTSGESQNLIH-CNITSVVKMTQLVLKHMESRRKGLI 176
Cdd:cd05353   81 TaidAFGRVD---------------ILVNNAGILRD---RSFAKMSEEDWDLVMrVHLKGSFKVTRAAWPYMRKQKFGRI 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792573 177 LNISSGAAlrpwpLY-----SLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSiSTPMTK 233
Cdd:cd05353  143 INTSSAAG-----LYgnfgqANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPAA-GSRMTE 198
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 44-233 9.33e-19

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: 83.29  E-value: 9.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTREDIYDHIKEHLegleigi 123
Cdd:cd05351    7 GKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPGIEPVCVDLSDWDATEEALGSVGPVDL------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 124 LVNN--VGMLPSF-------FPSHFlstsgesqnliHCNITSVVKMTQLVLKHMESRR-KGLILNISSGAALRPWPLYSL 193
Cdd:cd05351   80 LVNNaaVAILQPFlevtkeaFDRSF-----------DVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHTV 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 153792573 194 YSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:cd05351  149 YCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGR 188
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
44-231 1.13e-18

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 83.70  E-value: 1.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTlEKLQTIAEEIERTTGSCVKiVQADFTREDIYDHIKEHLEGLE--I 121
Cdd:PRK08226   6 GKTALITGALQGIGEGIARVFARHGANLILLDIS-PEIEKLADELCGRGHRCTA-VVADVRDPASVAAAIKRAKEKEgrI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMLPSffpSHFLSTSGESQNL-IHCNITSVVKMTQLVLKHMESRRKGLILNISS-GAALRPWPLYSLYSASKA 199
Cdd:PRK08226  84 DILVNNAGVCRL---GSFLDMSDEDRDFhIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSvTGDMVADPGETAYALTKA 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK08226 161 AIVGLTKSLAVEYAQSGIRVNAICPGYVRTPM 192
PRK07035 PRK07035
SDR family oxidoreductase;
44-224 1.61e-18

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 83.14  E-value: 1.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTREDI---YDHIKEHLEGLE 120
Cdd:PRK07035   8 GKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIdalFAHIRERHGRLD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 igILVNNVGMLPSFfpSHFLSTS-GESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:PRK07035  88 --ILVNNAAANPYF--GHILDTDlGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITKA 163

                        170       180
                 ....*....|....*....|....*
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTP 224
Cdd:PRK07035 164 AVISMTKAFAKECAPFGIRVNALLP 188
PRK06914 PRK06914
SDR family oxidoreductase;
47-262 1.69e-18

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 83.53  E-value: 1.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEI-ERTTGSCVKIVQADFTRE----DIYDHIKEHLEgleI 121
Cdd:PRK06914   6 AIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtQLNLQQNIKVQQLDVTDQnsihNFQLVLKEIGR---I 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMLPSFFPSHFlsTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:PRK06914  83 DLLVNNAGYANGGFVEEI--PVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYAL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792573 202 YTFSKALSVEYRDKGIIIQVLTPYSISTPM-TKYLNNKMTKTAD-----EFVKESLKYVTIGAESCG 262
Cdd:PRK06914 161 EGFSESLRLELKPFGIDVALIEPGSYNTNIwEVGKQLAENQSETtspykEYMKKIQKHINSGSDTFG 227
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 44-262 1.83e-18

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: 82.97  E-value: 1.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKL----QTIAEEIERTTGSCVKIVQADfTREDIYDHIKEHLEGl 119
Cdd:cd08936   10 NKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVdravATLQGEGLSVTGTVCHVGKAE-DRERLVATAVNLHGG- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 eIGILVNNVGMLPsFFPSHFLSTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:cd08936   88 -VDILVSNAAVNP-FFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVSKT 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLnnKMTKTADEFVKESLKYVTIG-AESCG 262
Cdd:cd08936  166 ALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSAL--WMDKAVEESMKETLRIRRLGqPEDCA 227
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
45-231 2.74e-18

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 82.42  E-value: 2.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  45 QWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEK-LQTIAEEiertTGSCVKIVQADFTR--------EDIYDHIKEH 115
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKeLTKLAEQ----YNSNLTFHSLDLQDvheletnfNEILSSIQED 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 116 LEGleiGI-LVNNVGMLPSFFPSHflstSGESQNLI---HCNITSVVKMTQLVLKHMESRR-KGLILNISSGAALRPWPL 190
Cdd:PRK06924  78 NVS---SIhLINNAGMVAPIKPIE----KAESEELItnvHLNLLAPMILTSTFMKHTKDWKvDKRVINISSGAAKNPYFG 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 153792573 191 YSLYSASKAFVYTFSKALSVEYRDKGIIIQVLT--PYSISTPM 231
Cdd:PRK06924 151 WSAYCSSKAGLDMFTQTVATEQEEEEYPVKIVAfsPGVMDTNM 193
PRK07814 PRK07814
SDR family oxidoreductase;
41-229 2.89e-18

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 82.52  E-value: 2.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  41 RSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTRED----IYDHIKEHL 116
Cdd:PRK07814   7 RLDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQI-RAAGRRAHVVAADLAHPEatagLAGQAVEAF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 117 EGLEigILVNNVGmlpSFFPSHFLSTSgeSQNLIHC---NITSVVKMTQLVLKHM-ESRRKGLILNISSGAALRPWPLYS 192
Cdd:PRK07814  86 GRLD--IVVNNVG---GTMPNPLLSTS--TKDLADAftfNVATAHALTVAAVPLMlEHSGGGSVINISSTMGRLAGRGFA 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 153792573 193 LYSASKAFV--YTFSKALSVEYRdkgIIIQVLTPYSIST 229
Cdd:PRK07814 159 AYGTAKAALahYTRLAALDLCPR---IRVNAIAPGSILT 194
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 43-233 4.67e-18

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: 81.72  E-value: 4.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLIS-RTLEKLQTIAEEIERTTGSCVKIVQADFTR----EDIYDHIKEHLE 117
Cdd:cd08940    1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGfGDAAEIEAVRAGLAAKHGVKVLYHGADLSKpaaiEDMVAYAQRQFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 118 GLEIgiLVNNVGM----LPSFFPShflstsgESQN-LIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYS 192
Cdd:cd08940   81 GVDI--LVNNAGIqhvaPIEDFPT-------EKWDaIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKS 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 153792573 193 LYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:cd08940  152 AYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVE 192
PRK07063 PRK07063
SDR family oxidoreductase;
41-232 5.28e-18

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 81.64  E-value: 5.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  41 RSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIER-TTGSCVKIVQADFTREDIYDHIKEHLEGl 119
Cdd:PRK07063   4 RLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARdVAGARVLAVPADVTDAASVAAAVAAAEE- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIG---ILVNNVGMlpSFFPSHFLSTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSA 196
Cdd:PRK07063  83 AFGpldVLVNNAGI--NVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPV 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 153792573 197 SKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:PRK07063 161 AKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLT 196
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 48-217 7.29e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 81.16  E-value: 7.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKiVQADFTREDIYDHIKEhlEGLE----IGI 123
Cdd:PRK07890   9 VVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALA-VPTDITDEDQCANLVA--LALErfgrVDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 124 LVNNVGMLPSFFPshFLSTSGES-QNLIHCNITSVVKMTQLVLKHMeSRRKGLILNISSGAALRPWPLYSLYSASKAFVY 202
Cdd:PRK07890  86 LVNNAFRVPSMKP--LADADFAHwRAVIELNVLGTLRLTQAFTPAL-AESGGSIVMINSMVLRHSQPKYGAYKMAKGALL 162

                        170
                 ....*....|....*
gi 153792573 203 TFSKALSVEYRDKGI 217
Cdd:PRK07890 163 AASQSLATELGPQGI 177
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 44-234 1.02e-17

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


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 81.12  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTG-SCVKIVQADF-----TREdIYDHIKEhlE 117
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGnAKVEVIQLDLsslasVRQ-FAEEFLA--R 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 118 GLEIGILVNNVGMlpsFFPSHFLSTSG-ESQnlIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALR---------- 186
Cdd:cd05327   78 FPRLDILINNAGI---MAPPRRLTKDGfELQ--FAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAgpidfndldl 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153792573 187 -PWPLYS---LYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKY 234
Cdd:cd05327  153 eNNKEYSpykAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRR 204
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 47-232 1.05e-17

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: 80.73  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573   47 AVITGAGDGIGKAYSFELAR----HGLNVVLISRTLEKLQTIAEEIERTT-GSCVKIVQADFTRE-DIYDHIKEHLE--- 117
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIGAERsGLRVVRVSLDLGAEaGLEQLLKALRElpr 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  118 --GLEIGILVNNVGMLPSFFP-SHFLSTSGESQNLIHCNITSVVKMTQLVLKHMESRR--KGLILNISSGAALRPWPLYS 192
Cdd:TIGR01500  83 pkGLQRLLLINNAGTLGDVSKgFVDLSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPglNRTVVNISSLCAIQPFKGWA 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 153792573  193 LYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:TIGR01500 163 LYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQ 202
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 47-224 1.41e-17

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


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 80.58  E-value: 1.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIErTTGSCVKIVQADFTREDIYDHIKEHLEGL--EIGIL 124
Cdd:cd08935    8 AVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEIT-ALGGRAIALAADVLDRASLERAREEIVAQfgTVDIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 VNNVGML---PSFFPSHFLSTSGES---------QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYS 192
Cdd:cd08935   87 INGAGGNhpdATTDPEHYEPETEQNffdldeegwEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSPLTKVP 166

                        170       180       190
                 ....*....|....*....|....*....|..
gi 153792573 193 LYSASKAFVYTFSKALSVEYRDKGIIIQVLTP 224
Cdd:cd08935  167 AYSAAKAAVSNFTQWLAVEFATTGVRVNAIAP 198
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 44-235 1.74e-17

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 80.02  E-value: 1.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIErTTGSCVKIVQADFTRED----IYDHIKEHLEGL 119
Cdd:PRK12939   7 GKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALE-AAGGRAHAIAADLADPAsvqrFFDAAAAALGGL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIgiLVNNVGMLPSFFPSHFlsTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:PRK12939  86 DG--LVNNAGITNSKSATEL--DIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKG 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYL 235
Cdd:PRK12939 162 AVIGMTRSLARELGGRGITVNAIAPGLTATEATAYV 197
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 49-208 1.83e-17

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 79.80  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  49 ITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIerttGSCVKIVQADFT-REDIYDHIKEHLEGL-EIGILVN 126
Cdd:PRK10538   5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDEL----GDNLYIAQLDVRnRAAIEEMLASLPAEWrNIDVLVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 127 NVGMLPSFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYTFSK 206
Cdd:PRK10538  81 NAGLALGLEPAHKASVE-DWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSL 159


                 ..
gi 153792573 207 AL 208
Cdd:PRK10538 160 NL 161
PRK07775 PRK07775
SDR family oxidoreductase;
47-231 2.62e-17

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 80.18  E-value: 2.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKiVQADFTRED-IYDHIKEHLEGL-EIGIL 124
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVA-FPLDVTDPDsVKSFVAQAEEALgEIEVL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 VNNVGMLpSFFPSHFLSTSG-ESQNLIHcnITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYT 203
Cdd:PRK07775  92 VSGAGDT-YFGKLHEISTEQfESQVQIH--LVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEA 168

                        170       180
                 ....*....|....*....|....*...
gi 153792573 204 FSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK07775 169 MVTNLQMELEGTGVRASIVHPGPTLTGM 196
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 47-232 3.00e-17

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: 78.94  E-value: 3.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERttgscVKIVQADFTreDIYDH-----IKEHLEGlEI 121
Cdd:cd08932    3 ALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSASGGD-----VEAVPYDAR--DPEDAralvdALRDRFG-RI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMLPsffPSHFLSTS-GESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAF 200
Cdd:cd08932   75 DVLVHNAGIGR---PTTLREGSdAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFA 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 153792573 201 VYTFSKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:cd08932  152 LRALAHALRQEGWDHGVRVSAVCPGFVDTPMA 183
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 44-232 3.01e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 80.01  E-value: 3.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIErtTGSCVKIVQADFTR----EDIYDHIKEHLEGl 119
Cdd:PRK05872   9 GKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELG--GDDRVLTVVADVTDlaamQAAAEEAVERFGG- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 eIGILVNNVGMLPsffPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMeSRRKGLILNISSGAALRPWPLYSLYSASK 198
Cdd:PRK05872  86 -IDVVVANAGIAS---GGSVAQVDPDAfRRVIDVNLLGVFHTVRATLPAL-IERRGYVLQVSSLAAFAAAPGMAAYCASK 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:PRK05872 161 AGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLV 194
PRK07326 PRK07326
SDR family oxidoreductase;
43-280 3.01e-17

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 79.28  E-value: 3.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERttGSCVKIVQADFTR----EDIYDHIKEHLEG 118
Cdd:PRK07326   5 KGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNN--KGNVLGLAADVRDeadvQRAVDAIVAAFGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEIgiLVNNVGmLPSFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMeSRRKGLILNISSGAALRPWPLYSLYSASK 198
Cdd:PRK07326  83 LDV--LIANAG-VGHFAPVEELTPE-EWRLVIDTNLTGAFYTIKAAVPAL-KRGGGYIINISSLAGTNFFAGGAAYNASK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTPYSISTpmtkYLNNKMTKTADEFvkeslkyvTIGAESCGCLAHEIIAIILNRIPS 278
Cdd:PRK07326 158 FGLVGFSEAAMLDLRQYGIKVSTIMPGSVAT----HFNGHTPSEKDAW--------KIQPEDIAQLVLDLLKMPPRTLPS 225


                 ..
gi 153792573 279 RI 280
Cdd:PRK07326 226 KI 227
PRK12743 PRK12743
SDR family oxidoreductase;
43-232 4.06e-17

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 79.31  E-value: 4.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNV-VLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTR----EDIYDHIKEHLE 117
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDIgITWHSDEEGAKETAEEV-RSHGVRAEIRQLDLSDlpegAQALDKLIQRLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 118 GleIGILVNNVGMLpsfFPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHM-ESRRKGLILNISSGAALRPWPLYSLYS 195
Cdd:PRK12743  80 R--IDVLVNNAGAM---TKAPFLDMDFDEwRKIFTVDVDGAFLCSQIAARHMvKQGQGGRIINITSVHEHTPLPGASAYT 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 153792573 196 ASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:PRK12743 155 AAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMN 191
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 47-231 4.11e-17

