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Conserved domains on  [gi|153792573|ref|NP_032317|]
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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 1.29e-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: 1.29e-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 1.29e-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: 1.29e-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 5.23e-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: 5.23e-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
DltE COG0300
Short-chain dehydrogenase [General function prediction only];
42-233 5.98e-55

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 223377 [Multi-domain]  Cd Length: 265  Bit Score: 179.37  E-value: 5.98e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  42 SMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTRED----IYDHIKEhlE 117
Cdd:COG0300    4 MKGKTALITGASSGIGAELAKQLARRGYNLILVARREDKLEALAKELEDKTGVEVEVIPADLSDPEalerLEDELKE--R 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 118 GLEIGILVNNVGmlpsfF--PSHFLSTS-GESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLY 194
Cdd:COG0300   82 GGPIDVLVNNAG-----FgtFGPFLELSlDEEEEMIQLNILALTRLTKAVLPGMVERGAGHIINIGSAAGLIPTPYMAVY 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:COG0300  157 SATKAFVLSFSEALREELKGTGVKVTAVCPGPTRTEFFD 195
PLN02780 PLN02780
ketoreductase/ oxidoreductase
28-299 2.77e-49

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 166.19  E-value: 2.77e-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 9.90e-18

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: 9.90e-18
                          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
SDR_dihy_bifunc NF012208
bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family ...
47-255 7.62e-16

bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family are SDR family oxidoreductases, unrelated to previously known families of dihydrofolate reductase (DHFR), one of which was demonstrated to be a bifunctional dihydropteridine reductase/dihydrofolate reductase. The DHFR activity can give a heterologously expressed protein the ability to confer resistance to trimethoprim, an inhibitor of most forms of DHFR.


Pssm-ID: 411089 [Multi-domain]  Cd Length: 233  Bit Score: 74.96  E-value: 7.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNV-VLISRTLEKLQTIAEEIERTTGSCVKiVQADFTRED----IYDHIKEHLEGLei 121
Cdd:NF012208   1 ALVTGSARGIGRAIALALAREGFDVaVHYRRSAEAAEQTAQEAEALGVKAIT-LQADLTDPEqarsLVEEAAEALGGL-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 122 GILVNNVGmlpSFFPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAA--LRPWPLYSLYSASK 198
Cdd:NF012208  78 SVLVNNVG---NYLHKPLLETTDEEwHEMLDSNLNATFYVTQAALPLMRAAGWGRIVNLGYAGAqnLLARPGITPYVIAK 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTP----YSISTPMTKyLNNKMTKTADE-------FVKESLKYVT 255
Cdd:NF012208 155 TGVIIYSKALAKELAGDGITVNVVSPgvaeNSVSQPLPE-IPAGRPATLEEladavlfFVRPSSDYIT 221
anticapsin_BacC NF033173
dihydroanticapsin 7-dehydrogenase; Members of this family are dihydroanticapsin ...
43-252 7.31e-14

dihydroanticapsin 7-dehydrogenase; Members of this family are dihydroanticapsin 7-dehydrogenase (EC 1.1.1.385), one of seven key molecular markers for biosynthesis of the non-cognate amino acid anticapsin, a building block for the dipeptide antibiotic natural product bacilysin.


Pssm-ID: 380181 [Multi-domain]  Cd Length: 252  Bit Score: 70.05  E-value: 7.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  43 MGQWAVITGAGDGIGKAYSFELARHGLNVVLISrtLEKLQTiAEEIERTTGSCVKIVQADFTREDIYDH-IKEHLE---G 118
Cdd:NF033173   3 TDKTVLITGGASGIGYAAVQAFLNQQANVVVAD--IDEAQG-EAMVRKENNDRLHFVQTDITDEAACQNaVQSAVDtfgG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 119 LEIgiLVNNVGmLPSFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASK 198
Cdd:NF033173  80 LDV--LINNAG-IEIVAPIHEMELS-DWNKVLQVNLTGMFLMSKHALKHMLAAGKGNIINTCSVGGVVAWPDIPAYNASK 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 153792573 199 AFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK--YLNNKmTKTADEFVKESLK 252
Cdd:NF033173 156 GGVLQLTRSMAVDYAKHQIRVNCVCPGIIDTPLNEksFLENN-EGTLEEIKKEKAK 210
 
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 1.29e-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: 1.29e-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 5.23e-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: 5.23e-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
DltE COG0300
Short-chain dehydrogenase [General function prediction only];
42-233 5.98e-55

