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Conserved domains on  [gi|1034574112|ref|XP_016873370|]
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very-long-chain 3-oxoacyl-CoA reductase isoform X1 [Homo sapiens]

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) ...
 23-257 3.01e-133

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: 376.56  E-value: 3.01e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDF-ASEDIYDKIKTGLAGLEIGILVNN 101
Cdd:cd05356     6 VTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFsAGDDIYERIEKELEGLDIGILVNN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 102 VGMSYEYPEYFLDVPDldNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFFS 181
Cdd:cd05356    86 VGISHSIPEYFLETPE--DELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLDFFS 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034574112 182 QCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPSPETFVKSAIKTVGLQSRTNGYLIHALMGSIISNLPSWI 257
Cdd:cd05356   164 RALYEEYKSQGIDVQSLLPYLVATKMSKIRKSSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARLVPEWI 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) ...
 23-257 3.01e-133

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: 376.56  E-value: 3.01e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDF-ASEDIYDKIKTGLAGLEIGILVNN 101
Cdd:cd05356     6 VTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFsAGDDIYERIEKELEGLDIGILVNN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 102 VGMSYEYPEYFLDVPDldNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFFS 181
Cdd:cd05356    86 VGISHSIPEYFLETPE--DELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLDFFS 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034574112 182 QCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPSPETFVKSAIKTVGLQSRTNGYLIHALMGSIISNLPSWI 257
Cdd:cd05356   164 RALYEEYKSQGIDVQSLLPYLVATKMSKIRKSSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARLVPEWI 239
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 23-254 7.20e-69

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 215.89  E-value: 7.20e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKF-KVETRTIAVDFaSEDIYD---KIKTGLAGLEIGIL 98
Cdd:PLN02780   58 VTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYsKTQIKTVVVDF-SGDIDEgvkRIKETIEGLDVGVL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEYPEYFLDVPDldNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGML--PVPLLTIYSATKTF 176
Cdd:PLN02780  137 INNVGVSYPYARFFHEVDE--ELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVipSDPLYAVYAATKAY 214

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPSPETFVKSAIKTVGLQSRTNGYLIHALMGSIISNLP 254
Cdd:PLN02780  215 IDQFSRCLYVEYKKSGIDVQCQVPLYVATKMASIRRSSFLVPSSDGYARAALRWVGYEPRCTPYWPHSLIWGLISALP 292
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
22-265 2.11e-53

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 173.90  E-value: 2.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASED----IYDKIKTglAGLEIGI 97
Cdd:COG0300     9 LITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAA-GARVEVVALDVTDPDavaaLAEAVLA--RFGPIDV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYeyPEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:COG0300    86 LVNNAGVGG--GGPFEELDLED--LRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKP--SPETFVKSAIKtvGLQSRTNGYLIHA---LMGSIISN 252
Cdd:COG0300   162 EGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPllSPEEVARAILR--ALERGRAEVYVGWdarLLARLLRL 239

                         250
                  ....*....|...
gi 1034574112 253 LPSWiYLKIVMNM 265
Cdd:COG0300   240 LPRL-FDRLLRRA 251
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 22-209 1.08e-48

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 160.09  E-value: 1.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASED----IYDKIKTGLAGleIGI 97
Cdd:pfam00106   4 LVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAL-GGKALFIQGDVTDRAqvkaLVEQAVERLGR--LDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPEYFLDVPDldnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDED----WERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAV 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDTDMTK 188
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 23-195 4.22e-12

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: 64.55  E-value: 4.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAK----HGMKVVLISRSKDKLDQVSSEI-KEKFKVETRTIAVDFASE-DIYDKIKTGLA----- 91
Cdd:TIGR01500   5 VTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIgAERSGLRVVRVSLDLGAEaGLEQLLKALRElprpk 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  92 GLEIGILVNNVGMSYEYPEYFLDVPDLDNvIKKMININILSVCKMTQLVLPGMVER--SKGAILNISSGSGMLPVPLLTI 169
Cdd:TIGR01500  85 GLQRLLLINNAGTLGDVSKGFVDLSDSTQ-VQNYWALNLTSMLCLTSSVLKAFKDSpgLNRTVVNISSLCAIQPFKGWAL 163

                         170       180
                  ....*....|....*....|....*.
gi 1034574112 170 YSATKTFVDFFSQCLHEEYRSKGVFV 195
Cdd:TIGR01500 164 YCAGKAARDMLFQVLALEEKNPNVRV 189
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 23-51 4.43e-03

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 37.08  E-value: 4.43e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034574112   23 VTGSTDGIGKSYAEELAKHGM-KVVLISRS 51
Cdd:smart00822   5 ITGGLGGLGRALARWLAERGArRLVLLSRS 34
 
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) ...
 23-257 3.01e-133

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: 376.56  E-value: 3.01e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDF-ASEDIYDKIKTGLAGLEIGILVNN 101
Cdd:cd05356     6 VTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFsAGDDIYERIEKELEGLDIGILVNN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 102 VGMSYEYPEYFLDVPDldNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFFS 181
Cdd:cd05356    86 VGISHSIPEYFLETPE--DELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLDFFS 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034574112 182 QCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPSPETFVKSAIKTVGLQSRTNGYLIHALMGSIISNLPSWI 257
Cdd:cd05356   164 RALYEEYKSQGIDVQSLLPYLVATKMSKIRKSSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARLVPEWI 239
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 23-254 7.20e-69

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 215.89  E-value: 7.20e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKF-KVETRTIAVDFaSEDIYD---KIKTGLAGLEIGIL 98
Cdd:PLN02780   58 VTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYsKTQIKTVVVDF-SGDIDEgvkRIKETIEGLDVGVL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEYPEYFLDVPDldNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGML--PVPLLTIYSATKTF 176
Cdd:PLN02780  137 INNVGVSYPYARFFHEVDE--ELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVipSDPLYAVYAATKAY 214

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPSPETFVKSAIKTVGLQSRTNGYLIHALMGSIISNLP 254
Cdd:PLN02780  215 IDQFSRCLYVEYKKSGIDVQCQVPLYVATKMASIRRSSFLVPSSDGYARAALRWVGYEPRCTPYWPHSLIWGLISALP 292
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
22-265 2.11e-53

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 173.90  E-value: 2.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASED----IYDKIKTglAGLEIGI 97
Cdd:COG0300     9 LITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAA-GARVEVVALDVTDPDavaaLAEAVLA--RFGPIDV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYeyPEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:COG0300    86 LVNNAGVGG--GGPFEELDLED--LRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKP--SPETFVKSAIKtvGLQSRTNGYLIHA---LMGSIISN 252
Cdd:COG0300   162 EGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPllSPEEVARAILR--ALERGRAEVYVGWdarLLARLLRL 239

                         250
                  ....*....|...
gi 1034574112 253 LPSWiYLKIVMNM 265
Cdd:COG0300   240 LPRL-FDRLLRRA 251
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 22-209 1.08e-48

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 160.09  E-value: 1.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASED----IYDKIKTGLAGleIGI 97
Cdd:pfam00106   4 LVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAL-GGKALFIQGDVTDRAqvkaLVEQAVERLGR--LDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPEYFLDVPDldnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDED----WERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAV 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDTDMTK 188
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 22-218 1.09e-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: 1.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVssEIKEKFKVETRTIAVDFASEDIYDKI--KTGLAGLEIGILV 99
Cdd:cd05233     2 LVTGASSGIGRAIARRLAREGAKVVLADRNEEALAEL--AAIEALGGNAVAVQADVSDEEDVEALveEALEEFGRLDILV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NNVGMSYEYPeyFLDVPDldNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDF 179
Cdd:cd05233    80 NNAGIARPGP--LEELTD--EDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEG 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034574112 180 FSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKP 218
Cdd:cd05233   156 LTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEK 194
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 22-208 1.61e-40

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 140.32  E-value: 1.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFkvetRTIAVDFASEDiydKIKTGLAGLE-----IG 96
Cdd:COG4221     9 LITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRA----LAVPLDVTDEA---AVEAAVAAAVaefgrLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSYeyPEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:COG4221    82 VLVNNAGVAL--LGPLEELDPED--WDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAA 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVATKLA 208
Cdd:COG4221   158 VRGLSESLRAELRPTGIRVTVIEPGAVDTEFL 189
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 22-209 8.29e-37

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 131.06  E-value: 8.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASED----IYDKIKTGLAGLEIgi 97
Cdd:COG1028    10 LVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAA-GGRALAVAADVTDEAaveaLVAAAVAAFGRLDI-- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPeyFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:COG1028    87 LVNNAGITPPGP--LEELTEED--WDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAV 162

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:COG1028   163 VGLTRSLALELAPRGIRVNAVAPGPIDTPMTR 194
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 23-236 2.09e-36

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: 130.01  E-value: 2.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFAS-EDIYDKIKTGLAGL-EIGILVN 100
Cdd:cd05332     8 ITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVPLDMSDlEDAEQVVEEALKLFgGLDILIN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSYeyPEYFLDVpDLDNViKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFF 180
Cdd:cd05332    88 NAGISM--RSLFHDT-SIDVD-RKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHALQGF 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034574112 181 SQCLHEEYRSKGVFVQSVLPYFVAT------------KLAKIRKPTLDKPSPETFVKSAIKTVGLQSR 236
Cdd:cd05332   164 FDSLRAELSEPNISVTVVCPGLIDTniamnalsgdgsMSAKMDDTTANGMSPEECALEILKAIALRKR 231
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 22-211 1.00e-34

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: 125.47  E-value: 1.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASEDiydKIKTGLAGL-----EIG 96
Cdd:cd05346     4 LITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVKVLPLQLDVSDRE---SIEAALENLpeefrDID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSyeypeyfLDVPDLDNV----IKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSA 172
Cdd:cd05346    81 ILVNNAGLA-------LGLDPAQEAdledWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCA 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034574112 173 TKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIR 211
Cdd:cd05346   154 TKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFSLVR 192
PRK07454 PRK07454
SDR family oxidoreductase;
22-207 6.37e-34

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 123.15  E-value: 6.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFA-SEDIYDKIKTGLA-GLEIGILV 99
Cdd:PRK07454   10 LITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRST-GVKAAAYSIDLSnPEAIAPGIAELLEqFGCPDVLI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NNVGMSYEYPEYFLDVPDLDNVikkmININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDF 179
Cdd:PRK07454   89 NNAGMAYTGPLLEMPLSDWQWV----IQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAA 164

                         170       180
                  ....*....|....*....|....*...
gi 1034574112 180 FSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK07454  165 FTKCLAEEERSHGIRVCTITLGAVNTPL 192
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 22-209 3.71e-33