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: 79.12  E-value: 4.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTR-EDIYDHIKEHLEGL-EIGIL 124
Cdd:cd08945    6 ALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKEL-REAGVEADGRTCDVRSvPEIEALVAAAVARYgPIDVL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 VNNVGMlpsffpshflSTSGESQNL--------IHCNITSVVKMTQLVLKH--MESRRKGLILNISSGAALRPWPLYSLY 194
Cdd:cd08945   85 VNNAGR----------SGGGATAELadelwldvVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPY 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:cd08945  155 SASKHGVVGFTKALGLELARTGITVNAVCPGFVETPM 191
PRK06114 PRK06114
SDR family oxidoreductase;
44-233 4.51e-17

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 79.06  E-value: 4.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLIS-RTLEKLQTIAEEIERTTGSCVKIvQADFT-REDIYDHI---KEHLEG 118
Cdd:PRK06114   8 GQVAFVTGAGSGIGQRIAIGLAQAGADVALFDlRTDDGLAETAEHIEAAGRRAIQI-AADVTsKADLRAAVartEAELGA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEIGilVNNVGMLPSFfPSHFLsTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISS--GAALRPWPLYSLYSA 196
Cdd:PRK06114  87 LTLA--VNAAGIANAN-PAEEM-EEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASmsGIIVNRGLLQAHYNA 162

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 153792573 197 SKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:PRK06114 163 SKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNT 199
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
41-238 4.95e-17

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 78.99  E-value: 4.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  41 RSMGQWAVITGAGDGIGKAYSFELARHGLNVVLI-SRTLEKLQTIAEEIERTTGSCVkIVQADFTRE----DIYDHIKEH 115
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEIEALGRKAL-AVKANVGDVekikEMFAQIDEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 116 LEGLEIgiLVNNV--GMLPsffPSHFLSTSG-------ESQNLIHCnitsvvkmTQLVLKHMESRRKGLILNISSGAALR 186
Cdd:PRK08063  80 FGRLDV--FVNNAasGVLR---PAMELEESHwdwtmniNAKALLFC--------AQEAAKLMEKVGGGKIISLSSLGSIR 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 153792573 187 PWPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNK 238
Cdd:PRK08063 147 YLENYTTVGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPNR 198
PRK09730 PRK09730
SDR family oxidoreductase;
47-231 6.35e-17

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 78.35  E-value: 6.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNV-VLISRTLEKLQTIAEEIERTTGSCVKIvQADFTRED----IYDHIKEHLEGLei 121
Cdd:PRK09730   4 ALVTGGSRGIGRATALLLAQEGYTVaVNYQQNLHAAQEVVNLITQAGGKAFVL-QADISDENqvvaMFTAIDQHDEPL-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMLpsFFPSHFLSTSGESQN-LIHCNITSVVKMTQLVLKHMESR---RKGLILNISSGAALRPWP-LYSLYSA 196
Cdd:PRK09730  81 AALVNNAGIL--FTQCTVENLTAERINrVLSTNVTGYFLCCREAVKRMALKhggSGGAIVNVSSAASRLGAPgEYVDYAA 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 197 SKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK09730 159 SKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEM 193
PRK06182 PRK06182
short chain dehydrogenase; Validated
 47-230 7.64e-17

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 78.85  E-value: 7.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEeierttgSCVKIVQADFTREDIYDHIKEHLEGLE--IGIL 124
Cdd:PRK06182   6 ALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLAS-------LGVHPLSLDVTDEASIKAAVDTIIAEEgrIDVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 VNNVGmlpsfFPSHflstsG--------ESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSA 196
Cdd:PRK06182  79 VNNAG-----YGSY-----GaiedvpidEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHA 148

                        170       180       190
                 ....*....|....*....|....*....|....
gi 153792573 197 SKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTP 230
Cdd:PRK06182 149 TKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTE 182
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 44-231 7.92e-17

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 78.39  E-value: 7.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTRE----DIYDHIKEHLEGL 119
Cdd:PRK12429   4 GKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEAL-QKAGGKAIGVAMDVTDEeainAGIDYAVETFGGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EigILVNNVGM-----LPSFFPSHFlstsgesQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLY 194
Cdd:PRK12429  83 D--ILVNNAGIqhvapIEDFPTEKW-------KKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAY 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK12429 154 VSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTPL 190
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
43-243 8.11e-17

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 78.23  E-value: 8.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKiVQADFT-REDIY---DHIKEHLEG 118
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIA-VKADVSdRDQVFaavRQVVDTFGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEigILVNNVGMLPSfFPshfLSTSGESQ--NLIHCNITSVVKMTQLVLKHMESR-RKGLILNISSGAALRPWPLYSLYS 195
Cdd:PRK08643  80 LN--VVVNNAGVAPT-TP---IETITEEQfdKVYNINVGGVIWGIQAAQEAFKKLgHGGKIINATSQAGVVGNPELAVYS 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 153792573 196 ASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTKTA 243
Cdd:PRK08643 154 STKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPMMFDIAHQVGENA 201
PRK06172 PRK06172
SDR family oxidoreductase;
44-231 8.41e-17

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 78.25  E-value: 8.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTREDiydHIKEHLEGL---- 119
Cdd:PRK06172   7 GKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALI-REAGGEALFVACDVTRDA---EVKALVEQTiaay 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 -EIGILVNNVGMlpsffpshflstSGESQNLIHCN------ITSV-VKMTQLVLKH----MESRRKGLILNISSGAALRP 187
Cdd:PRK06172  83 gRLDYAFNNAGI------------EIEQGRLAEGSeaefdaIMGVnVKGVWLCMKYqiplMLAQGGGAIVNTASVAGLGA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 153792573 188 WPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK06172 151 APKMSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDM 194
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 47-231 1.15e-16

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: 77.51  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEeierttgscvkivQADFTREDIYD--HIKEHLEGLE---- 120
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGD-------------PLRLTPLDVADaaAVREVCSRLLaehg 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 -IGILVNNVGMLpSFFPSHFLSTsGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:cd05331   68 pIDALVNCAGVL-RPGATDPLST-EDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKA 145

                        170       180       190
                 ....*....|....*....|....*....|..
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:cd05331  146 ALASLSKCLGLELAPYGVRCNVVSPGSTDTAM 177
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 46-211 1.25e-16

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: 77.32  E-value: 1.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  46 WAVITGAGDGIGKAYSFELARHGLNVVLISRTLE-KLQTIAEEIERTTGSCVkIVQADFTR----EDIYDHIKEHLEGLE 120
Cdd:cd05357    2 VALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEaEAQRLKDELNALRNSAV-LVQADLSDfaacADLVAAAFRAFGRCD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 igILVNNVGmlpSFFPSHFLSTsgeSQNLIHCNITSVVKMTQLVLKHMESR----RKGLILNISSGAALRPWPLYSLYSA 196
Cdd:cd05357   81 --VLVNNAS---AFYPTPLGQG---SEDAWAELFGINLKAPYLLIQAFARRlagsRNGSIINIIDAMTDRPLTGYFAYCM 152

                        170
                 ....*....|....*
gi 153792573 197 SKAFVYTFSKALSVE 211
Cdd:cd05357  153 SKAALEGLTRSAALE 167
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 37-229 1.37e-16

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 77.58  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  37 SSFLRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKiVQADFTRE-DIYDHIKEH 115
Cdd:PRK06113   4 SDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFA-CRCDITSEqELSALADFA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 116 LEGL-EIGILVNNVGmlpSFFPSHFLSTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLY 194
Cdd:PRK06113  83 LSKLgKVDILVNNAG---GGGPKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSY 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGIIIQVLTPYSIST 229
Cdd:PRK06113 160 ASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILT 194
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 43-232 1.47e-16

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 77.31  E-value: 1.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRtleklqtiaEEIERTTGScVKIVQADFTrediyDHIKEHLEGL-EI 121
Cdd:PRK06550   4 MTKTVLITGAASGIGLAQARAFLAQGAQVYGVDK---------QDKPDLSGN-FHFLQLDLS-----DDLEPLFDWVpSV 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMLPSFFPShfLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISS---------GAAlrpwply 191
Cdd:PRK06550  69 DILCNTAGILDDYKPL--LDTSLEEwQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSiasfvagggGAA------- 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 153792573 192 slYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:PRK06550 140 --YTASKHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMT 178
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 49-233 1.69e-16

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: 76.72  E-value: 1.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  49 ITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIErttGSCVKIVQADFTREDIYDHIKEHL---EGLEIGILV 125
Cdd:cd08931    5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELG---AENVVAGALDVTDRAAWAAALADFaaaTGGRLDALF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 126 NNVGMLpSFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYTFS 205
Cdd:cd08931   82 NNAGVG-RGGPFEDVPLA-AHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGLT 159

                        170       180
                 ....*....|....*....|....*...
gi 153792573 206 KALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:cd08931  160 EALDVEWARHGIRVADVWPWFVDTPILT 187
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 43-231 1.77e-16

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 77.07  E-value: 1.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLIS----RTLEKLQTIAEEIERTTGScVKIVQADFTR----EDIYDHIKE 114
Cdd:PRK12827   5 DSRRVLITGGSGGLGRAIAVRLAADGADVIVLDihpmRGRAEADAVAAGIEAAGGK-ALGLAFDVRDfaatRAALDAGVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 115 HLEGLEIgiLVNNVGMLPSF-FPShfLSTSgESQNLIHCNITSVVKMTQLVLKHM-ESRRKGLILNISSGAALRPWPLYS 192
Cdd:PRK12827  84 EFGRLDI--LVNNAGIATDAaFAE--LSIE-EWDDVIDVNLDGFFNVTQAALPPMiRARRGGRIVNIASVAGVRGNRGQV 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 153792573 193 LYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK12827 159 NYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPM 197
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 44-249 1.80e-16

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 77.63  E-value: 1.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKiVQADFTRED----IYDHIKEHLEGL 119
Cdd:PRK13394   7 GKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIG-VAMDVTNEDavnaGIDKVAERFGSV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EigILVNNVGM-----LPSFfpshflsTSGESQNLIHCNITSVVKMTQLVLKHM-ESRRKGLILNISSGAALRPWPLYSL 193
Cdd:PRK13394  86 D--ILVSNAGIqivnpIENY-------SFADWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153792573 194 YSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMtkylnnkMTKTADEFVKE 249
Cdd:PRK13394 157 YVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPL-------VDKQIPEQAKE 205
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 37-230 3.48e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 76.48  E-value: 3.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  37 SSFLRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTleKLQTIAEEIErttgscvkIVQADFTRED----IYDHI 112
Cdd:PRK06523   2 SFFLELAGKRALVTGGTKGIGAATVARLLEAGARVVTTARS--RPDDLPEGVE--------FVAADLTTAEgcaaVARAV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 113 KEHLEGLEIgiLVNNVGMlPSFFPSHFLS-TSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLY 191
Cdd:PRK06523  72 LERLGGVDI--LVHVLGG-SSAPAGGFAAlTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPES 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 153792573 192 SL-YSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTP 230
Cdd:PRK06523 149 TTaYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETE 188
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 44-231 3.54e-16

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 76.58  E-value: 3.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVL-ISRTLEKLQTIAEEIeRTTGSCVKIVQADFTREDIYDHIKEHLEGL--E 120
Cdd:PRK12935   6 GKVAIVTGGAKGIGKAITVALAQEGAKVVInYNSSKEAAENLVNEL-GKEGHDVYAVQADVSKVEDANRLVEEAVNHfgK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 IGILVNNVGMLPSffpSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:PRK12935  85 VDILVNNAGITRD---RTFKKLNREDwERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKA 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK12935 162 GMLGFTKSLALELAKTNVTVNAICPGFIDTEM 193
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 44-248 4.78e-16

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 75.93  E-value: 4.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVL-ISRTLEKLQTIAEEIERTTGSCVKiVQADFTREDIYDHIKEHLEGL--E 120
Cdd:PRK12937   5 NKVAIVTGASRGIGAAIARRLAADGFAVAVnYAGSAAAADELVAEIEAAGGRAIA-VQADVADAAAVTRLFDAAETAfgR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 IGILVNNVGMLPsffPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMesRRKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:PRK12937  84 IDVLVNNAGVMP---LGTIADFDLEDfDRTIATNLRGAFVVLREAARHL--GQGGRIINLSTSVIALPLPGYGPYAASKA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPMtkYLNNKMTKTADEFVK 248
Cdd:PRK12937 159 AVEGLVHVLANELRGRGITVNAVAPGPVATEL--FFNGKSAEQIDQLAG 205
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 41-235 7.44e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 75.54  E-value: 7.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  41 RSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTtgscvkIVQADFTRED----IYDHIKEHL 116
Cdd:PRK06057   4 RLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGL------FVPTDVTDEDavnaLFDTAAETY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 117 EGLEIGIlvNNVGMLPSFFPShFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISS-----GAALRPWPl 190
Cdd:PRK06057  78 GSVDIAF--NNAGISPPEDDS-ILNTGLDAwQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASfvavmGSATSQIS- 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 153792573 191 yslYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYL 235
Cdd:PRK06057 154 ---YTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQEL 195
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 47-217 7.59e-16

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: 75.11  E-value: 7.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTRED----IYDHIKEHLEGLEig 122
Cdd:cd05373    2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDeviaLFDLIEEEIGPLE-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ILVNNVGmlpSFFPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:cd05373   80 VLVYNAG---ANVWFPILETTPRVfEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFAL 156

                        170
                 ....*....|....*.
gi 153792573 202 YTFSKALSVEYRDKGI 217
Cdd:cd05373  157 RALAQSMARELGPKGI 172
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 47-232 1.03e-15

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: 74.75  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGL-NVVLISRTLEKlqtiAEEIERTTGSCVKIVQADFTreDIyDHIKEHLEGL-EIGIL 124
Cdd:cd05354    6 VLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGS----AAHLVAKYGDKVVPLRLDVT--DP-ESIKAAAAQAkDVDVV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 VNNVGML--PSFFPSHFLSTSgesQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVY 202
Cdd:cd05354   79 INNAGVLkpATLLEEGALEAL---KQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAAY 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 153792573 203 TFSKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:cd05354  156 SLTQGLRAELAAQGTLVLSVHPGPIDTRMA 185
PRK08267 PRK08267
SDR family oxidoreductase;
49-239 1.56e-15