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 223377 [Multi-domain]  Cd Length: 265  Bit Score: 179.37  E-value: 5.98e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  42 SMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADFTRED----IYDHIKEhlE 117
Cdd:COG0300    4 MKGKTALITGASSGIGAELAKQLARRGYNLILVARREDKLEALAKELEDKTGVEVEVIPADLSDPEalerLEDELKE--R 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 118 GLEIGILVNNVGmlpsfF--PSHFLSTS-GESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLY 194
Cdd:COG0300   82 GGPIDVLVNNAG-----FgtFGPFLELSlDEEEEMIQLNILALTRLTKAVLPGMVERGAGHIINIGSAAGLIPTPYMAVY 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 153792573 195 SASKAFVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTK 233
Cdd:COG0300  157 SATKAFVLSFSEALREELKGTGVKVTAVCPGPTRTEFFD 195
PLN02780 PLN02780
ketoreductase/ oxidoreductase
28-299 2.77e-49

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 166.19  E-value: 2.77e-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
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
47-233 2.27e-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: 2.27e-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
PRK07454 PRK07454
SDR family oxidoreductase;
38-231 2.09e-38

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 135.47  E-value: 2.09e-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 COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
47-248 4.42e-38

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 223959 [Multi-domain]  Cd Length: 251  Bit Score: 135.33  E-value: 4.42e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRT--LEKLQTIAEEIERTTGSCVKIVQADFTR-----EDIYDHIKEHLEGL 119
Cdd:COG1028    8 ALVTGASSGIGRAIARALAREGARVVVAARRseEEAAEALAAAIKEAGGGRAAAVAADVSDdeesvEALVAAAEEEFGRI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 120 EIgiLVNNVGMLPSFFPSHFLSTSgESQNLIHCNITSVVKMTQLVLKHMESRRkglILNISSGAALRPWPLYSLYSASKA 199
Cdd:COG1028   88 DI--LVNNAGIAGPDAPLEELTEE-DWDRVIDVNLLGAFLLTRAALPLMKKQR---IVNISSVAGLGGPPGQAAYAASKA 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 153792573 200 FVYTFSKALSVEYRDKGIIIQVLTPYSISTPMTKYLNNKMTKTADEFVK 248
Cdd:COG1028  162 ALIGLTKALALELAPRGIRVNAVAPGYIDTPMTAALESAELEALKRLAA 210
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
44-252 1.52e-37

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 133.28  E-value: 1.52e-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 5.74e-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: 5.74e-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
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion];
47-224 5.79e-35

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion];


Pssm-ID: 226674 [Multi-domain]  Cd Length: 246  Bit Score: 126.60  E-value: 5.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  47 AVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTgscVKIVQADFT-REDIYDHIKEHLEGL-EIGIL 124
Cdd:COG4221    9 ALITGASSGIGEATARALAEAGAKVVLAARREERLEALADEIGAGA---ALALALDVTdRAAVEAAIEALPEEFgRIDIL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 125 VNNVG-MLPSFFPShflSTSGESQNLIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYT 203
Cdd:COG4221   86 VNNAGlALGDPLDE---ADLDDWDRMIDTNVKGLLNGTRAVLPGMVERKSGHIINLGSIAGRYPYPGGAVYGATKAAVRA 162
                        170       180
                 ....*....|....*....|.
gi 153792573 204 FSKALSVEYRDKGIIIQVLTP 224
Cdd:COG4221  163 FSLGLRQELAGTGIRVTVISP 183
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
43-243 3.61e-34

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 124.50  E-value: 3.61e-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 1.74e-32

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 120.33  E-value: 1.74e-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 1.45e-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: 1.45e-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 4.46e-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: 4.46e-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 5.68e-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: 5.68e-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 2.41e-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: 2.41e-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 1.13e-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: 1.13e-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 1.20e-28

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 110.30  E-value: 1.20e-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 4.48e-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: 4.48e-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 4.65e-28

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 108.74  E-value: 4.65e-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 5.41e-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: 5.41e-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 5.50e-28

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 108.42  E-value: 5.50e-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 1.89e-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: 1.89e-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 4.92e-27

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 106.00  E-value: 4.92e-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 9.18e-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: 9.18e-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 5.23e-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: 5.23e-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 6.34e-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: 6.34e-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 9.08e-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: 9.08e-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
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
47-249 1.35e-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: 1.35e-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;
55-237 1.68e-25