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: 121.57  E-value: 3.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDqvssEIKEKFKVETRTIAVDFASEDIYDKIKTGLAGLE--IGILV 99
Cdd:cd05374     4 LITGCSSGIGLALALALAAQGYRVIATARNPDKLE----SLGELLNDNLEVLELDVTDEESIKAAVKEVIERFgrIDVLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NNVGMSYEYPeyFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDF 179
Cdd:cd05374    80 NNAGYGLFGP--LEETSIEE--VRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEA 155

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034574112 180 FSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:cd05374   156 LSESLRLELAPFGIKVTIIEPGPVRTGFAD 185
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 22-218 7.50e-33

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 120.56  E-value: 7.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkFKVETRTIAVDFASEDiydKIKTGLAGLE-----IG 96
Cdd:PRK07666   11 LITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEA-YGVKVVIATADVSDYE---EVTAAIEQLKnelgsID 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSyeypEY--FLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATK 174
Cdd:PRK07666   87 ILINNAGIS----KFgkFLELDPAE--WEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034574112 175 TFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKP 218
Cdd:PRK07666  161 FGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGLTDGNP 204
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 22-229 2.24e-32

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


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 119.50  E-value: 2.24e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkfkveTRTIAVDFASEDI----YDKIKTGLAGLeiGI 97
Cdd:COG3967     9 LITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPG-----LHTIVLDVADPASiaalAEQVTAEFPDL--NV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPeyFLDVPDLDNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:COG3967    82 LINNAGIMRAED--LLDEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATKAAL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPSPETFVKSAIK 229
Cdd:COG3967   160 HSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQGGDPRAMPLDEFADEVMA 211
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 23-229 5.55e-32

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: 117.79  E-value: 5.55e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkfkveTRTIAVDFA-SEDI---YDKIKTglAGLEIGIL 98
Cdd:cd05370    10 ITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-----IHTIVLDVGdAESVealAEALLS--EYPNLDIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMsyEYPEYFLDVPDLDNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVD 178
Cdd:cd05370    83 INNAGI--QRPIDLRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKAALH 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVLPYFVATKL-AKIRKPTLDKP---SPETFVKSAIK 229
Cdd:cd05370   161 SYTLALRHQLKDTGVEVVEIVPPAVDTELhEERRNPDGGTPrkmPLDEFVDEVVA 215
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 22-233 4.44e-31

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: 116.22  E-value: 4.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKeKFKVETRTIAVDFASEDIYDKI--KTGLAGLEIGILV 99
Cdd:cd05344     5 LVTAASSGIGLAIARALAREGARVAICARNRENLERAASELR-AGGAGVLAVVADLTDPEDIDRLveKAGDAFGRVDILV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NNVGMSYeyPEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDF 179
Cdd:cd05344    84 NNAGGPP--PGPFAELTDED--WLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034574112 180 FSQCLHEEYRSKGVFVQSVLPYFVAT----KLAKIRKPtLDKPSPETFVKSAIKTVGL 233
Cdd:cd05344   160 LVKTLSRELAPDGVTVNSVLPGYIDTervrRLLEARAE-KEGISVEEAEKEVASQIPL 216
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 23-208 1.76e-30

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: 114.53  E-value: 1.76e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASED----IYDKIKTGLAGleIGIL 98
Cdd:cd05343    11 VTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLFPYQCDLSNEEqilsMFSAIRTQHQG--VDVC 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSyeYPEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVER--SKGAILNISSGSG--MLPVPLLTIYSATK 174
Cdd:cd05343    89 INNAGLA--RPEPLLSGKTEG--WKEMFDVNVLALSICTREAYQSMKERnvDDGHIININSMSGhrVPPVSVFHFYAATK 164

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1034574112 175 TFVDFFSQCLHEEYR--SKGVFVQSVLPYFVATKLA 208
Cdd:cd05343   165 HAVTALTEGLRQELReaKTHIRATSISPGLVETEFA 200
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 23-224 2.79e-30

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 114.65  E-value: 2.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKekfKVETRTIAV-DFAS-EDIYDKIKTGLAglEIGILVN 100
Cdd:PRK07825   10 ITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELG---LVVGGPLDVtDPASfAAFLDAVEADLG--PIDVLVN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSYEYPeyFLDVPDldNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFF 180
Cdd:PRK07825   85 NAGVMPVGP--FLDEPD--AVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKHAVVGF 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034574112 181 SQCLHEEYRSKGVFVQSVLPYFVATKLA------KIRKP------------TLDKPSPETFV 224
Cdd:PRK07825  161 TDAARLELRGTGVHVSVVLPSFVNTELIagtggaKGFKNvepedvaaaivgTVAKPRPEVRV 222
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 22-265 1.34e-27

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: 106.56  E-value: 1.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFAS-EDIY---DKIKTglAGLEIGI 97
Cdd:cd05339     3 LITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKA-GGKVHYYKCDVSKrEEVYeaaKKIKK--EVGDVTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPeyFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:cd05339    80 LINNAGVVSGKK--LLELPDEE--IEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 178 DFFSQCLHEEYRS---KGVFVQSVLPYFVATKL---AKIRKPTLDKP-SPETFVKSAIKTVglqsRTNGYLIhalmgsii 250
Cdd:cd05339   156 VGFHESLRLELKAygkPGIKTTLVCPYFINTGMfqgVKTPRPLLAPIlEPEYVAEKIVRAI----LTNQQML-------- 223

                         250
                  ....*....|....*
gi 1034574112 251 sNLPSWIYLKIVMNM 265
Cdd:cd05339   224 -YLPFYAYFLPILKR 237
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 22-208 7.80e-27

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: 104.54  E-value: 7.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIK-EKFKVETrtIAVDFASE----DIYDKIKTGLAGLEIg 96
Cdd:cd08934     7 LVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEaEGGKALV--LELDVTDEqqvdAAVERTVEALGRLDI- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 iLVNNVGMSYEYPEYFLDVPDLDnvikKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:cd08934    84 -LVNNAGIMLLGPVEDADTTDWT----RMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFG 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVATKLA 208
Cdd:cd08934   159 VNAFSEGLRQEVTERGVRVVVIEPGTVDTELR 190
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 23-205 2.07e-26

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 103.40  E-value: 2.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkFKVETRTIAVDFAS-EDIYDKIKTGLAGL-EIGILVN 100
Cdd:cd05333     5 VTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKA-LGGNAAALEADVSDrEAVEALVEKVEAEFgPVDILVN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVG---------MSYEypeyfldvpDLDNVikkmININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYS 171
Cdd:cd05333    84 NAGitrdnllmrMSEE---------DWDAV----INVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYA 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034574112 172 ATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:cd05333   151 ASKAGVIGFTKSLAKELASRGITVNAVAPGFIDT 184
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 22-200 2.18e-26

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


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 103.49  E-value: 2.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVET---RTIAVDFASediYDKIKTGLA-----GL 93
Cdd:cd08939     5 LITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANASGqkvSYISADLSD---YEEVEQAFAqavekGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  94 EIGILVNNVGMSYeyPEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSAT 173
Cdd:cd08939    82 PPDLVVNCAGISI--PGLFEDLTAEE--FERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPS 157

                         170       180
                  ....*....|....*....|....*..
gi 1034574112 174 KTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:cd08939   158 KFALRGLAESLRQELKPYNIRVSVVYP 184
FabG-like PRK07231
SDR family oxidoreductase;
23-209 2.31e-26

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 103.76  E-value: 2.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkfkvETRTIAV--DFASEDIYDKIKTglAGLE----IG 96
Cdd:PRK07231   10 VTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILA----GGRAIAVaaDVSDEADVEAAVA--AALErfgsVD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSYEYpEYFLDVpDLDNViKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:PRK07231   84 ILVNNAGTTHRN-GPLLDV-DEAEF-DRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:PRK07231  161 VITLTKALAAELGPDKIRVNAVAPVVVETGLLE 193
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 23-233 9.79e-26

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: 102.10  E-value: 9.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEK--FKVETRTIAVDFASEDIYDKI-KTGLAGL-EIGIL 98
Cdd:cd05364     8 ITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAgvSEKKILLVVADLTEEEGQDRIiSTTLAKFgRLDIL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEYPEYFLDVPDLDnvikKMININILSVCKMTQLVLPGMVErSKGAILNISSGSGMLPVPLLTIYSATKTFVD 178
Cdd:cd05364    88 VNNAGILAKGGGEDQDIEEYD----KVMNLNLRAVIYLTKLAVPHLIK-TKGEIVNVSSVAGGRSFPGVLYYCISKAALD 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVLPYFVATKLAkiRKPTLDKPSPETFVKSAIKTVGL 233
Cdd:cd05364   163 QFTRCTALELAPKGVRVNSVSPGVIVTGFH--RRMGMPEEQYIKFLSRAKETHPL 215
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 22-205 1.19e-25

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 101.42  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVL-ISRSKDKLDQVSSEIKEKfKVETRTIAVDFASED----IYDKIKTGLAGLEIg 96
Cdd:PRK05557    9 LVTGASRGIGRAIAERLAAQGANVVInYASSEAGAEALVAEIGAL-GGKALAVQGDVSDAEsverAVDEAKAEFGGVDI- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 iLVNNVGMSYEYPEYFLDVPDLDNVIkkmiNINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:PRK05557   87 -LVNNAGITRDNLLMRMKEEDWDRVI----DTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAG 161

                         170       180
                  ....*....|....*....|....*....
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK05557  162 VIGFTKSLARELASRGITVNAVAPGFIET 190
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 23-218 5.81e-25

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: 99.83  E-value: 5.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEK-FKVETrtIAVDFASEDIYDKIK---TGLAGLEIGIL 98
Cdd:cd05329    11 VTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKgFKVEG--SVCDVSSRSERQELMdtvASHFGGKLNIL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMS-------YEYPEYfldvpdldnviKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYS 171
Cdd:cd05329    89 VNNAGTNirkeakdYTEEDY-----------SLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1034574112 172 ATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAkirKPTLDKP 218
Cdd:cd05329   158 ATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLV---EPVIQQK 201
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 23-210 2.86e-24

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 97.93  E-value: 2.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVsseIKEKFKVETrtIAVDFASediYDKIKTGLAGL-EIGILVNN 101
Cdd:cd05351    12 VTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSL---VRECPGIEP--VCVDLSD---WDATEEALGSVgPVDLLVNN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 102 VGMSYEYPeyFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERS-KGAILNISSGSGMLPVPLLTIYSATKTFVDFF 180
Cdd:cd05351    84 AAVAILQP--FLEVTKEA--FDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHTVYCSTKAALDML 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034574112 181 SQCLHEEYRSKGVFVQSVLPYFVATKLAKI 210
Cdd:cd05351   160 TKVMALELGPHKIRVNSVNPTVVMTDMGRD 189
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-209 3.12e-24