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 74.59  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  49 ITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIertTGSCVKIVQADFTREDIYDHIKEH---LEGLEIGILV 125
Cdd:PRK08267   6 ITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAEL---GAGNAWTGALDVTDRAAWDAALADfaaATGGRLDVLF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 126 NNVGMLPSffpSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYTF 204
Cdd:PRK08267  83 NNAGILRG---GPFEDIPLEAhDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGL 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 205 SKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKM 239
Cdd:PRK08267 160 TEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEV 194
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 48-231 1.58e-15

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 74.54  E-value: 1.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTR------EDIYDHIKEHLEGLEi 121
Cdd:cd05340    8 LVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFILDLLTctsencQQLAQRIAVNYPRLD- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILvNNVGMLPSFFPSHFLsTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:cd05340   87 GVL-HNAGLLGDVCPLSEQ-NPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSKFAT 164

                        170       180       190
                 ....*....|....*....|....*....|
gi 153792573 202 YTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:cd05340  165 EGL*QVLADEYQQRNLRVNCINPGGTRTAM 194
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 44-231 1.69e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 74.37  E-value: 1.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIerttgSCVKIVQaDFTREDIYDHIKEHLEGLEIgi 123
Cdd:PRK07060   9 GKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGET-----GCEPLRL-DVGDDAAIRAALAAAGAFDG-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 124 LVNNVGM--LPSFfpshfLSTSGES-QNLIHCNITSVVKMTQLVLKHM-ESRRKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:PRK07060  81 LVNCAGIasLESA-----LDMTAEGfDRVMAVNARGAALVARHVARAMiAAGRGGSIVNVSSQAALVGLPDHLAYCASKA 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK07060 156 ALDAITRVLCVELGPHGIRVNSVNPTVTLTPM 187
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 40-243 2.18e-15

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: 74.49  E-value: 2.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  40 LRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTRE-DIYDHIKEHLEG 118
Cdd:cd08933    5 LRYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKFVPCDVTKEeDIKTLISVTVER 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 L-EIGILVNNVGMLPSffPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMEsRRKGLILNISSGAALRPWPLYSLYSA 196
Cdd:cd08933   85 FgRIDCLVNNAGWHPP--HQTTDETSAQEfRDLLNLNLISYFLASKYALPHLR-KSQGNIINLSSLVGSIGQKQAAPYVA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153792573 197 SKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTKTA 243
Cdd:cd08933  162 TKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAQTPDTL 208
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 41-231 3.39e-15

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: 73.64  E-value: 3.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  41 RSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGScvkIVQADFTRED----IYDHIKEHL 116
Cdd:cd05326    1 RLDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDIS---FVHCDVTVEAdvraAVDTAVARF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 117 EGLEIgiLVNNVGMLPSFFPSHFLSTSGESQNLIHCNITSVVkmtqLVLKH----MESRRKGLILNISSGAALRPWPLYS 192
Cdd:cd05326   78 GRLDI--MFNNAGVLGAPCYSILETSLEEFERVLDVNVYGAF----LGTKHaarvMIPAKKGSIVSVASVAGVVGGLGPH 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 153792573 193 LYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:cd05326  152 AYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPL 190
PRK06138 PRK06138
SDR family oxidoreductase;
40-252 4.08e-15

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 73.65  E-value: 4.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  40 LRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIerTTGSCVKIVQADFTR----EDIYDHIKEH 115
Cdd:PRK06138   1 MRLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAI--AAGGRAFARQGDVGSaeavEALVDFVAAR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 116 LEGLEIgiLVNNVGMLPSffpSHFLSTSGESQN-LIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLY 194
Cdd:PRK06138  79 WGRLDV--LVNNAGFGCG---GTVVTTDEADWDaVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAY 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMtkyLNNKMTKTAD-EFVKESLK 252
Cdd:PRK06138 154 VASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPY---FRRIFARHADpEALREALR 209
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 44-234 4.63e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 73.54  E-value: 4.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTlEKLQTIAEEIERTTGscvKIVQADFTRED----IYDHIKEHLEGl 119
Cdd:PRK06841  15 GKVAVVTGGASGIGHAIAELFAAKGARVALLDRS-EDVAEVAAQLLGGNA---KGLVCDVSDSQsveaAVAAVISAFGR- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 eIGILVNNVGMLPsFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:PRK06841  90 -IDILVNSAGVAL-LAPAEDVSEE-DWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASKA 166

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKY 234
Cdd:PRK06841 167 GVVGMTKVLALEWGPYGITVNAISPTVVLTELGKK 201
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 43-232 5.07e-15

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 73.07  E-value: 5.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRT-LEKLQTIAEEIeRTTGSCVKIVQADF----TREDIYDHIKEHLE 117
Cdd:PRK12745   1 MRPVALVTGGRRGIGLGIARALAAAGFDLAINDRPdDEELAATQQEL-RALGVEVIFFPADVadlsAHEAMLDAAQAAWG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 118 GLEigILVNNVGMLPSfFPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRK------GLILNISSGAALRPWPL 190
Cdd:PRK12745  80 RID--CLVNNAGVGVK-VRGDLLDLTPESfDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVSSVNAIMVSPN 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 153792573 191 YSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:PRK12745 157 RGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMT 198
PRK06484 PRK06484
short chain dehydrogenase; Validated
 47-230 5.99e-15

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 74.89  E-value: 5.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEeierTTGSCVKIVQADFTREDIYDHIKEHLEGL--EIGIL 124
Cdd:PRK06484 272 VAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAE----ALGDEHLSVQADITDEAAVESAFAQIQARwgRLDVL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 VNNVGMLPSFFPShfLSTSGES-QNLIHCNITSVVKMTQLVLKHMesRRKGLILNISSGAALRPWPLYSLYSASKAFVYT 203
Cdd:PRK06484 348 VNNAGIAEVFKPS--LEQSAEDfTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAYCASKAAVTM 423

                        170       180
                 ....*....|....*....|....*..
gi 153792573 204 FSKALSVEYRDKGIIIQVLTPYSISTP 230
Cdd:PRK06484 424 LSRSLACEWAPAGIRVNTVAPGYIETP 450
PRK07832 PRK07832
SDR family oxidoreductase;
47-233 7.01e-15

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 73.15  E-value: 7.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTRediYDHIKE-----HLEGLEI 121
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPEHRALDISD---YDAVAAfaadiHAAHGSM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGmlpsffpshfLSTSGESQNLIHCNITSVVK---------MTQLVLKHMESRRKGLILNISSGAALRPWPLYS 192
Cdd:PRK07832  80 DVVMNIAG----------ISAWGTVDRLTHEQWRRMVDvnlmgpihvIETFVPPMVAAGRGGHLVNVSSAAGLVALPWHA 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 153792573 193 LYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:PRK07832 150 AYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVN 190
PRK09291 PRK09291
SDR family oxidoreductase;
43-224 7.27e-15

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 72.72  E-value: 7.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERtTGSCVKIVQADFTreDIYDhiKEHLEGLEIG 122
Cdd:PRK09291   1 MSKTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAAR-RGLALRVEKLDLT--DAID--RAQAAEWDVD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ILVNNVGMlpsffpshflstsGESQNLI-----------HCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLY 191
Cdd:PRK09291  76 VLLNNAGI-------------GEAGAVVdipvelvrelfETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFT 142

                        170       180       190
                 ....*....|....*....|....*....|...
gi 153792573 192 SLYSASKAFVYTFSKALSVEYRDKGIIIQVLTP 224
Cdd:PRK09291 143 GAYCASKHALEAIAEAMHAELKPFGIQVATVNP 175
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 48-241 1.16e-14

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 72.30  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVqADFTRE----DIYDHIKEHLEGleIGI 123
Cdd:PRK08217   9 VITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYA-ANVTDEedveATFAQIAEDFGQ--LNG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 124 LVNNVG-----MLPSFFPSHFLSTSG--ESQNLIHCNITSVVKMTQLVLKHM-ESRRKGLILNISS-------GAalrpw 188
Cdd:PRK08217  86 LINNAGilrdgLLVKAKDGKVTSKMSleQFQSVIDVNLTGVFLCGREAAAKMiESGSKGVIINISSiaragnmGQ----- 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 153792573 189 plySLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLN----NKMTK 241
Cdd:PRK08217 161 ---TNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKpealERLEK 214
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 44-235 2.01e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 71.71  E-value: 2.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTREDIYDHIKEHLEgLEIG- 122
Cdd:PRK08085   9 GKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKL-RQEGIKAHAAPFNVTHKQEVEAAIEHIE-KDIGp 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 --ILVNNVGMLPSF----FPSHflstsgESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSA 196
Cdd:PRK08085  87 idVLINNAGIQRRHpfteFPEQ------EWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAA 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 153792573 197 SKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYL 235
Cdd:PRK08085 161 SKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKAL 199
PRK07069 PRK07069
short chain dehydrogenase; Validated
 47-231 2.80e-14

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 70.89  E-value: 2.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEK-LQTIAEEIERTTGSCVKI-VQADFTREDIYDHI----KEHLEGLE 120
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAgLDAFAAEINAAHGEGVAFaAVQDVTDEAQWQALlaqaADAMGGLS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 IgiLVNNVGMlpsffpSHFLSTSGESQNLIH----CNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSA 196
Cdd:PRK07069  82 V--LVNNAGV------GSFGAIEQIELDEWRrvmaINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNA 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 153792573 197 SKAFVYTFSKALSVEYRDKGIIIQV--LTPYSISTPM 231
Cdd:PRK07069 154 SKAAVASLTKSIALDCARRGLDVRCnsIHPTFIRTGI 190
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 44-231 3.02e-14

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: 71.11  E-value: 3.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIErtTGSCVkiVQADFT-REDIYDHIKEHLEGL-EI 121
Cdd:cd05363    3 GKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIG--PAACA--ISLDVTdQASIDRCVAALVDRWgSI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMlpsFFPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESR-RKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:cd05363   79 DILVNNAAL---FDLAPIVDITRESyDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEALVGVYCATKA 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:cd05363  156 AVISLTQSAGLNLIRHGINVNAIAPGVVDGEH 187
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 41-217 3.04e-14

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 71.13  E-value: 3.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  41 RSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTlEKLQTIAEEIERTTGSCVKIVqADFTR----EDIYDHIKEHL 116
Cdd:PRK12823   5 RFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRS-ELVHEVAAELRAAGGEALALT-ADLETyagaQAAMAAAVEAF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 117 EGLEigILVNNVG----MLP---------------SFFPShflstsgesqnLIHCnitsvvkmtQLVLKHMESRRKGLIL 177
Cdd:PRK12823  83 GRID--VLINNVGgtiwAKPfeeyeeeqieaeirrSLFPT-----------LWCC---------RAVLPHMLAQGGGAIV 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 153792573 178 NISSGA--ALRPWPlyslYSASKAFVYTFSKALSVEYRDKGI 217
Cdd:PRK12823 141 NVSSIAtrGINRVP----YSAAKGGVNALTASLAFEYAEHGI 178
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 40-217 3.41e-14

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 70.84  E-value: 3.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  40 LRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTREDiyDHIKEHLEGL 119
Cdd:PRK06125   3 LHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVDVAVHALDLSSPE--AREQLAAEAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIGILVNNVGMLPSffPSHFLSTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:PRK06125  81 DIDILVNNAGAIPG--GGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAGENPDADYICGSAGNA 158

                        170
                 ....*....|....*...
gi 153792573 200 FVYTFSKALSVEYRDKGI 217
Cdd:PRK06125 159 ALMAFTRALGGKSLDDGV 176
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
44-199 5.18e-14

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 72.19  E-value: 5.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCvkIVQADFTRED----IYDHIKEHLEGL 119
Cdd:PRK08324 422 GKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPDRAL--GVACDVTDEAavqaAFEEAALAFGGV 499

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EigILVNNVGMlpsFFPSHFLSTSGESQNLIH-CNITSVVKMTQLVLKHMesRRKGL---ILNISSGAALRPWPLYSLYS 195
Cdd:PRK08324 500 D--IVVSNAGI---AISGPIEETSDEDWRRSFdVNATGHFLVAREAVRIM--KAQGLggsIVFIASKNAVNPGPNFGAYG 572


                 ....
gi 153792573 196 ASKA 199
Cdd:PRK08324 573 AAKA 576
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 49-231 5.24e-14

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 70.29  E-value: 5.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  49 ITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADF---TREDiYDHIKEHLEGlEIGIL- 124
Cdd:PRK08945  17 VTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIPLDLltaTPQN-YQQLADTIEE-QFGRLd 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 --VNNVGMLPSFFPshFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:PRK08945  95 gvLHNAGLLGELGP--MEQQDPEVwQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANWGAYAVSKFAT 172

                        170       180       190
                 ....*....|....*....|....*....|
gi 153792573 202 YTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK08945 173 EGMMQVLADEYQGTNLRVNCINPGGTRTAM 202
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 49-234 1.86e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 68.91  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  49 ITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIerttGSCVKIVQADFT-REDIYDHIKEHLEGL-EIGILVN 126
Cdd:PRK08263   8 ITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKY----GDRLLPLALDVTdRAAVFAAVETAVEHFgRLDIVVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 127 NVGMLPSFFPSHFlsTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYTFSK 206
Cdd:PRK08263  84 NAGYGLFGMIEEV--TESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEGMSE 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 153792573 207 ALSVEYRDKGIIIQVLTP--YS---------ISTPMTKY 234
Cdd:PRK08263 162 ALAQEVAEFGIKVTLVEPggYStdwagtsakRATPLDAY 200
PRK07102 PRK07102
SDR family oxidoreductase;
49-232 2.61e-13

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 68.03  E-value: 2.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  49 ITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTRediYDHIKEHLEGL--EIGILVN 126
Cdd:PRK07102   6 IIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAVAVSTHELDILD---TASHAAFLDSLpaLPDIVLI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 127 NVGMLPSffPSHFLSTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYTFSK 206
Cdd:PRK07102  83 AVGTLGD--QAACEADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKAALTAFLS 160

                        170       180
                 ....*....|....*....|....*...
gi 153792573 207 ALSVEYRDKGiiIQVLT--PYSISTPMT 232
Cdd:PRK07102 161 GLRNRLFKSG--VHVLTvkPGFVRTPMT 186
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 44-231 5.23e-13