Enoyl-(Acyl carrier protein) reductase;


Pssm-ID: 404451 [Multi-domain]  Cd Length: 236  Bit Score: 101.34  E-value: 1.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573   55 GIGKAYSFELARHGLNVVLISRTlEKLQTIAEEIERTTGScvKIVQADFTRED----IYDHIKEHLEGLEIgiLVNNVGM 130
Cdd:pfam13561   7 GIGWAIARALAEEGAEVVLTDLN-EALKKRVEELAEELGA--AVLPCDVTDEEqveaLVAAAVEKFGRLDI--LVNNAGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  131 LPsFFPSHFLSTSGES-QNLIHCNITSVVKMTQLVLKHMesRRKGLILNISSGAALRPWPLYSLYSASKAFVYTFSKALS 209
Cdd:pfam13561  82 AP-KEKGPFLDTSREDfDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLA 158
                         170       180
                  ....*....|....*....|....*...
gi 153792573  210 VEYRDKGIIIQVLTPYSISTPMTKYLNN 237
Cdd:pfam13561 159 VELGPRGIRVNAISPGPIKTLAASGIPG 186
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
44-231 1.96e-25

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 102.11  E-value: 1.96e-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 2.91e-25

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 101.15  E-value: 2.91e-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 7.62e-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: 7.62e-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 8.06e-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: 8.06e-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 9.76e-25

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 99.80  E-value: 9.76e-25
                         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 1.47e-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: 1.47e-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 1.67e-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: 1.67e-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 4.49e-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: 4.49e-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 1.40e-23

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 96.93  E-value: 1.40e-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 1.59e-23

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 96.74  E-value: 1.59e-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 4.25e-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: 4.25e-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 1.00e-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: 1.00e-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 1.14e-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: 1.14e-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 1.22e-22

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 97.71  E-value: 1.22e-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 2.32e-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: 2.32e-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 3.45e-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: 3.45e-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 1.10e-21

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 91.52  E-value: 1.10e-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 1.84e-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: 1.84e-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 3.05e-21

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 90.73  E-value: 3.05e-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 3.05e-21

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 90.50  E-value: 3.05e-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
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
49-251 4.62e-21

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


Pssm-ID: 226476 [Multi-domain]  Cd Length: 245  Bit Score: 89.80  E-value: 4.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573  49 ITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQTIAEEIERTTGSCVKIVQADfTREDIYDHIKEHLEGLEIgiLVNNV 128
Cdd:COG3967   10 ITGGASGIGLALAKRFLELGNTVIICGRNEERLAEAKAENPEIHTEVCDVADRD-SRRELVEWLKKEYPNLNV--LINNA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792573 129 GMLPS--FFPSHFLSTSGESQnlIHCNITSVVKMTQLVLKHMESRRKGLILNISSGAALRPWPLYSLYSASKAFVYTFSK 206
Cdd:COG3967   87 GIQRNedLTGAEDLLDDAEQE--IATNLLAPIRLTALLLPHLLRQPEATIINVSSGLAFVPMASTPVYCATKAAIHSYTL 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 153792573 207 ALSVEYRDKGI-IIQVLTPYSISTPMTKYLNNKMTKTADEFVKESL 251
Cdd:COG3967  165 ALREQLKDTSVeVIELAPPLVDTTEGNTQARGKMPLSAFISETEDL 210
PRK07825 PRK07825
short chain dehydrogenase; Provisional
48-232 5.96e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 90.00  E-value: 5.96e-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 6.56e-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: 6.56e-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 7.81e-21

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 89.65  E-value: 7.81e-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 8.63e-21

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 89.03  E-value: 8.63e-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 1.66e-20

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 88.67  E-value: 1.66e-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 2.24e-20

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 89.60  E-value: 2.24e-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 2.89e-20

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 90.81  E-value: 2.89e-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 3.07e-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: 3.07e-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 3.25e-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: 3.25e-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 3.87e-20

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 87.39  E-value: 3.87e-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 4.07e-20

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 88.26  E-value: 4.07e-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 4.48e-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: 4.48e-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 6.11e-20

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 87.10  E-value: 6.11e-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 1.13e-19

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 88.75  E-value: 1.13e-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 1.56e-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: 1.56e-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 2.08e-19

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 85.38  E-value: 2.08e-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 2.22e-19

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 85.72  E-value: 2.22e-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