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 97.61  E-value: 3.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLI-SRSKDKLDQVSSEIKEKfKVETRTIAVDFASED----IYDKIKTGLAGLEIgi 97
Cdd:PRK05565   10 VTGASGGIGRAIAELLAKEGAKVVIAyDINEEAAQELLEEIKEE-GGDAIAVKADVSSEEdvenLVEQIVEKFGKIDI-- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPeyFLDVPDldNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:PRK05565   87 LVNNAGISNFGL--VTDMTD--EEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGAV 162

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:PRK05565  163 NAFTKALAKELAPSGIRVNAVAPGAIDTEMWS 194
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 22-211 3.46e-24

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 97.91  E-value: 3.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKvetrtiavdFASEDIYDK--IKTGLAGL-----E 94
Cdd:PRK10538    4 LVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLY---------IAQLDVRNRaaIEEMLASLpaewrN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  95 IGILVNNVGMSYEY-PEYFLDVPDLDNvikkMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSAT 173
Cdd:PRK10538   75 IDVLVNNAGLALGLePAHKASVEDWET----MIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGAT 150

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034574112 174 KTFVDFFSQCLHEEYRSKGVFVQSVLPYFVA-TKLAKIR 211
Cdd:PRK10538  151 KAFVRQFSLNLRTDLHGTAVRVTDIEPGLVGgTEFSNVR 189
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 23-220 3.64e-24

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 97.05  E-value: 3.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRtiAVDFASEDIYDKIKTGLAGlEIGILVNNV 102
Cdd:cd08932     5 VTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSASGGDVEAVPYD--ARDPEDARALVDALRDRFG-RIDVLVHNA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 103 GMsyEYPEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFFSQ 182
Cdd:cd08932    82 GI--GRPTTLREGSDAE--LEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAH 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034574112 183 CLHEEYRSKGVFVQSVLPYFVATKLAkiRKPTLDKPSP 220
Cdd:cd08932   158 ALRQEGWDHGVRVSAVCPGFVDTPMA--QGLTLVGAFP 193
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 23-209 5.51e-24

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: 97.04  E-value: 5.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIkEKFKVETRTIAVDFASEDiydKIKTGLAGLE-----IGI 97
Cdd:cd05347    10 VTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLI-EKEGVEATAFTCDVSDEE---AIKAAVEAIEedfgkIDI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPeyFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:cd05347    86 LVNNAGIIRRHP--AEEFPEAE--WRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGV 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:cd05347   162 AGLTKALATEWARHGIQVNAIAPGYFATEMTE 193
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
22-205 8.65e-24

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 96.38  E-value: 8.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFkVETRTIAVDFASEdiyDKIKTGLAGL-----EIG 96
Cdd:PRK05653    9 LVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAG-GEARVLVFDVSDE---AAVRALIEAAveafgALD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVG---------MSYEypeyfldvpDLDNVikkmININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLL 167
Cdd:PRK05653   85 ILVNNAGitrdallprMSEE---------DWDRV----IDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQ 151

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034574112 168 TIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK05653  152 TNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDT 189
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
23-217 2.08e-23

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 95.60  E-value: 2.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDkldQVSSEIKEKF---KVETRTIAVDFA-SEDIYDKIKTGLAGLE-IGI 97
Cdd:PRK12824    7 VTGAKRGIGSAIARELLNDGYRVIATYFSGN---DCAKDWFEEYgftEDQVRLKELDVTdTEECAEALAEIEEEEGpVDI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYeypeyfldvpdlDNVIKKM--------ININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTI 169
Cdd:PRK12824   84 LVNNAGITR------------DSVFKRMshqewndvINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTN 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034574112 170 YSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK-IRKPTLDK 217
Cdd:PRK12824  152 YSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVEqMGPEVLQS 200
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 23-207 2.85e-23

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: 95.03  E-value: 2.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVL-ISRSKDKLDQVSSEIKekfKVETRTIAV--DFASED----IYDKIKTGLAGLEI 95
Cdd:cd05362     8 VTGASRGIGRAIAKRLARDGASVVVnYASSKAAAEEVVAEIE---AAGGKAIAVqaDVSDPSqvarLFDAAEKAFGGVDI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 giLVNNVGMSYEYPEYFLDVPDLDnvikKMININILSVCKMTQLVLPGMveRSKGAILNISSGSGMLPVPLLTIYSATKT 175
Cdd:cd05362    85 --LVNNAGVMLKKPIAETSEEEFD----RMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPNYGAYAGSKA 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 176 FVDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:cd05362   157 AVEAFTRVLAKELGGRGITVNAVAPGPVDTDM 188
PRK06181 PRK06181
SDR family oxidoreductase;
23-227 1.75e-22

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 93.50  E-value: 1.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkFKVETRTIAVDFASEDIYDKIKTglAGLE----IGIL 98
Cdd:PRK06181    6 ITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELAD-HGGEALVVPTDVSDAEACERLIE--AAVArfggIDIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEYPeyFLDVPDLdNVIKKMININILSVCKMTQLVLPGMVERsKGAILNISSGSGMLPVPLLTIYSATKTFVD 178
Cdd:PRK06181   83 VNNAGITMWSR--FDELTDL-SVFERVMRVNYLGAVYCTHAALPHLKAS-RGQIVVVSSLAGLTGVPTRSGYAASKHALH 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVLPYFVATklaKIRKPTLD---KPSPETFVKSA 227
Cdd:PRK06181  159 GFFDSLRIELADDGVAVTVVCPGFVAT---DIRKRALDgdgKPLGKSPMQES 207
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 23-232 1.78e-22

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


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 92.86  E-value: 1.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGM-KVVLISRSKDKLDqvssEIKEKFKVETRTIAVDFASEDiydKIKTGLAGL-EIGILVN 100
Cdd:cd05354     8 VTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAA----HLVAKYGDKVVPLRLDVTDPE---SIKAAAAQAkDVDVVIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSYeyPEYFLDVPDLDNVIKKMiNINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFF 180
Cdd:cd05354    81 NAGVLK--PATLLEEGALEALKQEM-DVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAAYSL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034574112 181 SQCLHEEYRSKGVFVQSVLPYFVATKLAKirKPTLDKPSPETFVKSAIKTVG 232
Cdd:cd05354   158 TQGLRAELAAQGTLVLSVHPGPIDTRMAA--GAGGPKESPETVAEAVLKALK 207
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
22-233 1.81e-22

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 93.33  E-value: 1.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSkDKLDQVSSEIKEKfkvETRTIAV-----DFAS-----EDIYDKIKtgla 91
Cdd:PRK08226   10 LITGALQGIGEGIARVFARHGANLILLDIS-PEIEKLADELCGR---GHRCTAVvadvrDPASvaaaiKRAKEKEG---- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  92 glEIGILVNNVGMSYEYPeyFLDVPDLDNVIKkmININILSVCKMTQLVLPGMVERSKGAILNISSGSG-MLPVPLLTIY 170
Cdd:PRK08226   82 --RIDILVNNAGVCRLGS--FLDMSDEDRDFH--IDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGdMVADPGETAY 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034574112 171 SATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPSPETFVKSAIKTVGL 233
Cdd:PRK08226  156 ALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIARQSNPEDPESVLTEMAKAIPL 218
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 22-221 2.13e-22

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 93.11  E-value: 2.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEK-FKVETrtIAVDFASED----IYDKIKTGLAGLEIg 96
Cdd:PRK12939   11 LVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAgGRAHA--IAADLADPAsvqrFFDAAAAALGGLDG- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 iLVNNVGMSYEYPEYFLDVPDLDNVIkkmiNINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:PRK12939   88 -LVNNAGITNSKSATELDIDTWDAVM----NVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGA 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVATKLakirkpTLDKPSPE 221
Cdd:PRK12939  163 VIGMTRSLARELGGRGITVNAIAPGLTATEA------TAYVPADE 201
PRK05866 PRK05866
SDR family oxidoreductase;
23-205 2.60e-22

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 93.65  E-value: 2.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASEDIYDKIKTGLAGlEIG---ILV 99
Cdd:PRK05866   45 LTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRA-GGDAMAVPCDLSDLDAVDALVADVEK-RIGgvdILI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NNVGMSYEYP-----EYFLDVpdldnviKKMININILSVCKMTQLVLPGMVERSKGAILNISSGsGMLP--VPLLTIYSA 172
Cdd:PRK05866  123 NNAGRSIRRPlaeslDRWHDV-------ERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATW-GVLSeaSPLFSVYNA 194

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034574112 173 TKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK05866  195 SKAALSAVSRVIETEWGDRGVHSTTLYYPLVAT 227
PRK09242 PRK09242
SDR family oxidoreductase;
23-218 2.64e-22

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 92.89  E-value: 2.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRT-IAVDFA-SED---IYDKIKTGLAGLEIgi 97
Cdd:PRK09242   14 ITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEFPEREVHgLAADVSdDEDrraILDWVEDHWDGLHI-- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVG-------MSYEYPEYfldvpdldnviKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIY 170
Cdd:PRK09242   92 LVNNAGgnirkaaIDYTEDEW-----------RGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034574112 171 SATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAkirKPTLDKP 218
Cdd:PRK09242  161 GMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLT---SGPLSDP 205
PRK12826 PRK12826
SDR family oxidoreductase;
22-205 7.49e-22

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 91.52  E-value: 7.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKF-KVetRTIAVDFASEDiydKIKTGLAGLE-----I 95
Cdd:PRK12826   10 LVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGgKA--RARQVDVRDRA---ALKAAVAAGVedfgrL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 GILVNNVGMSYEYPEYFLDVPDLDNVIkkmiNINILSVCKMTQLVLPGMVERSKGAILNISSGSG-MLPVPLLTIYSATK 174
Cdd:PRK12826   85 DILVANAGIFPLTPFAEMDDEQWERVI----DVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGpRVGYPGLAHYAASK 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034574112 175 TFVDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK12826  161 AGLVGFTRALALELAARNITVNSVHPGGVDT 191
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
22-217 1.57e-21

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 90.46  E-value: 1.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSkdkldqvSSEIKEKFKVETRTIAVDF-----------ASEDIYDKIKTGL 90
Cdd:PRK12938    7 YVTGGMGGIGTSICQRLHKDGFKVVAGCGP-------NSPRRVKWLEDQKALGFDFiasegnvgdwdSTKAAFDKVKAEV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  91 AglEIGILVNNVGMSYEYPEYFLDVPDLDNVIkkmiNINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIY 170
Cdd:PRK12938   80 G--EIDVLVNNAGITRDVVFRKMTREDWTAVI----DTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNY 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034574112 171 SATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK-IRKPTLDK 217
Cdd:PRK12938  154 STAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKaIRPDVLEK 201
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 23-209 3.94e-21