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 67.60  E-value: 5.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRtleklqtiaeEIERTTGSCVKIVQADFTR----EDIYDHIKEHLEGL 119
Cdd:PRK08220   8 GKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQ----------AFLTQEDYPFATFVLDVSDaaavAQVCQRLLAETGPL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIgiLVNNVGMLpSFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:PRK08220  78 DV--LVNAAGIL-RMGATDSLSDE-DWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKA 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK08220 154 ALTSLAKCVGLELAPYGVRCNVVSPGSTDTDM 185
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 41-237 5.37e-13

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: 67.55  E-value: 5.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  41 RSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTlEKLQTIAEEIeRTTGSCVKIVQADFTREDIYDHIKEHLEGL- 119
Cdd:cd08937    1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRS-ELVHEVLAEI-LAAGDAAHVHTADLETYAGAQGVVRAAVERf 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 -EIGILVNNVG--MLPSFFpSHFlsTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSgAALRPwPLYSLYSA 196
Cdd:cd08937   79 gRVDVLINNVGgtIWAKPY-EHY--EEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSS-IATRG-IYRIPYSA 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 153792573 197 SKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNN 237
Cdd:cd08937  154 AKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPRN 194
PRK05867 PRK05867
SDR family oxidoreductase;
44-234 5.75e-13

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 67.37  E-value: 5.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIvQADFTRED----IYDHIKEHLEGL 119
Cdd:PRK05867   9 GKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPV-CCDVSQHQqvtsMLDQVTAELGGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIGilVNNVGMLpSFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHM-ESRRKGLILNIS--SGAALRPWPLYSLYSA 196
Cdd:PRK05867  88 DIA--VCNAGII-TVTPMLDMPLE-EFQRLQNTNVTGVFLTAQAAAKAMvKQGQGGVIINTAsmSGHIINVPQQVSHYCA 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 153792573 197 SKAFVYTFSKALSVEYRDKGIIIQVLTPYSIST----PMTKY 234
Cdd:PRK05867 164 SKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTelvePYTEY 205
PRK08264 PRK08264
SDR family oxidoreductase;
47-235 6.88e-13

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 66.84  E-value: 6.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLN-VVLISRTLEklqTIAEEIERttgscVKIVQADFT-REDIY---DHIKEhlegleI 121
Cdd:PRK08264   9 VLVTGANRGIGRAFVEQLLARGAAkVYAAARDPE---SVTDLGPR-----VVPLQLDVTdPASVAaaaEAASD------V 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMLPSffPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAF 200
Cdd:PRK08264  75 TILVNNAGIFRT--GSLLLEGDEDAlRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAA 152

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 201 VYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYL 235
Cdd:PRK08264 153 AWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAGL 187
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 45-224 7.43e-13

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: 67.10  E-value: 7.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  45 QWAVITGAGDGIGKAYSFELARHGLNVVL-ISRTLEKLQTIAEEIerttGSCVKIVQADFT-REDI---YDHIKEHLegL 119
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVnYYRSTESAEAVAAEA----GERAIAIQADVRdRDQVqamIEEAKNHF--G 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIGILVNNVGMLPSFFPSH---FLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYS 195
Cdd:cd05349   75 PVDTIVNNALIDFPFDPDQrktFDTIDWEDyQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYT 154

                        170       180
                 ....*....|....*....|....*....
gi 153792573 196 ASKAFVYTFSKALSVEYRDKGIIIQVLTP 224
Cdd:cd05349  155 TAKAALLGFTRNMAKELGPYGITVNMVSG 183
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 44-260 7.70e-13

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: 67.09  E-value: 7.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLE-KLQTIAEEIERTTGSCVkIVQADFTRED----IYDHIKEHLEG 118
Cdd:cd09763    3 GKIALVTGASRGIGRGIALQLGEAGATVYITGRTILpQLPGTAEEIEARGGKCI-PVRCDHSDDDeveaLFERVAREQQG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 lEIGILVNNV---------GMLPSFFpshflstsgESQNLIHCNITSVVKMTQLVLKH-----MESRRKGLILNISSGAA 184
Cdd:cd09763   82 -RLDILVNNAyaavqlilvGVAKPFW---------EEPPTIWDDINNVGLRAHYACSVyaaplMVKAGKGLIVIISSTGG 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792573 185 LRpwPLYSL-YSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKylnnKMTKTADEFVKESLKYVTIGAES 260
Cdd:cd09763  152 LE--YLFNVaYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVL----EMPEDDEGSWHAKERDAFLNGET 222
PRK06398 PRK06398
aldose dehydrogenase; Validated
 47-231 1.73e-12

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 66.01  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISrtleklqtiaeeIERTTGSCVKIVQADFTRED-IYDHIkEHLEGL--EIGI 123
Cdd:PRK06398   9 AIVTGGSQGIGKAVVNRLKEEGSNVINFD------------IKEPSYNDVDYFKVDVSNKEqVIKGI-DYVISKygRIDI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 124 LVNNVGmLPSFFPSHFLSTsGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYT 203
Cdd:PRK06398  76 LVNNAG-IESYGAIHAVEE-DEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAVLG 153

                        170       180
                 ....*....|....*....|....*...
gi 153792573 204 FSKALSVEYRDKgIIIQVLTPYSISTPM 231
Cdd:PRK06398 154 LTRSIAVDYAPT-IRCVAVCPGSIRTPL 180
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 48-231 3.43e-12

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: 65.23  E-value: 3.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEI-ERTTGSCVKIVQADFTRED-IYDHIKEHLEGL-EIGIL 124
Cdd:cd05330    7 LITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALlEIAPDAEVLLIKADVSDEAqVEAYVDATVEQFgRIDGF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 VNNVGMLPSFFPSHFLsTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYTF 204
Cdd:cd05330   87 FNNAGIEGKQNLTEDF-GADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHGVVGL 165

                        170       180
                 ....*....|....*....|....*..
gi 153792573 205 SKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:cd05330  166 TRNSAVEYGQYGIRINAIAPGAILTPM 192
PRK08219 PRK08219
SDR family oxidoreductase;
47-231 4.21e-12

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 64.57  E-value: 4.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGlNVVLISRTLEKLQTIAEEIERTTGscvkiVQADFTREDIYDHIKEHLEGLEIgiLVN 126
Cdd:PRK08219   6 ALITGASRGIGAAIARELAPTH-TLLLGGRPAERLDELAAELPGATP-----FPVDLTDPEAIAAAVEQLGRLDV--LVH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 127 NVGMLpsffpshFLSTSGES-----QNLIHCNITSVVKMTQLVLKHMESRRkGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:PRK08219  78 NAGVA-------DLGPVAEStvdewRATLEVNVVAPAELTRLLLPALRAAH-GHVVFINSGAGLRANPGWGSYAASKFAL 149

                        170       180       190
                 ....*....|....*....|....*....|..
gi 153792573 202 YTFSKALSVEYRDKgiiIQVLT--PYSISTPM 231
Cdd:PRK08219 150 RALADALREEEPGN---VRVTSvhPGRTDTDM 178
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 47-229 4.93e-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: 64.45  E-value: 4.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIA-EEIERTTGSCVKIVQADFTREdIYDHIKEHLEGLEIgiLV 125
Cdd:cd08929    3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAaQELEGVLGLAGDVRDEADVRR-AVDAMEEAFGGLDA--LV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 126 NNVGMlPSFFPSHFLSTSGESQNLIHcNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYTFS 205
Cdd:cd08929   80 NNAGV-GVMKPVEELTPEEWRLVLDT-NLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLS 157

                        170       180
                 ....*....|....*....|....
gi 153792573 206 KALSVEYRDKGIIIQVLTPYSIST 229
Cdd:cd08929  158 EAAMLDLREANIRVVNVMPGSVDT 181
PRK06139 PRK06139
SDR family oxidoreductase;
48-230 5.93e-12

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 65.13  E-value: 5.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTREDIYDHIKEHLEGL--EIGILV 125
Cdd:PRK06139  11 VITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEEC-RALGAEVLVVPTDVTDADQVKALATQAASFggRIDVWV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 126 NNVGMLPSffpSHFLSTSGE-SQNLIHCNITSVVKMTQLVLKHMESRRKGLILN-ISSGAalrpW---PLYSLYSASKAF 200
Cdd:PRK06139  90 NNVGVGAV---GRFEETPIEaHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINmISLGG----FaaqPYAAAYSASKFG 162

                        170       180       190
                 ....*....|....*....|....*....|.
gi 153792573 201 VYTFSKALSVEYRDK-GIIIQVLTPYSISTP 230
Cdd:PRK06139 163 LRGFSEALRGELADHpDIHVCDVYPAFMDTP 193
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 37-217 6.54e-12

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 64.65  E-value: 6.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  37 SSFLRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQtiaeeierttGSCVKIVQADFT-REDIYDHIKEH 115
Cdd:PRK06171   2 QDWLNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQ----------HENYQFVPTDVSsAEEVNHTVAEI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 116 LEGL-EIGILVNNVGM-LPSFF-------PSHFLSTSGESQnLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALR 186
Cdd:PRK06171  72 IEKFgRIDGLVNNAGInIPRLLvdekdpaGKYELNEAAFDK-MFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLE 150

                        170       180       190
                 ....*....|....*....|....*....|.
gi 153792573 187 PWPLYSLYSASKAFVYTFSKALSVEYRDKGI 217
Cdd:PRK06171 151 GSEGQSCYAATKAALNSFTRSWAKELGKHNI 181
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
47-233 7.10e-12

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 64.26  E-value: 7.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVL--------ISRTLEKLQTIAEEIERTTGScvkIVQADFTREdIYDHIKEhlEG 118
Cdd:PRK12938   6 AYVTGGMGGIGTSICQRLHKDGFKVVAgcgpnsprRVKWLEDQKALGFDFIASEGN---VGDWDSTKA-AFDKVKA--EV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEIGILVNNVGMLPSFFPSHFlsTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASK 198
Cdd:PRK12938  80 GEIDVLVNNAGITRDVVFRKM--TREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAK 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:PRK12938 158 AGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVK 192
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 48-290 8.15e-12

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: 64.02  E-value: 8.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELAR---HGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTREDIYDHIKEHLEGLEIGIL 124
Cdd:cd09806    4 LITGCSSGIGLHLAVRLASdpsKRFKVYATMRDLKKKGRLWEAAGALAGGTLETLQLDVCDSKSVAAAVERVTERHVDVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 VNNVGMlPSFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYTF 204
Cdd:cd09806   84 VCNAGV-GLLGPLEALSED-AMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALEGL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 205 SKALSVEYRDKGIIIQVLTPYSISTP-MTKYLNNKMT--------KTADEFVKESLKYVTIGAESCGCLAHEIIAIILNR 275
Cdd:cd09806  162 CESLAVQLLPFNVHLSLIECGPVHTAfMEKVLGSPEEvldrtaddITTFHFFYQYLAHSKQVFREAAQNPEEVAEVFLTA 241

                        250
                 ....*....|....*..
gi 153792573 276 I--PSRIFYSSTAQRFL 290
Cdd:cd09806  242 IraPKPPLRYFTNERYL 258
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 40-223 8.47e-12

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 63.96  E-value: 8.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  40 LRSMGQWAVITGAGDGIGKAYSFELARHGLNVVL-ISRTLEKLQTIAEEIerttGSCVKIVQADFT-REDI---YDHIKE 114
Cdd:PRK08642   1 MQISEQTVLVTGGSRGLGAAIARAFAREGARVVVnYHQSEDAAEALADEL----GDRAIALQADVTdREQVqamFATATE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 115 HLeGLEIGILVNNVGMLPSFFP---SHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPL 190
Cdd:PRK08642  77 HF-GKPITTVVNNALADFSFDGdarKKADDITWEDfQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPVVP 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 153792573 191 YSLYSASKAFVYTFSKALSVEYRDKGIIIQVLT 223
Cdd:PRK08642 156 YHDYTTAKAALLGLTRNLAAELGPYGITVNMVS 188
PRK05693 PRK05693
SDR family oxidoreductase;
47-229 1.25e-11

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 63.66  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEeierttgSCVKIVQADFTREDIYDHIKEHLEGL--EIGIL 124
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAA-------AGFTAVQLDVNDGAALARLAEELEAEhgGLDVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 VNNVG---MLPSFFPSHflstsGESQNLIHCNITSVVKMTQLVLKHMEsRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:PRK05693  77 INNAGygaMGPLLDGGV-----EAMRRQFETNVFAVVGVTRALFPLLR-RSRGLVVNIGSVSGVLVTPFAGAYCASKAAV 150

                        170       180
                 ....*....|....*....|....*...
gi 153792573 202 YTFSKALSVEYRDKGIIIQVLTPYSIST 229
Cdd:PRK05693 151 HALSDALRLELAPFGVQVMEVQPGAIAS 178
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 49-234 1.39e-11

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: 63.84  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  49 ITGAGDGIGKAysfeLARH----GLNVvlISRTLEKLQTIAEEIERTTGSCVKIVQADFTR-EDI---YDHIKEHLEGLE 120
Cdd:cd09805    5 ITGCDSGFGNL----LAKKldslGFTV--LAGCLTKNGPGAKELRRVCSDRLRTLQLDVTKpEQIkraAQWVKEHVGEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 IGILVNNVGMLpSFFPSHFLSTSGESQNLIHCNITSVVKMTQLVLKhMESRRKGLILNISSGAALRPWPLYSLYSASKAF 200
Cdd:cd09805   79 LWGLVNNAGIL-GFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAA 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 153792573 201 VYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKY 234
Cdd:cd09805  157 VEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGN 190
PRK08589 PRK08589
SDR family oxidoreductase;
47-255 1.43e-11

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 63.64  E-value: 1.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLnVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTRE----DIYDHIKEHLEglEIG 122
Cdd:PRK08589   9 AVITGASTGIGQASAIALAQEGA-YVLAVDIAEAVSETVDKI-KSNGGKAKAYHVDISDEqqvkDFASEIKEQFG--RVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ILVNNVGMLPSFFPSHFLSTSGESQnLIHCNITSVVKMTQLVLKHMeSRRKGLILNISSGAAlRPWPLY-SLYSASKAFV 201
Cdd:PRK08589  85 VLFNNAGVDNAAGRIHEYPVDVFDK-IMAVDMRGTFLMTKMLLPLM-MEQGGSIINTSSFSG-QAADLYrSGYNAAKGAV 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 153792573 202 YTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTKTADEFVKESLKYVT 255
Cdd:PRK08589 162 INFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTGTSEDEAGKTFRENQKWMT 215
PRK07024 PRK07024
SDR family oxidoreductase;
43-233 1.72e-11