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 89.62  E-value: 3.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASE-DIYDKIKTGLAGL-EIGILVN 100
Cdd:PRK08213   17 VTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEAL-GIDALWIAADVADEaDIERLAEETLERFgHVDILVN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSYEYPEyfLDVPdLDnVIKKMININILSVCKMTQLVLP-GMVERSKGAILNISSGSGM---LPVPLLTI-YSATKT 175
Cdd:PRK08213   96 NAGATWGAPA--EDHP-VE-AWDKVMNLNVRGLFLLSQAVAKrSMIPRGYGRIINVASVAGLggnPPEVMDTIaYNTSKG 171

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034574112 176 FVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:PRK08213  172 AVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTR 205
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 23-207 1.71e-20

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: 87.74  E-value: 1.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKldQVSSEIKEKF-KVETRTIAVDFAS-EDIYDKIKTglAGLEIG---I 97
Cdd:cd05323     5 ITGGASGIGLATAKLLLKKGAKVAILDRNENP--GAAAELQAINpKVKATFVQCDVTSwEQLAAAFKK--AIEKFGrvdI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVER---SKGAILNISSGSGMLPVPLLTIYSATK 174
Cdd:cd05323    81 LINNAGILDEKSYLFAGKLPPP--WEKTIDVNLTGVINTTYLALHYMDKNkggKGGVIVNIGSVAGLYPAPQFPVYSASK 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034574112 175 TFVDFFSQCLHEEYRSK-GVFVQSVLPYFVATKL 207
Cdd:cd05323   159 HGVVGFTRSLADLLEYKtGVRVNAICPGFTNTPL 192
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 23-207 1.71e-20

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 88.04  E-value: 1.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSeikekfkVETrtIAVDFASED-----IYDKIKtgLAGlEIGI 97
Cdd:PRK06179    9 VTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIPG-------VEL--LELDVTDDAsvqaaVDEVIA--RAG-RIDV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSyeypeyfldvpdldnVI-----------KKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPL 166
Cdd:PRK06179   77 LVNNAGVG---------------LAgaaeessiaqaQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPY 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034574112 167 LTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK06179  142 MALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNF 182
PRK08267 PRK08267
SDR family oxidoreductase;
22-220 2.19e-20

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 87.69  E-value: 2.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKE------KFKVETRTiAVDFASEDIydkikTGLAGLEI 95
Cdd:PRK08267    5 FITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAgnawtgALDVTDRA-AWDAALADF-----AAATGGRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 GILVNNVGMSYEYPeyFLDVPDLDnvIKKMININILSVCKMTQLVLPgMVERSKGA-ILNISSGSGMLPVPLLTIYSATK 174
Cdd:PRK08267   79 DVLFNNAGILRGGP--FEDIPLEA--HDRVIDINVKGVLNGAHAALP-YLKATPGArVINTSSASAIYGQPGLAVYSATK 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034574112 175 TFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPSP 220
Cdd:PRK08267  154 FAVRGLTEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEVDAGST 199
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-207 5.70e-20

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 86.31  E-value: 5.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLisRSKDKLDQVSSEIKEKFKVETRTIAV--DFAS----EDIYDKIKTGLAGLEIg 96
Cdd:PRK06077   11 VTGSGRGIGRAIAVRLAKEGSLVVV--NAKKRAEEMNETLKMVKENGGEGIGVlaDVSTregcETLAKATIDRYGVADI- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 iLVNNVGMSYEYPeyFLDVPDldNVIKKMININILSVCKMTQLVLPGMveRSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:PRK06077   88 -LVNNAGLGLFSP--FLNVDD--KLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSIYGAMKAA 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034574112 177 VDFFSQCLHEEYRSKgVFVQSVLPYFVATKL 207
Cdd:PRK06077  161 VINLTKYLALELAPK-IRVNAIAPGFVKTKL 190
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 23-209 1.20e-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: 1.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKIKTGLAGLEIgiLVNNV 102
Cdd:cd08944     8 VTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGGLDL--LVNNA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 103 G-MSYEYPEYFLDVPDLDNVIKkminINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFFS 181
Cdd:cd08944    86 GaMHLTPAIIDTDLAVWDQTMA----INLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLT 161

                         170       180
                  ....*....|....*....|....*...
gi 1034574112 182 QCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:cd08944   162 RTLAAELRHAGIRCNALAPGLIDTPLLL 189
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 23-261 1.29e-19

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 85.07  E-value: 1.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFK-VETRTIAV-DFAS-EDIYDKIKTGLAGLEIGILV 99
Cdd:cd05350     3 ITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPsVEVEILDVtDEERnQLVIAELEAELGGLDLVIIN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NNVGMsyeyPEYFLDVPDLDNviKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDF 179
Cdd:cd05350    83 AGVGK----GTSLGDLSFKAF--RETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 180 FSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPSPETFVKSAIKTVglqsRTNGYLI---HALMGSI--ISNLP 254
Cdd:cd05350   157 LAESLRYDVKKRGIRVTVINPGFIDTPLTANMFTMPFLMSVEQAAKRIYKAI----KKGAAEPtfpWRLAVPLrlLKLLP 232


                  ....*..
gi 1034574112 255 SWIYLKI 261
Cdd:cd05350   233 ERLRRRL 239
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 23-207 1.68e-19

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


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 85.59  E-value: 1.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfkvETRTIAV-----DFAS-EDIYDKIkTGLAGlEIG 96
Cdd:cd08935    10 ITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITAL---GGRAIALaadvlDRASlERAREEI-VAQFG-TVD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVG---------MSYEYPEYFLDVPDLD-NVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPL 166
Cdd:cd08935    85 ILINGAGgnhpdattdPEHYEPETEQNFFDLDeEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSPLTK 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034574112 167 LTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:cd08935   165 VPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQ 205
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 23-202 1.89e-19

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 85.20  E-value: 1.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASediYDKIKTGLAGLE-----IGI 97
Cdd:PRK07523   15 VTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQ-GLSAHALAFDVTD---HDAVRAAIDAFEaeigpIDI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPeyFLDVPdlDNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:PRK07523   91 LVNNAGMQFRTP--LEDFP--ADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKGAV 166

                         170       180
                  ....*....|....*....|....*.
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLP-YF 202
Cdd:PRK07523  167 GNLTKGMATDWAKHGLQCNAIAPgYF 192
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 22-208 2.85e-19

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


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 84.51  E-value: 2.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEK-FKVETRTIAVDfASEDIYDKIKTGLAGL-EIGILV 99
Cdd:cd08945     7 LVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAgVEADGRTCDVR-SVPEIEALVAAAVARYgPIDVLV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NNVGMSYEYpeyflDVPDL-DNVIKKMININILSVCKMTQLVLP--GMVERSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:cd08945    86 NNAGRSGGG-----ATAELaDELWLDVVETNLTGVFRVTKEVLKagGMLERGTGRIINIASTGGKQGVVHAAPYSASKHG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVATKLA 208
Cdd:cd08945   161 VVGFTKALGLELARTGITVNAVCPGFVETPMA 192
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 20-209 3.40e-19

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


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 83.65  E-value: 3.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  20 APFVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIkEKFKVETRTIAV-----------DFASEdiydkikt 88
Cdd:cd08931     2 AIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAEL-GAENVVAGALDVtdraawaaalaDFAAA-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  89 glAGLEIGILVNNVGMSYEYPeyFLDVPDLDNVIkkMININILSVCKMTQLVLPgMVERSKGA-ILNISSGSGMLPVPLL 167
Cdd:cd08931    73 --TGGRLDALFNNAGVGRGGP--FEDVPLAAHDR--MVDINVKGVLNGAYAALP-YLKATPGArVINTASSSAIYGQPDL 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034574112 168 TIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:cd08931   146 AVYSATKFAVRGLTEALDVEWARHGIRVADVWPWFVDTPILT 187
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 23-205 7.11e-19

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


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 83.20  E-value: 7.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfkvETRTIAV--DFASEDIYDKIkTGLAGLEIG---I 97
Cdd:cd05360     5 ITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVREL---GGEAIAVvaDVADAAQVERA-ADTAVERFGridT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEypEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:cd05360    81 WVNNAGVAVF--GRFEDVTPEE--FRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAV 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034574112 178 DFFSQCLHEEYRSKG--VFVQSVLPYFVAT 205
Cdd:cd05360   157 RGFTESLRAELAHDGapISVTLVQPTAMNT 186
PRK07201 PRK07201
SDR family oxidoreductase;
23-193 7.70e-19

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 86.16  E-value: 7.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASEDIYDK-IKTGLAGL-EIGILVN 100
Cdd:PRK07201  376 ITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAK-GGTAHAYTCDLTDSAAVDHtVKDILAEHgHVDYLVN 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMS--------------YEypeyfldvpdldnvikKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPL 166
Cdd:PRK07201  455 NAGRSirrsvenstdrfhdYE----------------RTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSIGVQTNAPR 518

                         170       180
                  ....*....|....*....|....*..
gi 1034574112 167 LTIYSATKTFVDFFSQCLHEEYRSKGV 193
Cdd:PRK07201  519 FSAYVASKAALDAFSDVAASETLSDGI 545
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 22-200 8.59e-19

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 83.57  E-value: 8.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFAS-EDIYDKIKTGLAGLEIgiLVN 100
Cdd:PRK12829   15 LVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGAKVTATVADVADPAQvERVFDTAVERFGGLDV--LVN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSYeyPEYFLDvpDLDNV-IKKMININILSVCKMTQLVLPGMVERSKG-AILNISSGSGMLPVPLLTIYSATKTFVD 178
Cdd:PRK12829   93 NAGIAG--PTGGID--EITPEqWEQTLAVNLNGQFYFARAAVPLLKASGHGgVIIALSSVAGRLGYPGRTPYAASKWAVV 168

                         170       180
                  ....*....|....*....|..
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK12829  169 GLVKSLAIELGPLGIRVNAILP 190
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 23-209 9.41e-19

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 83.27  E-value: 9.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLIS-RSKDKLDQVSSEIKEKFKVETRTIAVDF----ASEDIYDKIKTGLAGLEIgi 97
Cdd:cd08940     7 VTGSTSGIGLGIARALAAAGANIVLNGfGDAAEIEAVRAGLAAKHGVKVLYHGADLskpaAIEDMVAYAQRQFGGVDI-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPEYFLDVPDLDNVIKkminINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:cd08940    85 LVNNAGIQHVAPIEDFPTEKWDAIIA----LNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGV 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:cd08940   161 VGLTKVVALETAGTGVTCNAICPGWVLTPLVE 192
PRK06484 PRK06484
short chain dehydrogenase; Validated
 23-207 1.09e-18