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 63.02  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEieRTTGSCVKIVQADFTREDIYDHIKEHLE----- 117
Cdd:PRK07024   1 MPLKVFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAAR--LPKAARVSVYAADVRDADALAAAAADFIaahgl 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 118 --------GLEIGIL---------------VNNVGMLPSFFPshFLSTsgesqnlihcnitsvvkmtqlvlkhMESRRKG 174
Cdd:PRK07024  79 pdvvianaGISVGTLteeredlavfrevmdTNYFGMVATFQP--FIAP-------------------------MRAARRG 131

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153792573 175 LILNISSGAALRPWPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:PRK07024 132 TLVGIASVAGVRGLPGAGAYSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPMTA 190
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 44-217 2.05e-11

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 63.10  E-value: 2.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIerttGSCVKIVQADFTREDIYDH----IKEHLEGL 119
Cdd:PRK08265   6 GKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASL----GERARFIATDITDDAAIERavatVVARFGRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EigILVNNVGmlpSFFPSHFLSTSGESQNLIHCNITSVVKMTQLVLKHMeSRRKGLILNISS-----GAALRpWplysLY 194
Cdd:PRK08265  82 D--ILVNLAC---TYLDDGLASSRADWLAALDVNLVSAAMLAQAAHPHL-ARGGGAIVNFTSisakfAQTGR-W----LY 150

                        170       180
                 ....*....|....*....|...
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGI 217
Cdd:PRK08265 151 PASKAAIRQLTRSMAMDLAPDGI 173
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 44-252 2.78e-11

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 62.57  E-value: 2.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFT-REDIYDHIKEhlegleig 122
Cdd:PRK08339   8 GKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSYIVADLTkREDLERTVKE-------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ilVNNVGMLPSFF-------PSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLY 194
Cdd:PRK08339  80 --LKNIGEPDIFFfstggpkPGYFMEMSMEDwEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALS 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTKTADEFVKESLK 252
Cdd:PRK08339 158 NVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLAQDRAKREGKSVEEALQ 215
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 44-227 2.88e-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: 2.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIErtTGSCVKIVQADFTREdiyDHIKEHLEG--LEI 121
Cdd:cd08943    1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQ--GGPRALGVQCDVTSE---AQVQSAFEQavLEF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 G---ILVNNVGMLPSffpSHFLSTSGESQNLIH-CNITSVVKMTQLVLKHMESRRK-GLILNISSGAALRPWPLYSLYSA 196
Cdd:cd08943   76 GgldIVVSNAGIATS---SPIAETSLEDWNRSMdINLTGHFLVSREAFRIMKSQGIgGNIVFNASKNAVAPGPNAAAYSA 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 153792573 197 SKAFVYTFSKALSVEYRDKGIIIQVLTPYSI 227
Cdd:cd08943  153 AKAAEAHLARCLALEGGEDGIRVNTVNPDAV 183
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 48-227 6.27e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 61.62  E-value: 6.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGScVKIVQADF-TREDIYDHIKEHLEGL-EIGILV 125
Cdd:PRK07677   5 IITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQ-VLTVQMDVrNPEDVQKMVEQIDEKFgRIDALI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 126 NNVGmlPSFF-PSHFLSTSGeSQNLIHCNITSVVKMTQLVLKH-MESRRKGLILNISSGAALRPWPLYSLYSASKAFVYT 203
Cdd:PRK07677  84 NNAA--GNFIcPAEDLSVNG-WNSVIDIVLNGTFYCSQAVGKYwIEKGIKGNIINMVATYAWDAGPGVIHSAAAKAGVLA 160

                        170       180
                 ....*....|....*....|....*
gi 153792573 204 FSKALSVEYRDK-GIIIQVLTPYSI 227
Cdd:PRK07677 161 MTRTLAVEWGRKyGIRVNAIAPGPI 185
PRK07985 PRK07985
SDR family oxidoreductase;
41-231 1.19e-10

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 61.16  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  41 RSMGQWAVITGAGDGIGKAYSFELARHGLNVVL--ISRTLEKLQTIAEEIERTTGSCV----KIVQADFTREDIYDHIKE 114
Cdd:PRK07985  46 RLKDRKALVTGGDSGIGRAAAIAYAREGADVAIsyLPVEEEDAQDVKKIIEECGRKAVllpgDLSDEKFARSLVHEAHKA 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 115 hLEGLEIGILV-------NNVGMLpsffpshflsTSGESQNLIHCNITSVVKMTQLVLKHMESRRKglILNISSGAALRP 187
Cdd:PRK07985 126 -LGGLDIMALVagkqvaiPDIADL----------TSEQFQKTFAINVFALFWLTQEAIPLLPKGAS--IITTSSIQAYQP 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 153792573 188 WPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK07985 193 SPHLLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAL 236
PRK08628 PRK08628
SDR family oxidoreductase;
48-231 1.23e-10

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 60.74  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTiAEEIERTTGScVKIVQADFTRED-IYDHIKEHLEGL-EIGILV 125
Cdd:PRK08628  11 IVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEF-AEELRALQPR-AEFVQVDLTDDAqCRDAVEQTVAKFgRIDGLV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 126 NNVGMLPSFfpsHFLSTSGESQNLIHCNITSVVKMTQLVLKHMESRRkGLILNISSGAALRPWPLYSLYSASKAFVYTFS 205
Cdd:PRK08628  89 NNAGVNDGV---GLEAGREAFVASLERNLIHYYVMAHYCLPHLKASR-GAIVNISSKTALTGQGGTSGYAAAKGAQLALT 164

                        170       180
                 ....*....|....*....|....*.
gi 153792573 206 KALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK08628 165 REWAVALAKDGVRVNAVIPAEVMTPL 190
PRK07577 PRK07577
SDR family oxidoreductase;
47-231 1.23e-10

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 60.51  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTleklqtiaeEIERTTGSCVKIVQADFTR-EDIYDHIKEHlegLEIGILV 125
Cdd:PRK07577   6 VLVTGATKGIGLALSLRLANLGHQVIGIARS---------AIDDFPGELFACDLADIEQtAATLAQINEI---HPVDAIV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 126 NNVGM-LPSFFPSHFLSTsgeSQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISS----GAALRpwplySLYSASKAF 200
Cdd:PRK07577  74 NNVGIaLPQPLGKIDLAA---LQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSraifGALDR-----TSYSAAKSA 145

                        170       180       190
                 ....*....|....*....|....*....|.
gi 153792573 201 VYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK07577 146 LVGCTRTWALELAEYGITVNAVAPGPIETEL 176
PRK09135 PRK09135
pteridine reductase; Provisional
 47-211 1.43e-10

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 60.33  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRT-LEKLQTIAEEIERTTGSCVKIVQADFTR----EDIYDHIKEHLEGLEI 121
Cdd:PRK09135   9 ALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADALAAELNALRPGSAAALQADLLDpdalPELVAACVAAFGRLDA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 giLVNNVGmlpSFFPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMeSRRKGLILNISSGAALRPWPLYSLYSASKAF 200
Cdd:PRK09135  89 --LVNNAS---SFYPTPLGSITEAQwDDLFASNLKAPFFLSQAAAPQL-RKQRGAIVNITDIHAERPLKGYPVYCAAKAA 162

                        170
                 ....*....|.
gi 153792573 201 VYTFSKALSVE 211
Cdd:PRK09135 163 LEMLTRSLALE 173
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 47-232 1.49e-10

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: 60.55  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLIS-RTLEKLQTIAEEIERTTGSCVkIVQADFT----REDIYDHIKEHLEGLEi 121
Cdd:cd05337    4 AIVTGASRGIGRAIATELAARGFDIAINDlPDDDQATEVVAEVLAAGRRAI-YFQADIGelsdHEALLDQAWEDFGRLD- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 gILVNNVGMLPSFFpSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRK------GLILNISSGAALRPWPLYSLY 194
Cdd:cd05337   82 -CLVNNAGIAVRPR-GDLLDLTEDSfDRLIAINLRGPFFLTQAVARRMVEQPDrfdgphRSIIFVTSINAYLVSPNRGEY 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:cd05337  160 CISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMT 197
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 43-238 1.65e-10

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: 60.38  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERttgscVKIVQADFTRE-DIYDHIKEHLEGL-E 120
Cdd:cd05371    1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAKLGDN-----CRFVPVDVTSEkDVKAALALAKAKFgR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 IGILVNNVGMLPSF-------FPSHFLStsgESQNLIHCNITSVVKMTQLVLKHM------ESRRKGLILNISSGAALRP 187
Cdd:cd05371   76 LDIVVNCAGIAVAAktynkkgQQPHSLE---LFQRVINVNLIGTFNVIRLAAGAMgknepdQGGERGVIINTASVAAFEG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153792573 188 WPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNK 238
Cdd:cd05371  153 QIGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEK 203
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 49-224 1.67e-10

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 60.15  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  49 ITGAGDGIGKAYSFELARHGLNVVLISRTLE---KLQ----TIAEEIERTTGSCVKIVqADFTRED-IYDHIKEHLEGL- 119
Cdd:cd09762    8 ITGASRGIGKAIALKAARDGANVVIAAKTAEphpKLPgtiyTAAEEIEAAGGKALPCI-VDIRDEDqVRAAVEKAVEKFg 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIGILVNNVGMLPSffpSHFLSTSGESQNLIH-CNITSVVKMTQLVLKHMESRRKGLILNISSGAALRP--WPLYSLYSA 196
Cdd:cd09762   87 GIDILVNNASAISL---TGTLDTPMKRYDLMMgVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLNPkwFKNHTAYTM 163

                        170       180
                 ....*....|....*....|....*...
gi 153792573 197 SKAFVYTFSKALSVEYRDKGIIIQVLTP 224
Cdd:cd09762  164 AKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PRK06128 PRK06128
SDR family oxidoreductase;
39-231 1.75e-10

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 60.64  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  39 FLRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLisRTLEKLQTIAEEIER---TTGSCVKIVQADFTRE----DIYDH 111
Cdd:PRK06128  50 FGRLQGRKALITGADSGIGRATAIAFAREGADIAL--NYLPEEEQDAAEVVQliqAEGRKAVALPGDLKDEafcrQLVER 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 112 IKEHLEGLEigILVNNVGMLPSFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESrrKGLILNISSGAALRPWPLY 191
Cdd:PRK06128 128 AVKELGGLD--ILVNIAGKQTAVKDIADITTE-QFDATFKTNVYAMFWLCKAAIPHLPP--GASIINTGSIQSYQPSPTL 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 153792573 192 SLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK06128 203 LDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPL 242
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 44-248 2.31e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 60.05  E-value: 2.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISrtLEKLQTiAEE----IERTTGSCVKIV----QADFTREDIYDHIKEh 115
Cdd:PRK06701  46 GKVALITGGDSGIGRAVAVLFAKEGADIAIVY--LDEHED-ANEtkqrVEKEGVKCLLIPgdvsDEAFCKDAVEETVRE- 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 116 LEGLEigILVNNVGmlpsfFPSHFLS----TSGESQNLIHCNITSVVKMTQLVLKHMESrrKGLILNISSGAALRPWPLY 191
Cdd:PRK06701 122 LGRLD--ILVNNAA-----FQYPQQSlediTAEQLDKTFKTNIYSYFHMTKAALPHLKQ--GSAIINTGSITGYEGNETL 192

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 153792573 192 SLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMtkylnNKMTKTADEFVK 248
Cdd:PRK06701 193 IDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPL-----IPSDFDEEKVSQ 244
PRK08340 PRK08340
SDR family oxidoreductase;
48-230 3.68e-10

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 59.43  E-value: 3.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGscVKIVQADFT-REDIYDHIKEHLEGL-EIGILV 125
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYGE--VYAVKADLSdKDDLKNLVKEAWELLgGIDALV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 126 ---NNVGMLPSFFPSHFLSTSGESQnLIHCnITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVY 202
Cdd:PRK08340  82 wnaGNVRCEPCMLHEAGYSDWLEAA-LLHL-VAPGYLTTLLIQAWLEKKMKGVLVYLSSVSVKEPMPPLVLADVTRAGLV 159

                        170       180
                 ....*....|....*....|....*...
gi 153792573 203 TFSKALSVEYRDKGIIIQVLTPYSISTP 230
Cdd:PRK08340 160 QLAKGVSRTYGGKGIRAYTVLLGSFDTP 187
PRK07023 PRK07023
SDR family oxidoreductase;
47-231 4.00e-10

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 58.87  E-value: 4.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISR------------TLEKLQTIAEEIERTTGSCVKIVQADFtrediydhike 114
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPGIAVLGVARsrhpslaaaageRLAEVELDLSDAAAAAAWLAGDLLAAF----------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 115 hLEGLEIGILVNNVGMLPSFFPSHFLsTSGESQNLIHCNITSVVKMTQLVLKHME---SRRkglILNISSGAALRPWPLY 191
Cdd:PRK07023  73 -VDGASRVLLINNAGTVEPIGPLATL-DAAAIARAVGLNVAAPLMLTAALAQAASdaaERR---ILHISSGAARNAYAGW 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 153792573 192 SLYSASKAFVYTFSKALSVEyRDKGIIIQVLTPYSISTPM 231
Cdd:PRK07023 148 SVYCATKAALDHHARAVALD-ANRALRIVSLAPGVVDTGM 186
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 47-231 4.19e-10

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 59.26  E-value: 4.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573   47 AVITGAGDGIGKAYSFELARHGLNVVLISR-----TLEKLQTIAEEIERTTGSC---VKIVQADFTREDIYDHI----KE 114
Cdd:TIGR04504   4 ALVTGAARGIGAATVRRLAADGWRVVAVDLcaddpAVGYPLATRAELDAVAAACpdqVLPVIADVRDPAALAAAvalaVE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  115 HLEGLEIGILVNNV--GMLPsffpsHFLSTSGESQNLIHCNITSVVKMTQLVLKHMESR---RKGLILNISSGAALRPWP 189
Cdd:TIGR04504  84 RWGRLDAAVAAAGViaGGRP-----LWETTDAELDLLLDVNLRGVWNLARAAVPAMLARpdpRGGRFVAVASAAATRGLP 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 153792573  190 LYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:TIGR04504 159 HLAAYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAM 200
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
44-245 4.93e-10

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 58.73  E-value: 4.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISrTLEKLQTIaEEIErTTGSCVKIVQADFTREDIYDHIKEHL--EGLEI 121
Cdd:PRK08993  10 GKVAVVTGCDTGLGQGMALGLAEAGCDIVGIN-IVEPTETI-EQVT-ALGRRFLSLTADLRKIDGIPALLERAvaEFGHI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMLPSFFPSHFlsTSGESQNLIHCNITSVVKMTQLVLKH-MESRRKGLILNISSGAALRPWPLYSLYSASKAF 200
Cdd:PRK08993  87 DILVNNAGLIRREDAIEF--SEKDWDDVMNLNIKSVFFMSQAAAKHfIAQGNGGKIINIASMLSFQGGIRVPSYTASKSG 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 153792573 201 VYTFSKALSVEYRDKGIIIQVLTPYSISTpmtkylNNKMTKTADE 245
Cdd:PRK08993 165 VMGVTRLMANEWAKHNINVNAIAPGYMAT------NNTQQLRADE 203
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 44-232 5.01e-10

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 59.85  E-value: 5.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVL--ISRTLEKLQTIAEEIERTTgscvkiVQADFTREDIYDHIKEHLE--GL 119
Cdd:PRK08261 210 GKVALVTGAARGIGAAIAEVLARDGAHVVCldVPAAGEALAAVANRVGGTA------LALDITAPDAPARIAEHLAerHG 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIGILVNNVG---------MLPSFFPShflstsgesqnLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPL 190
Cdd:PRK08261 284 GLDIVVHNAGitrdktlanMDEARWDS-----------VLAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRG 352

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 153792573 191 YSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:PRK08261 353 QTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMT 394
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 44-232 6.97e-10

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 58.26  E-value: 6.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLqtiAEEIERTTgscVKIVQADFT-REDIYDHIKE-HLEGLEI 121
Cdd:PRK06463   7 GKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENE---AKELREKG---VFTIKCDVGnRDQVKKSKEVvEKEFGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMlpsFFPSHFLSTSGESQN-LIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPL-YSLYSASKA 199
Cdd:PRK06463  81 DVLVNNAGI---MYLMPFEEFDEEKYNkMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGTAAEgTTFYAITKA 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:PRK06463 158 GIIILTRRLAFELGKYGIRVNAVAPGWVETDMT 190
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 44-245 8.32e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 58.53  E-value: 8.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVL--ISRTLEKL-------QTIAEEIERTTGSCV----KIVQADfTREDIYD 110
Cdd:PRK07791   6 GRVVIVTGAGGGIGRAHALAFAAEGARVVVndIGVGLDGSasggsaaQAVVDEIVAAGGEAVangdDIADWD-GAANLVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 111 HIKEHLEGLEigILVNNVGMLPSFFpshFLSTSGESQNLIhcnITSVVKMTQLVLKHMESRRKGL----------ILNIS 180
Cdd:PRK07791  85 AAVETFGGLD--VLVNNAGILRDRM---IANMSEEEWDAV---IAVHLKGHFATLRHAAAYWRAEskagravdarIINTS 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792573 181 SGAALRPWPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPySISTPMTKYLNNKMTKTADE 245
Cdd:PRK07791 157 SGAGLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP-AARTRMTETVFAEMMAKPEE 220
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 44-224 9.76e-10

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 57.87  E-value: 9.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAG--DGIGKAYSFELARHGLNVVLI-----SRTL-------EKLQtIAEEIeRTTGSCVKIVQADFTREDIY 109
Cdd:PRK12859   6 NKVAVVTGVSrlDGIGAAICKELAEAGADIFFTywtayDKEMpwgvdqdEQIQ-LQEEL-LKNGVKVSSMELDLTQNDAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 110 ----DHIKEHLEglEIGILVNNVGMlpsffpshflSTSGESQNLI------HC--NITSVVKMTQLVLKHMESRRKGLIL 177
Cdd:PRK12859  84 kellNKVTEQLG--YPHILVNNAAY----------STNNDFSNLTaeeldkHYmvNVRATTLLSSQFARGFDKKSGGRII 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 153792573 178 NISSGAALRPWPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTP 224
Cdd:PRK12859 152 NMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINP 198
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 49-229 1.15e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 58.00  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  49 ITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEeierTTGSCVKIVQADFT-REDIYDHIKEHLEGL-EIGILVN 126
Cdd:PRK06180   9 ITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEA----LHPDRALARLLDVTdFDAIDAVVADAEATFgPIDVLVN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 127 NVGMlpsffpSHF----LSTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVY 202
Cdd:PRK06180  85 NAGY------GHEgaieESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALE 158

                        170       180
                 ....*....|....*....|....*..
gi 153792573 203 TFSKALSVEYRDKGIIIQVLTPYSIST 229
Cdd:PRK06180 159 GISESLAKEVAPFGIHVTAVEPGSFRT 185
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 44-241 1.27e-09

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 57.78  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLI--SRTLEKLQTIaEEIERTTGSCVKI---VQADFTREDIYDHIKEHLEG 118
Cdd:PRK12747   4 GKVALVTGASRGIGRAIAKRLANDGALVAIHygNRKEEAEETV-YEIQSNGGSAFSIganLESLHGVEALYSSLDNELQN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 ----LEIGILVNNVGMLPSFFPSHflSTSGESQNLIHCNITSVVKMTQLVLKHMesRRKGLILNISSGAALRPWPLYSLY 194
Cdd:PRK12747  83 rtgsTKFDILINNAGIGPGAFIEE--TTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLPDFIAY 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM-TKYLNNKMTK 241
Cdd:PRK12747 159 SMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMnAELLSDPMMK 206
PRK06123 PRK06123
SDR family oxidoreductase;
47-231 1.34e-09

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 57.48  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVL-ISRTLEKLQTIAEEIERTTGSCVKiVQADFTREDIYDHIKEHLEGlEIG--- 122
Cdd:PRK06123   5 MIITGASRGIGAATALLAAERGYAVCLnYLRNRDAAEAVVQAIRRQGGEALA-VAADVADEADVLRLFEAVDR-ELGrld 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ILVNNVGMLPSFFPSHFLStSGESQNLIHCNITSVVKMTQLVLKHMESR---RKGLILNISSGAALRPWP-LYSLYSASK 198
Cdd:PRK06123  83 ALVNNAGILEAQMRLEQMD-AARLTRIFATNVVGSFLCAREAVKRMSTRhggRGGAIVNVSSMAARLGSPgEYIDYAASK 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK06123 162 GAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEI 194
PRK07074 PRK07074
SDR family oxidoreductase;
43-230 1.58e-09

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 57.47  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEI--ERTTGscvkiVQADFTRE-DIYDHIKEHLEGL 119
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALgdARFVP-----VACDLTDAaSLAAALANAAAER 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 -EIGILVNNVGMLPSffpSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISS--GAALRPWPLYSlys 195
Cdd:PRK07074  76 gPVDVLVANAGAARA---ASLHDTTPASwRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSvnGMAALGHPAYS--- 149

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 196 ASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTP 230
Cdd:PRK07074 150 AAKAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQ 184
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 47-241 1.74e-09

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: 56.37  E-value: 1.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISrtleklqtiaeeierttgscvkivqadfTREDIydhikehlegleigiLVN 126
Cdd:cd02266    1 VLVTGGSGGIGGAIARWLASRGSPKVLVV----------------------------SRRDV---------------VVH 37

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 127 NVGmLPSFFPSHFLSTSGeSQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYTFSK 206
Cdd:cd02266   38 NAA-ILDDGRLIDLTGSR-IERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLAQ 115

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 207 ALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTK 241
Cdd:cd02266  116 QWASEGWGNGLPATAVACGTWAGSGMAKGPVAPEE 150
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 44-232 2.03e-09

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 56.99  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTiAEEIERTTGSCVKIVQADFTREdiyDHIKEHLEGLE--- 120
Cdd:PRK07097  10 GKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDK-GLAAYRELGIEAHGYVCDVTDE---DGVQAMVSQIEkev 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 --IGILVNNVGMLPSfFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASK 198
Cdd:PRK07097  86 gvIDILVNNAGIIKR-IPMLEMSAE-DFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAAK 163

                        170       180       190
                 ....*....|....*....|....*....|....
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:PRK07097 164 GGLKMLTKNIASEYGEANIQCNGIGPGYIATPQT 197
PRK08278 PRK08278
SDR family oxidoreductase;
44-235 2.84e-09

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 56.84  E-value: 2.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLE---KLQ----TIAEEIERTTGSCVKIVqADFTRED-IYDHIKEH 115
Cdd:PRK08278   6 GKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEphpKLPgtihTAAEEIEAAGGQALPLV-GDVRDEDqVAAAVAKA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 116 LEGL-EIGILVNNVGMLpsfFPSHFLSTSGESQNLIH-CNITSVVKMTQLVLKHMESRRKGLILNISSGAALRP--WPLY 191
Cdd:PRK08278  85 VERFgGIDICVNNASAI---NLTGTEDTPMKRFDLMQqINVRGTFLVSQACLPHLKKSENPHILTLSPPLNLDPkwFAPH 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 153792573 192 SLYSASKaFVYTF-SKALSVEYRDKGIIIQVLTPYS-ISTPMTKYL 235
Cdd:PRK08278 162 TAYTMAK-YGMSLcTLGLAEEFRDDGIAVNALWPRTtIATAAVRNL 206
PRK06124 PRK06124
SDR family oxidoreductase;
44-224 3.41e-09

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 56.26  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGScvkivqADFTREDIYDH----------IK 113
Cdd:PRK06124  11 GQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGA------AEALAFDIADEeavaaafariDA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 114 EHlegLEIGILVNNVGM-----LPSFFPSHFLStsgesqnLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPW 188
Cdd:PRK06124  85 EH---GRLDILVNNVGArdrrpLAELDDAAIRA-------LLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVAR 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 153792573 189 PLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTP 224
Cdd:PRK06124 155 AGDAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAP 190
PRK06101 PRK06101
SDR family oxidoreductase;
49-232 4.41e-09

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 56.03  E-value: 4.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  49 ITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAeeierTTGSCVKIVQADFTRediYDHIKEHLEGLEigilvnnv 128
Cdd:PRK06101   6 ITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELH-----TQSANIFTLAFDVTD---HPGTKAALSQLP-------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 129 gmlpsFFPSHFLSTSGES-------------QNLIHCNITSVVKMTQLVLKHMESRRKGLIL-NISSGAALrpwPLYSLY 194
Cdd:PRK06101  70 -----FIPELWIFNAGDCeymddgkvdatlmARVFNVNVLGVANCIEGIQPHLSCGHRVVIVgSIASELAL---PRAEAY 141

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMT 232
Cdd:PRK06101 142 GASKAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLT 179
PRK07856 PRK07856
SDR family oxidoreductase;
44-212 5.23e-09

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 55.71  E-value: 5.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTleklqtiaeEIERTTGScvkivQADFTREDIYDH--IKEHLEGLE- 120
Cdd:PRK07856   6 GRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRR---------APETVDGR-----PAEFHAADVRDPdqVAALVDAIVe 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 ----IGILVNNVGMLPsffpshFLSTSGESQNL----IHCNITSVVKMTQLVLKHMESR-RKGLILNISSGAALRPWPLY 191
Cdd:PRK07856  72 rhgrLDVLVNNAGGSP------YALAAEASPRFhekiVELNLLAPLLVAQAANAVMQQQpGGGSIVNIGSVSGRRPSPGT 145

                        170       180
                 ....*....|....*....|.
gi 153792573 192 SLYSASKAFVYTFSKALSVEY 212
Cdd:PRK07856 146 AAYGAAKAGLLNLTRSLAVEW 166
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 43-235 6.40e-09

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 55.81  E-value: 6.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKI-VQADFTRE-DIYDHIKEHLEGL- 119
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEGMAYgFGADATSEqSVLALSRGVDEIFg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIGILVNNVGMLPSFFPSHFlsTSGESQNLIHCNITSVVKMTQLVLKHM-ESRRKGLILNISSGAALRPWPLYSLYSASK 198
Cdd:PRK12384  81 RVDLLVYNAGIAKAAFITDF--QLGDFDRSLQVNLVGYFLCAREFSRLMiRDGIQGRIIQINSKSGKVGSKHNSGYSAAK 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTPYS-ISTPMTKYL 235
Cdd:PRK12384 159 FGGVGLTQSLALDLAEYGITVHSLMLGNlLKSPMFQSL 196
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 40-224 8.21e-09

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 55.47  E-value: 8.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  40 LRSMGQWAVITGA--GDGIGKAYSFELARHGLNVVL------------ISRTLEKLQtIAEEIERTtGSCVKIVQADFTR 105
Cdd:PRK12748   1 LPLMKKIALVTGAsrLNGIGAAVCRRLAAKGIDIFFtywspydktmpwGMHDKEPVL-LKEEIESY-GVRCEHMEIDLSQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 106 EDIYDHIKEHLEGlEIG---ILVNNvgmlpsffpsHFLSTSGESQNLI------H--CNITSVVKMTQLVLKHMESRRKG 174
Cdd:PRK12748  79 PYAPNRVFYAVSE-RLGdpsILINN----------AAYSTHTRLEELTaeqldkHyaVNVRATMLLSSAFAKQYDGKAGG 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 153792573 175 LILNISSGAALRPWPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTP 224
Cdd:PRK12748 148 RIINLTSGQSLGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNP 197
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 146-244 1.41e-08

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 54.25  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 146 SQNLIhcniTSVVKmTQLVLKHMESrrKGLILNISSGAALRPWPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLT-- 223
Cdd:cd05334   98 KQNLW----TSFIA-SHLATKHLLS--GGLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSLAAENSGLPAGSTANAil 170

                         90       100
                 ....*....|....*....|.
gi 153792573 224 PYSISTPMtkylNNKMTKTAD 244
Cdd:cd05334  171 PVTLDTPA----NRKAMPDAD 187
PRK07062 PRK07062
SDR family oxidoreductase;
44-217 2.55e-08