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 85.29  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkfkvETRTIAVDFASEDiydKIKTGLAGLE-----IGI 97
Cdd:PRK06484   10 VTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGP----DHHALAMDVSDEA---QIREGFEQLHrefgrIDV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKG-AILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:PRK06484   83 LVNNAGVTDPTMTATLDTTLEE--FARLQAINLTGAYLVAREALRLMIEQGHGaAIVNVASGAGLVALPKRTAYSASKAA 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK06484  161 VISLTRSLACEWAAKGIRVNAVLPGYVRTQM 191
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 22-222 1.18e-18

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 83.48  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVV-----LISRSKDKLDQVSSEikekfkvETRTIAVDFA-SEDI-----YDKIKTGL 90
Cdd:cd09805     4 LITGCDSGFGNLLAKKLDSLGFTVLagcltKNGPGAKELRRVCSD-------RLRTLQLDVTkPEQIkraaqWVKEHVGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  91 AGLeiGILVNNVG-MSYEYPEYFLDVPDLdnviKKMININILSVCKMTQLVLPgMVERSKGAILNISSGSGMLPVPLLTI 169
Cdd:cd09805    77 KGL--WGLVNNAGiLGFGGDEELLPMDDY----RKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRVPFPAGGA 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 170 YSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLA-------KIRKPTLDKPSPET 222
Cdd:cd09805   150 YCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITgnselweKQAKKLWERLPPEV 209
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 22-200 1.31e-18

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: 82.33  E-value: 1.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAK--HGMKVVLISRSKDKLDQVSSEIKEKFKVetRTIAVDFASEDIYDKIKTGL--AGLEIGI 97
Cdd:cd05367     3 ILTGASRGIGRALAEELLKrgSPSVVVLLARSEEPLQELKEELRPGLRV--TTVKADLSDAAGVEQLLEAIrkLDGERDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPEYFLDvpDLDNvIKKMININILSVCKMTQLVLPGMVERS-KGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:cd05367    81 LINNAGSLGPVSKIEFI--DLDE-LQKYFDLNLTSPVCLTSTLLRAFKKRGlKKTVVNVSSGAAVNPFKGWGLYCSSKAA 157

                         170       180
                  ....*....|....*....|....
gi 1034574112 177 VDFFSQCLHEEYrsKGVFVQSVLP 200
Cdd:cd05367   158 RDMFFRVLAAEE--PDVRVLSYAP 179
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 23-217 1.79e-18

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


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 82.23  E-value: 1.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKeKFKVETRTIAVDFASE-DIYDKIKTGLAGL-EIGILVN 100
Cdd:cd05365     4 VTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQ-QAGGQAIGLECNVTSEqDLEAVVKATVSQFgGITILVN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSYEYPEyflDVPDLDNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFF 180
Cdd:cd05365    83 NAGGGGPKPF---DMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHM 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034574112 181 SQCLHEEYRSKGVFVQSVLPYFVATK-LAKIRKPTLDK 217
Cdd:cd05365   160 TRNLAFDLGPKGIRVNAVAPGAVKTDaLASVLTPEIER 197
PRK09291 PRK09291
SDR family oxidoreductase;
23-200 1.99e-18

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 82.35  E-value: 1.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASEdiYDKIKTglAGLEIGILVNNV 102
Cdd:PRK09291    7 ITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARR-GLALRVEKLDLTDA--IDRAQA--AEWDVDVLLNNA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 103 GMSYEYPeyFLDVPdLDNViKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFFSQ 182
Cdd:PRK09291   82 GIGEAGA--VVDIP-VELV-RELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALEAIAE 157

                         170
                  ....*....|....*...
gi 1034574112 183 CLHEEYRSKGVFVQSVLP 200
Cdd:PRK09291  158 AMHAELKPFGIQVATVNP 175
PRK07326 PRK07326
SDR family oxidoreductase;
22-205 2.16e-18

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 81.98  E-value: 2.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVetRTIAVD---FAS-EDIYDKIKTGLAGLEigI 97
Cdd:PRK07326   10 LITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNV--LGLAADvrdEADvQRAVDAIVAAFGGLD--V 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSyeypeYFLDVPDL-DNVIKKMININILSVCKMTQLVLPGMVeRSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:PRK07326   86 LIANAGVG-----HFAPVEELtPEEWRLVIDTNLTGAFYTIKAAVPALK-RGGGYIINISSLAGTNFFAGGAAYNASKFG 159

                         170       180
                  ....*....|....*....|....*....
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK07326  160 LVGFSEAAMLDLRQYGIKVSTIMPGSVAT 188
PRK07774 PRK07774
SDR family oxidoreductase;
23-257 2.88e-18

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 81.71  E-value: 2.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASED----IYDKIKTGLAGLEigIL 98
Cdd:PRK07774   11 VTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVAD-GGTAIAVQVDVSDPDsakaMADATVSAFGGID--YL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEYPEYFLDVPDLDNvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVpllTIYSATKTFVD 178
Cdd:PRK07774   88 VNNAAIYGGMKLDLLITVPWDY-YKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLYS---NFYGLAKVGLN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRkptldkpSPETFVKSAIKTVGLQSR-TNGYLIHALMgSIISNLPSWI 257
Cdd:PRK07774  164 GLTQQLARELGGMNIRVNAIAPGPIDTEATRTV-------TPKEFVADMVKGIPLSRMgTPEDLVGMCL-FLLSDEASWI 235
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 23-206 3.29e-18

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 82.26  E-value: 3.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEK----FKVETRTIAVDF---ASEDIYDKIKTglagleI 95
Cdd:PRK08277   15 ITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAggeaLAVKADVLDKESleqARQQILEDFGP------C 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 GILVNNVG----------MSYEYPEYFLDVPDLD-NVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPV 164
Cdd:PRK08277   89 DILINGAGgnhpkattdnEFHELIEPTKTFFDLDeEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAFTPL 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034574112 165 PLLTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATK 206
Cdd:PRK08277  169 TKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE 210
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 22-205 5.19e-18

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 81.07  E-value: 5.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRS-KDKLDQVSSEIKEkFKVETRTIAVDFAS-EDIYDKIKTGLAGL-EIGIL 98
Cdd:PRK12825   10 LVTGAARGLGRAIALRLARAGADVVVHYRSdEEAAEELVEAVEA-LGRRAQAVQADVTDkAALEAAVAAAVERFgRIDIL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEYPeyFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVD 178
Cdd:PRK12825   89 VNNAGIFEDKP--LADMSDDE--WDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKAGLV 164

                         170       180
                  ....*....|....*....|....*..
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK12825  165 GLTKALARELAEYGITVNMVAPGDIDT 191
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 23-208 6.15e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 81.10  E-value: 6.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKdkLDQVSSEIkekfkvetRTIAVDFASED----IYDKIKTGLAGLEIgiL 98
Cdd:PRK06523   14 VTGGTKGIGAATVARLLEAGARVVTTARSR--PDDLPEGV--------EFVAADLTTAEgcaaVARAVLERLGGVDI--L 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEYPEYFLDVPDLDNVikKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTI-YSATKTFV 177
Cdd:PRK06523   82 VHVLGGSSAPAGGFAALTDEEWQ--DELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPESTTaYAAAKAAL 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLPYFVATKLA 208
Cdd:PRK06523  160 STYSKSLSKEVAPKGVRVNTVSPGWIETEAA 190
PRK06182 PRK06182
short chain dehydrogenase; Validated
 22-219 9.29e-18

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 80.77  E-value: 9.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSeikekfkVETRTIAVDFASEDiydKIKTGLAGLE-----IG 96
Cdd:PRK06182    7 LVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLAS-------LGVHPLSLDVTDEA---SIKAAVDTIIaeegrID 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGM-SYEYPEyflDVPdLDNViKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKT 175
Cdd:PRK06182   77 VLVNNAGYgSYGAIE---DVP-IDEA-RRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKF 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034574112 176 FVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPS 219
Cdd:PRK06182  152 ALEGFSDALRLEVAPFGIDVVVIEPGGIKTEWGDIAADHLLKTS 195
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 23-229 1.17e-17

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 79.82  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLdqvsSEIKEKFKVETRTIAV-DFASediydkIKTGLAGLE-IGILVN 100
Cdd:cd05368     7 ITAAAQGIGRAIALAFAREGANVIATDINEEKL----KELERGPGITTRVLDVtDKEQ------VAALAKEEGrIDVLFN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSYEypEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISS-GSGMLPVPLLTIYSATKTFVDF 179
Cdd:cd05368    77 CAGFVHH--GSILDCEDDD--WDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSvASSIKGVPNRFVYSTTKAAVIG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034574112 180 FSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRkpTLDKPSPETFVKSAIK 229
Cdd:cd05368   153 LTKSVAADFAQQGIRCNAICPGTVDTPSLEER--IQAQPDPEEALKAFAA 200
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 22-209 1.18e-17

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 79.59  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGM-KVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASED----IYDKIKTGLAGLEIg 96
Cdd:cd05324     4 LVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAE-GLSVRFHQLDVTDDAsieaAADFVEEKYGGLDI- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 iLVNNVGMSYEYpeyFLDVPDLDNVIKKMININILSVCKMTQLVLPgMVERSKGA-ILNISSGSGMLPVPlltiYSATKT 175
Cdd:cd05324    82 -LVNNAGIAFKG---FDDSTPTREQARETMKTNFFGTVDVTQALLP-LLKKSPAGrIVNVSSGLGSLTSA----YGVSKA 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034574112 176 FVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:cd05324   153 ALNALTRILAKELKETGIKVNACCPGWVKTDMGG 186
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 23-205 1.71e-17

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: 79.73  E-value: 1.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfkveTRTIAVDFASED----IYDKIKTGLAGLEIgiL 98
Cdd:cd05341    10 VTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDA----ARFFHLDVTDEDgwtaVVDTAREAFGRLDV--L 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYeyPEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVD 178
Cdd:cd05341    84 VNNAGILT--GGTVETTTLEE--WRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGAVR 159

                         170       180
                  ....*....|....*....|....*....
gi 1034574112 179 FFSQ--CLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:cd05341   160 GLTKsaALECATQGYGIRVNSVHPGYIYT 188
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 23-218 2.42e-17