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 53.89  E-value: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKL-QTIAEEIERTTGSCVKIVQADFTRED----IYDHIKEHLEG 118
Cdd:PRK07062   8 GRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLaSAEARLREKFPGARLLAARCDVLDEAdvaaFAAAVEARFGG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEigILVNNVGmlpSFFPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSAS 197
Cdd:PRK07062  88 VD--MLVNNAG---QGRVSTFADTTDDAwRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATSAA 162

                        170       180
                 ....*....|....*....|
gi 153792573 198 KAFVYTFSKALSVEYRDKGI 217
Cdd:PRK07062 163 RAGLLNLVKSLATELAPKGV 182
PRK12744 PRK12744
SDR family oxidoreductase;
44-230 4.91e-08

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 52.82  E-value: 4.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIE---RTTGSCVKIVQADFTR----EDIYDHIKEHL 116
Cdd:PRK12744   8 GKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAEETVaavKAAGAKAVAFQADLTTaaavEKLFDDAKAAF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 117 EGLEIGIlvNNVGMLpsfFPSHFLSTS-GESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPwpLYSLYS 195
Cdd:PRK12744  88 GRPDIAI--NTVGKV---LKKPIVEISeAEYDEMFAVNSKSAFFFIKEAGRHLNDNGKIVTLVTSLLGAFTP--FYSAYA 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792573 196 ASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTP 230
Cdd:PRK12744 161 GSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTP 195
PRK08703 PRK08703
SDR family oxidoreductase;
48-230 5.57e-08

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 52.63  E-value: 5.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADF--TREDIYDH----IKEHLEGLEI 121
Cdd:PRK08703  10 LVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPEPFAIRFDLmsAEEKEFEQfaatIAEATQGKLD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GIlVNNVGMLPSFFPSHFlSTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:PRK08703  90 GI-VHCAGYFYALSPLDF-QTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGGFGASKAAL 167

                        170       180       190
                 ....*....|....*....|....*....|
gi 153792573 202 YTFSKALSVEY-RDKGIIIQVLTPYSISTP 230
Cdd:PRK08703 168 NYLCKVAADEWeRFGNLRANVLVPGPINSP 197
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 44-245 6.01e-08

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: 52.48  E-value: 6.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIErTTGSCVKiVQADFTREDIYDHIKEHLEGLE--I 121
Cdd:cd08942    6 GKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELS-AYGECIA-IPADLSSEEGIEALVARVAERSdrL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGM-----LPSFFPSHFlstsgesQNLIHCNITSVVKMTQLVL----KHMESRRKGLILNISSGAALR-PWPLY 191
Cdd:cd08942   84 DVLVNNAGAtwgapLEAFPESGW-------DKVMDINVKSVFFLTQALLpllrAAATAENPARVINIGSIAGIVvSGLEN 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 153792573 192 SLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKY-LNNKMTKTADE 245
Cdd:cd08942  157 YSYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFlLNDPAALEAEE 211
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 44-234 1.41e-07

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 51.70  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIV-QADFTRED-IYDHIKEHL-EGLE 120
Cdd:cd09807    1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLNHEVIVrHLDLASLKsIRAFAAEFLaEEDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 IGILVNNVG--MLPsffpsHFLSTSG-ESQnlIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAAL------------ 185
Cdd:cd09807   81 LDVLINNAGvmRCP-----YSKTEDGfEMQ--FGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKagkinfddlnse 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153792573 186 RPWPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKY 234
Cdd:cd09807  154 KSYNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGRH 202
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
44-235 1.75e-07

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 51.44  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISrtLEKLQTIAEEIErTTGSCVKIVQADFTREDIYDHI-KEHLEGL-EI 121
Cdd:PRK12481   8 GKVAIITGCNTGLGQGMAIGLAKAGADIVGVG--VAEAPETQAQVE-ALGRKFHFITADLIQQKDIDSIvSQAVEVMgHI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGMLPSffpSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRK-GLILNISSGAALRPWPLYSLYSASKA 199
Cdd:PRK12481  85 DILINNAGIIRR---QDLLEFGNKDwDDVININQKTVFFLSQAVAKQFVKQGNgGKIINIASMLSFQGGIRVPSYTASKS 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYL 235
Cdd:PRK12481 162 AVMGLTRALATELSQYNINVNAIAPGYMATDNTAAL 197
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 106-257 2.34e-07

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: 50.65  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 106 EDIYDHIKEHLEGLEIgiLVNNvgmlpSFFPSHFLSTSGESQNLIHCNITSVV----KMTQLVLKHMESRRKGLILNISS 181
Cdd:cd05361   60 EELVDAVLQAGGAIDV--LVSN-----DYIPRPMNPIDGTSEADIRQAFEALSifpfALLQAAIAQMKKAGGGSIIFITS 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792573 182 GAALRPWPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPmtKYLNNKMTKTADEFVKESLKYVTIG 257
Cdd:cd05361  133 AVPKKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSP--TYFPTSDWENNPELRERVKRDVPLG 206
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 36-228 2.52e-07

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 50.72  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  36 PSSFLRSMGQWAVITGAGDGI--GKAYSFelARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADfTREdiYDHIK 113
Cdd:PRK07576   1 MTTMFDFAGKNVVVVGGTSGInlGIAQAF--ARAGANVAVASRSQEKVDAAVAQL-QQAGPEGLGVSAD-VRD--YAAVE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 114 EHLEGL-----EIGILVN----NvgmlpsfFPShflSTSGESQNlihcNITSVVKMTQL----VLK----HMesRRKGL- 175
Cdd:PRK07576  75 AAFAQIadefgPIDVLVSgaagN-------FPA---PAAGMSAN----GFKTVVDIDLLgtfnVLKaaypLL--RRPGAs 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153792573 176 ILNISSGAALRPWPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSIS 228
Cdd:PRK07576 139 IIQISAPQAFVPMPMQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPGPIA 191
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 44-206 3.74e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 50.39  E-value: 3.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGL-NVVLISRTLEKLQTIAEEIErTTGSCVKIVQADFTR-EDIYDHIKEHLEGL-E 120
Cdd:PRK06198   6 GKVALVTGGTQGLGAAIARAFAERGAaGLVICGRNAEKGEAQAAELE-ALGAKAVFVQADLSDvEDCRRVVAAADEAFgR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 121 IGILVNNVGML---------PSFFPSHFlstsgesqnliHCNITSVVKMTQLVLKHMESRR-KGLILNISSGAALRPWPL 190
Cdd:PRK06198  85 LDALVNAAGLTdrgtildtsPELFDRHF-----------AVNVRAPFFLMQEAIKLMRRRKaEGTIVNIGSMSAHGGQPF 153

                        170
                 ....*....|....*.
gi 153792573 191 YSLYSASKAFVYTFSK 206
Cdd:PRK06198 154 LAAYCASKGALATLTR 169
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 44-129 5.63e-07

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 49.90  E-value: 5.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGS---CVKIVQADFTREdIYDHIKE-HLEGL 119
Cdd:cd09808    1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETESGNqniFLHIVDMSDPKQ-VWEFVEEfKEEGK 79

                         90
                 ....*....|
gi 153792573 120 EIGILVNNVG 129
Cdd:cd09808   80 KLHVLINNAG 89
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 44-131 7.53e-07

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 49.78  E-value: 7.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVL--ISRTLEKlQTIAEEIeRTTGSCVKIVQADFTREDIYDHIKEHLEGL-E 120
Cdd:PRK07792  12 GKVAVVTGAAAGLGRAEALGLARLGATVVVndVASALDA-SDVLDEI-RAAGAKAVAVAGDISQRATADELVATAVGLgG 89

                         90
                 ....*....|.
gi 153792573 121 IGILVNNVGML 131
Cdd:PRK07792  90 LDIVVNNAGIT 100
PRK06194 PRK06194
hypothetical protein; Provisional
 44-229 8.70e-07

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 49.63  E-value: 8.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIeRTTGSCVKIVQADFTREdiydhikEHLEGL---- 119
Cdd:PRK06194   6 GKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAEL-RAQGAEVLGVRTDVSDA-------AQVEALadaa 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 -----EIGILVNN-----VGMLpsffpshFLSTSGESQNLIHCNITSVVKMTQLVLKHMESRRK------GLILNISSGA 183
Cdd:PRK06194  78 lerfgAVHLLFNNagvgaGGLV-------WENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEkdpayeGHIVNTASMA 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 153792573 184 ALRPWPLYSLYSASKAFVYTFSKALsveYRDKGIIIQ-----VLTPYSIST 229
Cdd:PRK06194 151 GLLAPPAMGIYNVSKHAVVSLTETL---YQDLSLVTDqvgasVLCPYFVPT 198
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 44-212 9.51e-07

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 49.92  E-value: 9.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSC-VKIVQADFTREDIyDHIKEHLEGLEIG 122
Cdd:COG3347  425 GRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGADaVDATDVDVTAEAA-VAAAFGFAGLDIG 503

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ILVNNVGMLPSFFPSHFLSTSGESQNLihcNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVY 202
Cdd:COG3347  504 GSDIGVANAGIASSSPEEETRLSFWLN---NFAHLSTGQFLVARAAFQGTGGQGLGGSSVFAVSKNAAAAAYGAAAAATA 580

                        170
                 ....*....|
gi 153792573 203 TFSKALSVEY 212
Cdd:COG3347  581 KAAAQHLLRA 590
PRK07831 PRK07831
SDR family oxidoreductase;
43-235 1.10e-06

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 48.88  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGA-GDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTG-SCVKIVQADFTRED----IYDHIKEHL 116
Cdd:PRK07831  16 AGKVVLVTAAaGTGIGSATARRALEEGARVVISDIHERRLGETADELAAELGlGRVEAVVCDVTSEAqvdaLIDAAVERL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 117 EGLEIgiLVNNVG---------MlpsffpshflsTSGESQNLIHCNITSVVKMTQLVLKHMESR-RKGLILNISSGAALR 186
Cdd:PRK07831  96 GRLDV--LVNNAGlggqtpvvdM-----------TDDEWSRVLDVTLTGTFRATRAALRYMRARgHGGVIVNNASVLGWR 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153792573 187 PWPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPysiSTPMTKYL 235
Cdd:PRK07831 163 AQHGQAHYAAAKAGVMALTRCSALEAAEYGVRINAVAP---SIAMHPFL 208
PRK08862 PRK08862
SDR family oxidoreductase;
49-181 1.61e-06

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 48.18  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  49 ITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTREDI---YDHIKEHLeGLEIGILV 125
Cdd:PRK08862  10 ITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCSALTDNVYSFQLKDFSQESIrhlFDAIEQQF-NRAPDVLV 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153792573 126 NNV--GMLPSFFPShflSTSGESQNLIHCNITSVVKMTQLVLKHMESR-RKGLILNISS 181
Cdd:PRK08862  89 NNWtsSPLPSLFDE---QPSESFIQQLSSLASTLFTYGQVAAERMRKRnKKGVIVNVIS 144
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 48-107 1.72e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 48.65  E-value: 1.72e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIE-RTTGSCVKIVQADFTRED 107
Cdd:PRK05875  11 LVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEaLKGAGAVRYEPADVTDED 71
PLN02253 PLN02253
xanthoxin dehydrogenase
 36-229 1.84e-06

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 48.28  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  36 PSSFLRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCvkIVQADFTRED----IYDH 111
Cdd:PLN02253  10 SLPSQRLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVC--FFHCDVTVEDdvsrAVDF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 112 IKEHLEGLEigILVNNVGMLPSFFPSHFLSTSGESQNLIHCNitsvVKMTQLVLKH----MESRRKGLILNISSGAA--- 184
Cdd:PLN02253  88 TVDKFGTLD--IMVNNAGLTGPPCPDIRNVELSEFEKVFDVN----VKGVFLGMKHaariMIPLKKGSIVSLCSVASaig 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 153792573 185 -LRPwplySLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSIST 229
Cdd:PLN02253 162 gLGP----HAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPT 203
PRK05854 PRK05854
SDR family oxidoreductase;
44-132 2.00e-06

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 48.52  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTT-GSCVKIVQADFTREDIYDHIKEHL--EGLE 120
Cdd:PRK05854  14 GKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTAVpDAKLSLRALDLSSLASVAALGEQLraEGRP 93

                         90
                 ....*....|...
gi 153792573 121 IGILVNNVG-MLP 132
Cdd:PRK05854  94 IHLLINNAGvMTP 106
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 44-210 2.91e-06

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: 47.57  E-value: 2.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKlqtiAEEIERTTGSCVKIVQADFTRED-IYDHIKEHLEGLE-I 121
Cdd:cd09761    1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEER----GADFAEAEGPNLFFVHGDVADETlVKFVVYAMLEKLGrI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVG-MLPSFFPSHFLstsGESQNLIHCNITSVVKMTQLVLKHMeSRRKGLILNISSGAALRPWPLYSLYSASKAF 200
Cdd:cd09761   77 DVLVNNAArGSKGILSSLLL---EEWDRILSVNLTGPYELSRYCRDEL-IKNKGRIINIASTRAFQSEPDSEAYAASKGG 152

                        170
                 ....*....|
gi 153792573 201 VYTFSKALSV 210
Cdd:cd09761  153 LVALTHALAM 162
PRK12746 PRK12746
SDR family oxidoreductase;
44-224 3.13e-06

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 47.72  E-value: 3.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHG-LNVVLISRTLEKLQTIAEEIERTTGSCVkIVQADFTREDIYDHIKEHLEG---- 118
Cdd:PRK12746   6 GKVALVTGASRGIGRAIAMRLANDGaLVAIHYGRNKQAADETIREIESNGGKAF-LIEADLNSIDGVKKLVEQLKNelqi 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 ----LEIGILVNNVGmlpsffpshfLSTSGESQN--------LIHCNITSVVKMTQLVLKHMesRRKGLILNISSGAALR 186
Cdd:PRK12746  85 rvgtSEIDILVNNAG----------IGTQGTIENtteeifdeIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRL 152

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 153792573 187 PWPLYSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTP 224
Cdd:PRK12746 153 GFTGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMP 190
PRK06482 PRK06482
SDR family oxidoreductase;
49-229 3.78e-06