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: 79.35  E-value: 2.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRS-KDKLDQVSSEIKekfKVETRTIAV--DFASE-DIYDKIKTGLAGLE-IGI 97
Cdd:cd05358     8 VTGASSGIGKAIAIRLATAGANVVVNYRSkEDAAEEVVEEIK---AVGGKAIAVqaDVSKEeDVVALFQSAIKEFGtLDI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPEYFLDVPDLDnvikKMININILSVCKMTQLVLPGMVE-RSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:cd05358    85 LVNNAGLQGDASSHEMTLEDWN----KVIDVNLTGQFLCAREAIKRFRKsKIKGKIINMSSVHEKIPWPGHVNYAASKGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVATklaKIRKPTLDKP 218
Cdd:cd05358   161 VKMMTKTLAQEYAPKGIRVNAIAPGAINT---PINAEAWDDP 199
PRK05855 PRK05855
SDR family oxidoreductase;
23-205 2.61e-17

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 81.57  E-value: 2.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkFKVETRTIAVDFASEDIYDKIKTGLAGlEIG---ILV 99
Cdd:PRK05855  320 VTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRA-AGAVAHAYRVDVSDADAMEAFAEWVRA-EHGvpdIVV 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NN--VGMSyeypEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGA-ILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:PRK05855  398 NNagIGMA----GGFLDTSAED--WDRVLDVNLWGVIHGCRLFGRQMVERGTGGhIVNVASAAAYAPSRSLPAYATSKAA 471

                         170       180
                  ....*....|....*....|....*....
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK05855  472 VLMLSECLRAELAAAGIGVTAICPGFVDT 500
PRK08264 PRK08264
SDR family oxidoreductase;
22-235 2.70e-17

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 78.78  E-value: 2.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHG-MKVVLISRSKDKLDQVSSeikekfKVETrtIAVDFAS-EDIYDKikTGLAGlEIGILV 99
Cdd:PRK08264   10 LVTGANRGIGRAFVEQLLARGaAKVYAAARDPESVTDLGP------RVVP--LQLDVTDpASVAAA--AEAAS-DVTILV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NNVGMSYeyPEYFLDVPDLDNVIKKMiNINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDF 179
Cdd:PRK08264   79 NNAGIFR--TGSLLLEGDEDALRAEM-ETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAAWS 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034574112 180 FSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRkpTLDKPSPETFVKSAIKtvGLQS 235
Cdd:PRK08264  156 LTQALRAELAPQGTRVLGVHPGPIDTDMAAGL--DAPKASPADVARQILD--ALEA 207
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 23-207 3.01e-17

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: 78.97  E-value: 3.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfkveTRTIAVDFASEDIYDKI------KTGlaglEIG 96
Cdd:cd05345    10 VTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEA----AIAIQADVTKRADVEAMveaalsKFG----RLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSYEyPEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:cd05345    82 ILVNNAGITHR-NKPMLEVDEEE--FDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGW 158

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:cd05345   159 VVTATKAMAVELAPRNIRVNCLCPVAGETPL 189
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 22-205 3.99e-17

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 78.30  E-value: 3.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIK-EKFKVETRTIAVDFASEDIYDKIKTGLAGLEIgiLVN 100
Cdd:PRK12828   11 AITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPaDALRIGGIDLVDPQAARRAVDEVNRQFGRLDA--LVN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVG-MSYEypeyflDVPDLD-NVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVD 178
Cdd:PRK12828   89 IAGaFVWG------TIADGDaDTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAGVA 162

                         170       180
                  ....*....|....*....|....*..
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK12828  163 RLTEALAAELLDRGITVNAVLPSIIDT 189
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 22-243 4.85e-17

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: 78.11  E-value: 4.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHG-MKVVLISRSKDKLDQVSSEIKEKFKVetRTIAVDFASE--DIYDKIKTGLAGLEIGIL 98
Cdd:cd05325     2 LITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAALGASHSRL--HILELDVTDEiaESAEAVAERLGDAGLDVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYeyPEYFLDVPDLDNvIKKMININILSVCKMTQLVLPGMVERSKGAILNISS--GS-GMLPVPLLTIYSATKT 175
Cdd:cd05325    80 INNAGILH--SYGPASEVDSED-LLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSrvGSiGDNTSGGWYSYRASKA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 176 FVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKiRKPTLDKP-SPETFVKSAIKTV-GLQSRTNGYLIH 243
Cdd:cd05325   157 ALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGG-PFAKNKGPiTPEESVAGLLKVIdNLNEEDSGKFLD 225
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 22-207 6.47e-17

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


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 78.42  E-value: 6.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKF---KVEtrTIAVDFAS--------EDIYDKIKtgl 90
Cdd:cd05327     5 VITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETgnaKVE--VIQLDLSSlasvrqfaEEFLARFP--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  91 aglEIGILVNNVGMSyeYPEYFLDVPDLDnvikKMININILSVCKMTQLVLPGMVERSKGAILNISSGS--------GML 162
Cdd:cd05327    80 ---RLDILINNAGIM--APPRRLTKDGFE----LQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAhragpidfNDL 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034574112 163 PVPLLTIYSATKTFVD------FFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:cd05327   151 DLENNKEYSPYKAYGQsklaniLFTRELARRLEGTGVTVNALHPGVVRTEL 201
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 23-200 6.49e-17

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 78.13  E-value: 6.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLI-----SRSKDKLDQVSSEIKEKFKVETrtiAVDFASEdiydkiKTGlaglEIGI 97
Cdd:PRK06171   14 VTGGSSGIGLAIVKELLANGANVVNAdihggDGQHENYQFVPTDVSSAEEVNH---TVAEIIE------KFG----RIDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSY---------EYPEYFLDVPDLDnvikKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLT 168
Cdd:PRK06171   81 LVNNAGINIprllvdekdPAGKYELNEAAFD----KMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQS 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 169 IYSATKTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK06171  157 CYAATKAALNSFTRSWAKELGKHNIRVVGVAP 188
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 23-207 7.08e-17

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: 77.76  E-value: 7.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASediYDKIKTGLAGLE-----IGI 97
Cdd:cd05352    13 VTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSS---QESVEKTFKQIQkdfgkIDI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPeyFLDVPdLDNViKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLP-VPLL-TIYSATKT 175
Cdd:cd05352    90 LIANAGITVHKP--ALDYT-YEQW-NKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVnRPQPqAAYNASKA 165

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 176 FVDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:cd05352   166 AVIHLAKSLAVEWAKYFIRVNSISPGYIDTDL 197
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 23-200 1.12e-16

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 77.46  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDK-LDQVSSEIKekfKVETRTIAV--DFASE-DIYDKIKTGLAglEIG-- 96
Cdd:PRK08936   12 ITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEeANDVAEEIK---KAGGEAIAVkgDVTVEsDVVNLIQTAVK--EFGtl 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 -ILVNNVGMSYEYPEYFLDVPDLDnvikKMININILSVCKMTQLVLPGMVERS-KGAILNISSGSGMLPVPLLTIYSATK 174
Cdd:PRK08936   87 dVMINNAGIENAVPSHEMSLEDWN----KVINTNLTGAFLGSREAIKYFVEHDiKGNIINMSSVHEQIPWPLFVHYAASK 162

                         170       180
                  ....*....|....*....|....*.
gi 1034574112 175 TFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK08936  163 GGVKLMTETLAMEYAPKGIRVNNIGP 188
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 22-207 1.33e-16

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 77.23  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASEdiyDKIKTGLAGLE-----IG 96
Cdd:PRK12429    8 LVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKA-GGKAIGVAMDVTDE---EAINAGIDYAVetfggVD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSY-----EYP-EYFldvpdldnviKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIY 170
Cdd:PRK12429   84 ILVNNAGIQHvapieDFPtEKW----------KKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAY 153

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1034574112 171 SATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK12429  154 VSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTPL 190
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 22-200 1.69e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 77.26  E-value: 1.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkfkvetRTIAVDFASEDiYDKIKTGLAGLE-----IG 96
Cdd:PRK06180    8 LITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPD------RALARLLDVTD-FDAIDAVVADAEatfgpID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSYEypEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:PRK06180   81 VLVNNAGYGHE--GAIEESPLAE--MRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFA 156

                         170       180
                  ....*....|....*....|....
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK06180  157 LEGISESLAKEVAPFGIHVTAVEP 180
PRK06949 PRK06949
SDR family oxidoreductase;
22-207 1.97e-16

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 76.72  E-value: 1.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIkEKFKVETRTIAVDFASediYDKIKTGLAGLE-----IG 96
Cdd:PRK06949   13 LVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEI-EAEGGAAHVVSLDVTD---YQSIKAAVAHAEteagtID 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSYEypEYFLDVP--DLDNVikkmININILSVCKMTQLVLPGMVERSKGA--------ILNISSGSGMLPVPL 166
Cdd:PRK06949   89 ILVNNSGVSTT--QKLVDVTpaDFDFV----FDTNTRGAFFVAQEVAKRMIARAKGAgntkpggrIINIASVAGLRVLPQ 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034574112 167 LTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK06949  163 IGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEI 203
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 29-209 2.11e-16

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 76.32  E-value: 2.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  29 GIGKSYAEELAKHGMKVVLISRSKDKLDQVSsEIKEKFKVETrtIAVDFASED----IYDKIKTGLAGLEIgiLVNNVGM 104
Cdd:pfam13561   7 GIGWAIARALAEEGAEVVLTDLNEALAKRVE-ELAEELGAAV--LPCDVTDEEqveaLVAAAVEKFGRLDI--LVNNAGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 105 SYEYPEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERskGAILNISSGSGMLPVPLLTIYSATKTFVDFFSQCL 184
Cdd:pfam13561  82 APKLKGPFLDTSRED--FDRALDVNLYSLFLLAKAALPLMKEG--GSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYL 157

                         170       180
                  ....*....|....*....|....*
gi 1034574112 185 HEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:pfam13561 158 AVELGPRGIRVNAISPGPIKTLAAS 182
PRK09072 PRK09072
SDR family oxidoreductase;
24-207 2.97e-16

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 76.52  E-value: 2.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  24 TGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETrtIAVDFASEDIYDKIKTgLAGLEIGI--LVNN 101
Cdd:PRK09072   11 TGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGRHRW--VVADLTSEAGREAVLA-RAREMGGInvLINN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 102 VGMSYeypeyFLDVPDLDNV-IKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFF 180
Cdd:PRK09072   88 AGVNH-----FALLEDQDPEaIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFALRGF 162

                         170       180
                  ....*....|....*....|....*..
gi 1034574112 181 SQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK09072  163 SEALRRELADTGVRVLYLAPRATRTAM 189
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 23-174 4.69e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 76.88  E-value: 4.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFkVETRTIAVDFASED----IYDKIKTGLAGLEigIL 98
Cdd:PRK07109   13 ITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAG-GEALAVVADVADAEavqaAADRAEEELGPID--TW 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034574112  99 VNNVGMSYEYPeyFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATK 174
Cdd:PRK07109   90 VNNAMVTVFGP--FEDVTPEE--FRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAK 161
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 23-232 5.49e-16

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 75.66  E-value: 5.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQ-VSSEIKEKFKVETRTIAVDFAsEDIYDKIKTG--LAGlEIGILV 99
Cdd:cd08936    15 VTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRaVATLQGEGLSVTGTVCHVGKA-EDRERLVATAvnLHG-GVDILV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NNVGMSyeyPEYFLDVPDLDNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDF 179
Cdd:cd08936    93 SNAAVN---PFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVSKTALLG 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034574112 180 FSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRkpTLDKPSPETFVKS-AIKTVG 232
Cdd:cd08936   170 LTKNLAPELAPRNIRVNCLAPGLIKTSFSSAL--WMDKAVEESMKETlRIRRLG 221
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 22-216 6.92e-16

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 75.48  E-value: 6.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASEDiydKIKTGLAGLE-----IG 96
Cdd:PRK07097   14 LITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYREL-GIEAHGYVCDVTDED---GVQAMVSQIEkevgvID 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSYEYPeyFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:PRK07097   90 ILVNNAGIIKRIP--MLEMSAED--FRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAAKGG 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVAT-KLAKIRKPTLD 216
Cdd:PRK07097  166 LKMLTKNIASEYGEANIQCNGIGPGYIATpQTAPLRELQAD 206
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 22-207 7.58e-16

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 74.95  E-value: 7.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKIKTGLAGLEIgiLVNN 101
Cdd:PRK12936   10 LVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLEGVDI--LVNN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 102 VGMSYEYPEYFLDVPDLDNVIKkminINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFFS 181
Cdd:PRK12936   88 AGITKDGLFVRMSDEDWDSVLE----VNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIGFS 163

                         170       180
                  ....*....|....*....|....*.
gi 1034574112 182 QCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK12936  164 KSLAQEIATRNVTVNCVAPGFIESAM 189
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 22-228 1.33e-15

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: 74.35  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLD------------QVSSEIKEKfKVETRTIAVDFASEDIYDKI--- 86
Cdd:cd05338     7 FVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDngsakslpgtieETAEEIEAA-GGQALPIVVDVRDEDQVRALvea 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  87 ---KTGlaglEIGILVNNVGMSYEypEYFLDVP----DLdnvikkMININILSVCKMTQLVLPGMVERSKGAILNISSGS 159
Cdd:cd05338    86 tvdQFG----RLDILVNNAGAIWL--SLVEDTPakrfDL------MQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034574112 160 GMLPVPLLTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLP-----YFVATKLAKIRKPTlDKPSPETFVKSAI 228
Cdd:cd05338   154 SLRPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPstaieTPAATELSGGSDPA-RARSPEILSDAVL 226
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 23-236 1.80e-15

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 73.76  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFAS------EDIYDKIKTGLAGLEiG 96
Cdd:cd05340     9 VTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFILDLLTctsencQQLAQRIAVNYPRLD-G 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILvNNVGMSYE-YPEYFLDvpdlDNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKT 175
Cdd:cd05340    88 VL-HNAGLLGDvCPLSEQN----PQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSKF 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034574112 176 FVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDK---PSPETFVKSAIKTVGLQSR 236
Cdd:cd05340   163 ATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAFPTEDPqklKTPADIMPLYLWLMGDDSR 226
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 23-209 2.01e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 73.92  E-value: 2.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkfkvETRTIAVDFASEDIYDKIKTGLAGL--EIGILVN 100
Cdd:PRK06841   20 VTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGG----NAKGLVCDVSDSQSVEAAVAAVISAfgRIDILVN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSYEYPEYFLDVPDLDnvikKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFF 180
Cdd:PRK06841   96 SAGVALLAPAEDVSEEDWD----KTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASKAGVVGM 171

                         170       180
                  ....*....|....*....|....*....
gi 1034574112 181 SQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:PRK06841  172 TKVLALEWGPYGITVNAISPTVVLTELGK 200
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 23-207 2.42e-15

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 73.50  E-value: 2.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVL-ISRSKDKLDQVSSEIK----EKFKVETRTIAVDFASEdIYDKIKTGLAGLEIgi 97
Cdd:PRK12935   11 VTGGAKGIGKAITVALAQEGAKVVInYNSSKEAAENLVNELGkeghDVYAVQADVSKVEDANR-LVEEAVNHFGKVDI-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPEYFLDVPDLdnviKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:PRK12935   88 LVNNAGITRDRTFKKLNREDW----ERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAGM 163

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK12935  164 LGFTKSLALELAKTNVTVNAICPGFIDTEM 193
PRK07035 PRK07035
SDR family oxidoreductase;
22-208 2.57e-15

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 73.51  E-value: 2.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEK-FKVEtrTIAVDFAS-EDI---YDKIKTGLAGLEig 96
Cdd:PRK07035   12 LVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAgGKAE--ALACHIGEmEQIdalFAHIRERHGRLD-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSyeyPeYFLDVPDLD-NVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKT 175
Cdd:PRK07035   88 ILVNNAAAN---P-YFGHILDTDlGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITKA 163

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034574112 176 FVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLA 208
Cdd:PRK07035  164 AVISMTKAFAKECAPFGIRVNALLPGLTDTKFA 196
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 23-221 2.60e-15

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 73.78  E-value: 2.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIkEKFKVETRTIAVDFASED----IYDKIKTGLAGLEigIL 98
Cdd:PRK13394   12 VTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEI-NKAGGKAIGVAMDVTNEDavnaGIDKVAERFGSVD--IL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEYPEYFLDVPDLdnviKKMININILSVCKMTQLVLPGMV-ERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:PRK13394   89 VSNAGIQIVNPIENYSFADW----KKMQAIHVDGAFLTTKAALKHMYkDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGL 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLPYFVatklakiRKPTLDKPSPE 221
Cdd:PRK13394  165 LGLARVLAKEGAKHNVRSHVVCPGFV-------RTPLVDKQIPE 201
PRK05650 PRK05650
SDR family oxidoreductase;
22-214 5.83e-15

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 72.77  E-value: 5.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEK----FKVEtrtiaVDFASED----IYDKIKTGLAGl 93
Cdd:PRK05650    4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAggdgFYQR-----CDVRDYSqltaLAQACEEKWGG- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  94 eIGILVNNVGMSYEypEYFLDVP--DLDNVIkkmiNINILSVCKMTQLVLPgMVERSK-GAILNISSGSGMLPVPLLTIY 170
Cdd:PRK05650   78 -IDVIVNNAGVASG--GFFEELSleDWDWQI----AINLMGVVKGCKAFLP-LFKRQKsGRIVNIASMAGLMQGPAMSSY 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034574112 171 SATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLA-KIRKPT 214
Cdd:PRK05650  150 NVAKAGVVALSETLLVELADDEIGVHVVCPSFFQTNLLdSFRGPN 194
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 23-205 1.16e-14

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: 72.02  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDK-LDQVSSEIKEkFKVETRTIAVDFASED----IYDKIKTGLAGLEIgi 97
Cdd:cd05366     7 ITGAAQGIGRAIAERLAADGFNIVLADLNLEEaAKSTIQEISE-AGYNAVAVGADVTDKDdveaLIDQAVEKFGSFDV-- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPeyFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVER-SKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:cd05366    84 MVNNAGIAPITP--LLTITEED--LKKVYAVNVFGVLFGIQAAARQFKKLgHGGKIINASSIAGVQGFPNLGAYSASKFA 159

                         170       180
                  ....*....|....*....|....*....
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:cd05366   160 VRGLTQTAAQELAPKGITVNAYAPGIVKT 188
PRK06484 PRK06484
short chain dehydrogenase; Validated
 5-205 1.33e-14

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 73.34  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112   5 SRPAASSVTRCPPWFAP---FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQvsseIKEKFKVETRTIAVDFASED 81
Cdd:PRK06484  253 SGPASTAQAPSPLAESPrvvAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKK----LAEALGDEHLSVQADITDEA 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  82 IYDKIKTGLAGL--EIGILVNNVGMSyeypEYFldVPDLDN---VIKKMININILSVCKMTQLVLPGMveRSKGAILNIS 156
Cdd:PRK06484  329 AVESAFAQIQARwgRLDVLVNNAGIA----EVF--KPSLEQsaeDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLG 400

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034574112 157 SGSGMLPVPLLTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK06484  401 SIASLLALPPRNAYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449
PRK06914 PRK06914
SDR family oxidoreductase;
22-200 1.46e-14

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 71.98  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkFKVETRtIAV------DFAS-EDIYDKIKT-Glagl 93
Cdd:PRK06914    7 IVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQ-LNLQQN-IKVqqldvtDQNSiHNFQLVLKEiG---- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  94 EIGILVNNVGmsYEYPEYFLDVPdLDNVIKKMiNINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSAT 173
Cdd:PRK06914   81 RIDLLVNNAG--YANGGFVEEIP-VEEYRKQF-ETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSS 156

                         170       180
                  ....*....|....*....|....*..
gi 1034574112 174 KTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK06914  157 KYALEGFSESLRLELKPFGIDVALIEP 183
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 20-237 1.57e-14

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


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 71.00  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  20 APFVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfkveTRTIAVDFASED----IYDKIKTGLAGLEi 95
Cdd:cd08929     2 AALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEG----VLGLAGDVRDEAdvrrAVDAMEEAFGGLD- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 gILVNNVGMSYEYP-------EYFLDVPDldnvikkminiNILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLT 168
Cdd:cd08929    77 -ALVNNAGVGVMKPveeltpeEWRLVLDT-----------NLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGA 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034574112 169 IYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPSPETFVKSAIKTVGLQSRT 237
Cdd:cd08929   145 AYNASKFGLLGLSEAAMLDLREANIRVVNVMPGSVDTGFAGSPEGQAWKLAPEDVAQAVLFALEMPARA 213
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 23-235 1.57e-14

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: 71.55  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLI--SRSKDKLDQVSSEIKEKfKVETRTIAVDFASE----DIYDKIKTGLAGLEIg 96
Cdd:cd05355    31 ITGGDSGIGRAVAIAFAREGADVAINylPEEEDDAEETKKLIEEE-GRKCLLIPGDLGDEsfcrDLVKEVVKEFGKLDI- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 iLVNNVGMSYEYPeyflDVPDLDNV-IKKMININILSVCKMTQLVLPGMveRSKGAILNISSGSGMLPVPLLTIYSATKT 175
Cdd:cd05355   109 -LVNNAAYQHPQE----SIEDITTEqLEKTFRTNIFSMFYLTKAALPHL--KKGSSIINTTSVTAYKGSPHLLDYAATKG 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 176 FVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAkirkptldkpsPETFVKSAIKTVGLQS 235
Cdd:cd05355   182 AIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLI-----------PSSFPEEKVSEFGSQV 230
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-213 1.84e-14