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 47.42  E-value: 3.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  49 ITGAGDGIGKAYSFELARHGLNVVlisRTLEKLQTIAEEIERTtGSCVKIVQADFTRED-IYDHIKEHLEGLE-IGILVN 126
Cdd:PRK06482   7 ITGASSGFGRGMTERLLARGDRVA---ATVRRPDALDDLKARY-GDRLWVLQLDVTDSAaVRAVVDRAFAALGrIDVVVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 127 NVGMlPSFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYTFSK 206
Cdd:PRK06482  83 NAGY-GLFGAAEELSDA-QIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVE 160

                        170       180
                 ....*....|....*....|...
gi 153792573 207 ALSVEYRDKGIIIQVLTPYSIST 229
Cdd:PRK06482 161 AVAQEVAPFGIEFTIVEPGPART 183
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
44-98 1.30e-05

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 45.99  E-value: 1.30e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 153792573  44 GQWAVI--TGAgdgIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKI 98
Cdd:COG5322  152 ATVAVVgaTGS---IGSVCARLLAREVKRLTLVARNLERLEELAEEILRNPGGKVTI 205
PRK06500 PRK06500
SDR family oxidoreductase;
41-231 1.57e-05

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 45.33  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  41 RSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLqtiaEEIERTTGSCVKIVQADF----TREDIYDHIKEHL 116
Cdd:PRK06500   3 RLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASL----EAARAELGESALVIRADAgdvaAQKALAQALAEAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 117 EGLEIGILvnNVGMLpSFFPshfLSTSGES--QNLIHCNITSVVKMTQLVLKHMeSRRKGLILNISSGAALRPwPLYSLY 194
Cdd:PRK06500  79 GRLDAVFI--NAGVA-KFAP---LEDWDEAmfDRSFNTNVKGPYFLIQALLPLL-ANPASIVLNGSINAHIGM-PNSSVY 150

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK06500 151 AASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPL 187
PRK09134 PRK09134
SDR family oxidoreductase;
47-208 1.77e-05

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 45.30  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNV-VLISRTLEKLQTIAEEIERTTGSCVkIVQADFTRED-IYDHIKEHLEGL-EIGI 123
Cdd:PRK09134  12 ALVTGAARRIGRAIALDLAAHGFDVaVHYNRSRDEAEALAAEIRALGRRAV-ALQADLADEAeVRALVARASAALgPITL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 124 LVNNVgmlpSFFPSHFLSTSGESQNLIH--CNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:PRK09134  91 LVNNA----SLFEYDSAASFTRASWDRHmaTNLRAPFVLAQAFARALPADARGLVVNMIDQRVWNLNPDFLSYTLSKAAL 166


                 ....*..
gi 153792573 202 YTFSKAL 208
Cdd:PRK09134 167 WTATRTL 173
PRK06947 PRK06947
SDR family oxidoreductase;
48-229 4.07e-05

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 44.03  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNV-VLISRTLEKLQTIAEEIERTTG-SCVkiVQADFTRED----IYDHIKEHLEGLEi 121
Cdd:PRK06947   6 LITGASRGIGRATAVLAAARGWSVgINYARDAAAAEETADAVRAAGGrACV--VAGDVANEAdviaMFDAVQSAFGRLD- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 gILVNNVGMLPsffPSHFLS--TSGESQNLIHCNITSVVKMTQLVLKHMESRR---KGLILNISSGAALRPWPL-YSLYS 195
Cdd:PRK06947  83 -ALVNNAGIVA---PSMPLAdmDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrGGAIVNVSSIASRLGSPNeYVDYA 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 153792573 196 ASKAFVYTFSKALSVEYRDKGIIIQVLTPYSIST 229
Cdd:PRK06947 159 GSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIET 192
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 47-231 7.50e-05

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: 42.89  E-value: 7.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTgscvkiVQADFTREDiydHIKEHLEGL-EIGILV 125
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALA------RPADVAAEL---EVWALAQELgPLDLLV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 126 NNVG-MLPSffPShfLSTSGES-QNLIHCNITSVVkmtqLVLKHMESR--RKGLILNISSGAALRPWPLYSLYSASKAFV 201
Cdd:cd11730   72 YAAGaILGK--PL--ARTKPAAwRRILDANLTGAA----LVLKHALALlaAGARLVFLGAYPELVMLPGLSAYAAAKAAL 143

                        170       180       190
                 ....*....|....*....|....*....|
gi 153792573 202 YTFSKALSVEYRdkGIIIQVLTPYSISTPM 231
Cdd:cd11730  144 EAYVEVARKEVR--GLRLTLVRPPAVDTGL 171
PRK08017 PRK08017
SDR family oxidoreductase;
43-236 8.26e-05

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 43.15  E-value: 8.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTleklqtiAEEIERTTGSCVKIVQADFTREDIYDHIKEHLEGLEIG 122
Cdd:PRK08017   1 MQKSVLITGCSSGIGLEAALELKRRGYRVLAACRK-------PDDVARMNSLGFTGILLDLDDPESVERAADEVIALTDN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 IL---VNNVGmLPSFFPSHFLSTSGESQNLiHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKA 199
Cdd:PRK08017  74 RLyglFNNAG-FGVYGPLSTISRQQMEQQF-STNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKY 151

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLN 236
Cdd:PRK08017 152 ALEAWSDALRMELRHSGIKVSLIEPGPIRTRFTDNVN 188
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 44-132 1.51e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 42.71  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTT-GSCVKIVQADFTRediYDHIKEHLEGLE-- 120
Cdd:PRK06197  16 GRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAATpGADVTLQELDLTS---LASVRAAADALRaa 92

                         90
                 ....*....|....*.
gi 153792573 121 ---IGILVNNVG-MLP 132
Cdd:PRK06197  93 yprIDLLINNAGvMYT 108
PRK09186 PRK09186
flagellin modification protein A; Provisional
 48-224 1.70e-04

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 42.28  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGS---CVkiVQADFTREDIYDHIKEHLEGLEIGI- 123
Cdd:PRK09186   8 LITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSkklSL--VELDITDQESLEEFLSKSAEKYGKId 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 124 -LVNNVGMLPSFFPSHFLSTSGESQNL-IHCNITSVVKMTQLVLKHMESRRKGLILNISS--GAALRPWPLYS------- 192
Cdd:PRK09186  86 gAVNCAYPRNKDYGKKFFDVSLDDFNEnLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSiyGVVAPKFEIYEgtsmtsp 165

                        170       180       190
                 ....*....|....*....|....*....|...
gi 153792573 193 -LYSASKAFVYTFSKALSVEYRDKGIIIQVLTP 224
Cdd:PRK09186 166 vEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSP 198
PRK07806 PRK07806
SDR family oxidoreductase;
44-290 1.72e-04

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 42.40  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRT-LEKLQTIAEEIERTTGSCVKiVQADFTRED----IYDHIKEHLEG 118
Cdd:PRK07806   6 GKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQkAPRANKVVAEIEAAGGRASA-VGADLTDEEsvaaLMDTAREEFGG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEIGILVNNVGMLPSFFPSHFLSTSGESQnlihcnitsvVKMTQLVLKHMESrrKGLILNISSGAA-----LRPWPLYSL 193
Cdd:PRK07806  85 LDALVLNASGGMESGMDEDYAMRLNRDAQ----------RNLARAALPLMPA--GSRVVFVTSHQAhfiptVKTMPEYEP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 194 YSASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTKTADEFVKESLKYVTIGAEscgcLAHEIIAIIL 273
Cdd:PRK07806 153 VARSKRAGEDALRALRPELAEKGIGFVVVSGDMIEGTVTATLLNRLNPGAIEARREAAGKLYTVSE----FAAEVARAVT 228

                        250
                 ....*....|....*...
gi 153792573 274 NRIPS-RIFYSSTAQRFL 290
Cdd:PRK07806 229 APVPSgHIEYVGGADYFL 246
PRK07041 PRK07041
SDR family oxidoreductase;
48-107 2.33e-04

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 41.56  E-value: 2.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGscVKIVQADFTRED 107
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGAP--VRTAALDITDEA 58
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 43-231 2.96e-04

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: 41.68  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTRE-----------DIYDH 111
Cdd:cd05322    1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYGFGADATNEqsvialskgvdEIFKR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 112 IKehlegleigILVNNVGMLPSFFPSHFlsTSGESQNLIHCNITSVVKMTQLVLKHM-ESRRKGLILNISSGAALRPWPL 190
Cdd:cd05322   81 VD---------LLVYSAGIAKSAKITDF--ELGDFDRSLQVNLVGYFLCAREFSKLMiRDGIQGRIIQINSKSGKVGSKH 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 153792573 191 YSLYSASKAFVYTFSKALSVEYRDKGIIIQVLTPYS-ISTPM 231
Cdd:cd05322  150 NSGYSAAKFGGVGLTQSLALDLAEHGITVNSLMLGNlLKSPM 191
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 49-214 4.22e-04

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: 40.94  E-value: 4.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  49 ITGAGDGIGKAYSFELARHGLNVVLISRTleklQTIAEEIERTTGSCVKIVQADFTREDIYDHIKEHLEGL-EIGILVNN 127
Cdd:cd08951   12 ITGSSDGLGLAAARTLLHQGHEVVLHARS----QKRAADAKAACPGAAGVLIGDLSSLAETRKLADQVNAIgRFDAVIHN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 128 VGMLPSffPSHFLSTSGESQnLIHCNITSVVKMTQLVlkhmeSRRKGLILnISSG------AAL-------RPWPLYSLY 194
Cdd:cd08951   88 AGILSG--PNRKTPDTGIPA-MVAVNVLAPYVLTALI-----RRPKRLIY-LSSGmhrggnASLddidwfnRGENDSPAY 158

                        170       180
                 ....*....|....*....|
gi 153792573 195 SASKAFVYTFSKALSVEYRD 214
Cdd:cd08951  159 SDSKLHVLTLAAAVARRWKD 178
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 48-135 4.29e-04

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 39.50  E-value: 4.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573   48 VITGAGdGIGKAYSFELARHG--LNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFtREDIYDHIKEHlegleiGILV 125
Cdd:pfam03435   2 LIIGAG-SVGQGVAPLLARHFdvDRITVADRTLEKAQALAAKLGGVRFIAVAVDADNY-EAVLAALLKEG------DLVV 73

                          90
                  ....*....|
gi 153792573  126 NnvgMLPSFF 135
Cdd:pfam03435  74 N---LSPPTL 80
PRK12742 PRK12742
SDR family oxidoreductase;
44-231 7.68e-04

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 40.13  E-value: 7.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLisrTLEKLQTIAEEIERTTGScvKIVQADFT-REDIYDHIKEhlEGlEIG 122
Cdd:PRK12742   6 GKKVLVLGGSRGIGAAIVRRFVTDGANVRF---TYAGSKDAAERLAQETGA--TAVQTDSAdRDAVIDVVRK--SG-ALD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 123 ILVNNVGMLpsFFPSHFLSTSGESQNLIHCNITSVVKMTqlvlkhMESRRK----GLILNISSGAALR-PWPLYSLYSAS 197
Cdd:PRK12742  78 ILVVNAGIA--VFGDALELDADDIDRLFKINIHAPYHAS------VEAARQmpegGRIIIIGSVNGDRmPVAGMAAYAAS 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 153792573 198 KAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPM 231
Cdd:PRK12742 150 KSALQGMARGLARDFGPRGITINVVQPGPIDTDA 183
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 48-124 1.22e-03

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 40.04  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  48 VITGAGDGIGKAYSFELARH-GLNVVLISRT------LEKLQTIAEeiERTTGSCVKIVQADFTR----EDIYDHIKEHL 116
Cdd:cd08953  209 LVTGGAGGIGRALARALARRyGARLVLLGRSplppeeEWKAQTLAA--LEALGARVLYISADVTDaaavRRLLEKVRERY 286


                 ....*...
gi 153792573 117 EGLEiGIL 124
Cdd:cd08953  287 GAID-GVI 293
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 44-88 2.35e-03

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: 38.53  E-value: 2.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEI 88
Cdd:cd01078   28 GKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAADSL 72
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 47-234 2.56e-03

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 38.33  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEklqtiaeeierttgscvkIVQADFTREdiyDHIKEHLEglEIG---I 123
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSG------------------DYQVDITDE---ASIKALFE--KVGhfdA 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 124 LVNNVGMlpSFFPSHFLSTSGESQNLIHCNITSVVKMTQLVLKHMesRRKGLILNISSGAALRPWPLYSLYSASKAFVYT 203
Cdd:cd11731   58 IVSTAGD--AEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYL--NDGGSITLTSGILAQRPIPGGAAAATVNGALEG 133

                        170       180       190
                 ....*....|....*....|....*....|.
gi 153792573 204 FSKALSVEYRDkGIIIQVLTPYSISTPMTKY 234
Cdd:cd11731  134 FVRAAAIELPR-GIRINAVSPGVVEESLEAY 163
PRK06720 PRK06720
hypothetical protein; Provisional
 40-112 2.97e-03

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 37.64  E-value: 2.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792573  40 LRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVkIVQADFTREDIYDHI 112
Cdd:PRK06720  12 MKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEITNLGGEAL-FVSYDMEKQGDWQRV 83
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 47-95 4.01e-03

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. 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 DHs, 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: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 37.25  E-value: 4.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGdGIGKAYSFELARHGL-NVVLISRTLEKLQTIAEEIERTTGSC 95
Cdd:cd01065   22 VLILGAG-GAARAVAYALAELGAaKIVIVNRTLEKAKALAERFGELGIAI 70
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
 49-107 4.54e-03

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: 38.02  E-value: 4.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 153792573  49 ITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEierttGscVKIVQADFTRED 107
Cdd:cd05269    3 VTGATGKLGTAVVELLLAKVASVVALVRNPEKAKAFAAD-----G--VEVRQGDYDDPE 54
PRK06196 PRK06196
oxidoreductase; Provisional
 44-131 6.16e-03

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 37.74  E-value: 6.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  44 GQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERttgscVKIVQADFTREDIYDHIKEHL--EGLEI 121
Cdd:PRK06196  26 GKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGIDG-----VEVVMLDLADLESVRAFAERFldSGRRI 100

                         90
                 ....*....|
gi 153792573 122 GILVNNVGML 131
Cdd:PRK06196 101 DILINNAGVM 110
 
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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