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 71.14  E-value: 1.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIkEKFKVETRTIAVDFASE----DIYDKIKTGLAGleIGIL 98
Cdd:PRK08217   10 ITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAEC-GALGTEVRGYAANVTDEedveATFAQIAEDFGQ--LNGL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEypEYFLDVPDlDNVIKKM--------ININILSVCKMTQLVLPGMVE-RSKGAILNISSGS-----GMlpv 164
Cdd:PRK08217   87 INNAGILRD--GLLVKAKD-GKVTSKMsleqfqsvIDVNLTGVFLCGREAAAKMIEsGSKGVIINISSIAragnmGQ--- 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034574112 165 pllTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKP 213
Cdd:PRK08217  161 ---TNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKP 206
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 23-208 2.00e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 70.90  E-value: 2.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKekfkveTRTIAVDFASEDIYDKIKTGLAGLEIgiLVNNV 102
Cdd:PRK07060   14 VTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETG------CEPLRLDVGDDAAIRAALAAAGAFDG--LVNCA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 103 GMSYEypEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVE-RSKGAILNISSGSGMLPVPLLTIYSATKTFVDFFS 181
Cdd:PRK07060   86 GIASL--ESALDMTAEG--FDRVMAVNARGAALVARHVARAMIAaGRGGSIVNVSSQAALVGLPDHLAYCASKAALDAIT 161

                         170       180
                  ....*....|....*....|....*..
gi 1034574112 182 QCLHEEYRSKGVFVQSVLPYFVATKLA 208
Cdd:PRK07060  162 RVLCVELGPHGIRVNSVNPTVTLTPMA 188
PRK07063 PRK07063
SDR family oxidoreductase;
22-208 2.11e-14

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 71.24  E-value: 2.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkfkvETRTIAVDFASEDIYDK--IKTGLAGLE----- 94
Cdd:PRK07063   11 LVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIAR----DVAGARVLAVPADVTDAasVAAAVAAAEeafgp 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  95 IGILVNNVGMS-YEYPeyfLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSAT 173
Cdd:PRK07063   87 LDVLVNNAGINvFADP---LAMTDED--WRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVA 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034574112 174 KTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLA 208
Cdd:PRK07063  162 KHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLT 196
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
23-211 2.18e-14

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 70.92  E-value: 2.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVvLISRSKDKLDQVSSEIKEkfkvETRTIA---VDFASEDIYDKI-KTGLAGL-EIGI 97
Cdd:PRK06935   20 VTGGNTGLGQGYAVALAKAGADI-IITTHGTNWDETRRLIEK----EGRKVTfvqVDLTKPESAEKVvKEALEEFgKIDI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPeyFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSgsgMLP------VPlltIYS 171
Cdd:PRK06935   95 LVNNAGTIRRAP--LLEYKDED--WNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIAS---MLSfqggkfVP---AYT 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034574112 172 ATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATK-LAKIR 211
Cdd:PRK06935  165 ASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTAnTAPIR 205
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 22-208 2.19e-14

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 71.22  E-value: 2.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDqvssEIKEKFKVETRTIAVDFASED-IYDKIKTGLAGL-EIGILV 99
Cdd:PRK08263    7 FITGASRGFGRAWTEAALERGDRVVATARDTATLA----DLAEKYGDRLLPLALDVTDRAaVFAAVETAVEHFgRLDIVV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NN-----VGMSYEYPEyfldvpdldNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATK 174
Cdd:PRK08263   83 NNagyglFGMIEEVTE---------SEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASK 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034574112 175 TFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLA 208
Cdd:PRK08263  154 WALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWA 187
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 23-209 3.19e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 70.55  E-value: 3.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEK--------FKVeTRTIAVDFASEDIYDKIKTglagle 94
Cdd:PRK08085   14 ITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEgikahaapFNV-THKQEVEAAIEHIEKDIGP------ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  95 IGILVNNVGMSYEYPeyFLDVP--DLDNVIkkmiNINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSA 172
Cdd:PRK08085   87 IDVLINNAGIQRRHP--FTEFPeqEWNDVI----AVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAA 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1034574112 173 TKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:PRK08085  161 SKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTK 197
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 22-208 4.57e-14

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 70.77  E-value: 4.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAV--DFASEDIYDKIKTGLAGleIGILV 99
Cdd:PRK05872   13 VVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVLTVVADVtdLAAMQAAAEEAVERFGG--IDVVV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NNVGMSyeYPEYFLDV-PDLdnvIKKMININILSVCKMTQLVLPGMVERsKGAILNISSGSGMLPVPLLTIYSATKTFVD 178
Cdd:PRK05872   91 ANAGIA--SGGSVAQVdPDA---FRRVIDVNLLGVFHTVRATLPALIER-RGYVLQVSSLAAFAAAPGMAAYCASKAGVE 164

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVLPYFVATKLA 208
Cdd:PRK05872  165 AFANALRLEVAHHGVTVGSAYLSWIDTDLV 194
PRK07577 PRK07577
SDR family oxidoreductase;
23-213 4.57e-14

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 69.76  E-value: 4.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDkldqvsseikEKFKVEtrTIAVDFA----SEDIYDKIktgLAGLEIGIL 98
Cdd:PRK07577    8 VTGATKGIGLALSLRLANLGHQVIGIARSAI----------DDFPGE--LFACDLAdieqTAATLAQI---NEIHPVDAI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEYPEYFLDVPDLDNVikkmININILSVCKMTQLVLPGMVERSKGAILNISSGSgMLPVPLLTIYSATKTFVD 178
Cdd:PRK07577   73 VNNVGIALPQPLGKIDLAALQDV----YDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRA-IFGALDRTSYSAAKSALV 147

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKP 213
Cdd:PRK07577  148 GCTRTWALELAEYGITVNAVAPGPIETELFRQTRP 182
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 22-200 5.52e-14

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: 69.92  E-value: 5.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFAS-EDIYDKIKTGLAGL-EIGILV 99
Cdd:cd05369     7 FITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGRAHPIQCDVRDpEAVEAAVDETLKEFgKIDILI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NNVGMSYEYPeyfldVPDLD-NVIKKMININILSVCKMTQLVLPGMVERSKGA-ILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:cd05369    87 NNAAGNFLAP-----AESLSpNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHGGsILNISATYAYTGSPFQVHSAAAKAGV 161

                         170       180
                  ....*....|....*....|...
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:cd05369   162 DALTRSLAVEWGPYGIRVNAIAP 184
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 23-160 1.11e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 69.30  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKIKTGLAglEIGILVNNV 102
Cdd:PRK06125   12 ITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVDVAVHALDLSSPEAREQLAAEAG--DIDILVNNA 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 103 GmsyeypeyflDVP--DLDNV----------IKKMININilsvckMTQLVLPGMVERSKGAILNISSGSG 160
Cdd:PRK06125   90 G----------AIPggGLDDVddaawragweLKVFGYID------LTRLAYPRMKARGSGVIVNVIGAAG 143
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-221 1.24e-13

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 69.04  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKV-VLISRSKDKLDQVSSEIKEKFK--VETRTiAVDFASEDIYDKIKtglaglEIGILV 99
Cdd:PRK06463   12 ITGGTRGIGRAIAEAFLREGAKVaVLYNSAENEAKELREKGVFTIKcdVGNRD-QVKKSKEVVEKEFG------RVDVLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NNVGMSYEYPEYFLDvpdlDNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGM-LPVPLLTIYSATKTFVD 178
Cdd:PRK06463   85 NNAGIMYLMPFEEFD----EEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgTAAEGTTFYAITKAGII 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVLPYFVATKLakirkpTLDKPSPE 221
Cdd:PRK06463  161 ILTRRLAFELGKYGIRVNAVAPGWVETDM------TLSGKSQE 197
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 22-205 1.52e-13

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: 68.53  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISR-SKDKLDQVSSEIKEKFKVETRTIAVDFASEDI---YDKIKTGLAGLEIgi 97
Cdd:cd05359     2 LVTGGSRGIGKAIALRLAERGADVVINYRkSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVeemFAAVKERFGRLDV-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPEYFLDVPDLDNVIkkmiNINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:cd05359    80 LVSNAAAGAFRPLSELTPAHWDAKM----NTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAAL 155

                         170       180
                  ....*....|....*....|....*...
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:cd05359   156 EALVRYLAVELGPRGIRVNAVSPGVIDT 183
PRK07814 PRK07814
SDR family oxidoreductase;
23-199 1.77e-13

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 68.65  E-value: 1.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKvETRTIAVDFASEDiydkIKTGLAGLEIG------ 96
Cdd:PRK07814   15 VTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGR-RAHVVAADLAHPE----ATAGLAGQAVEafgrld 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSyeYPEYFLD--VPDLDNVIKkminINILSVCKMTQLVLPGMVERS-KGAILNISSGSGMLPVPLLTIYSAT 173
Cdd:PRK07814   90 IVVNNVGGT--MPNPLLStsTKDLADAFT----FNVATAHALTVAAVPLMLEHSgGGSVINISSTMGRLAGRGFAAYGTA 163

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034574112 174 KTFVDFF----SQCLHEEYRSKGVFVQSVL 199
Cdd:PRK07814  164 KAALAHYtrlaALDLCPRIRVNAIAPGSIL 193
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 23-200 1.88e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 68.45  E-value: 1.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKvetRTIAVdfaSEDIYDK------IKTGLAGL-EI 95
Cdd:PRK07890   10 VSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGR---RALAV---PTDITDEdqcanlVALALERFgRV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 GILVNNvgmSYEYPeYFLDVPDLD-NVIKKMININILSVCKMTQLVLPGMVErSKGAILNISSGSGMLPVPLLTIYSATK 174
Cdd:PRK07890   84 DALVNN---AFRVP-SMKPLADADfAHWRAVIELNVLGTLRLTQAFTPALAE-SGGSIVMINSMVLRHSQPKYGAYKMAK 158

                         170       180
                  ....*....|....*....|....*.
gi 1034574112 175 TFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK07890  159 GALLAASQSLATELGPQGIRVNSVAP 184
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 23-212 2.05e-13

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 68.32  E-value: 2.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSkDKLDQVSSEIKEKfKVETRTIAVDFASEDIYDKIKTglAGLE----IGIL 98
Cdd:cd08937     9 VTGAAQGIGRGVAERLAGEGARVLLVDRS-ELVHEVLAEILAA-GDAAHVHTADLETYAGAQGVVR--AAVErfgrVDVL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSY------EYPEyfldvpdldNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGS--GMLPVPlltiY 170
Cdd:cd08937    85 INNVGGTIwakpyeHYEE---------EQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIAtrGIYRIP----Y 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034574112 171 SATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRK 212
Cdd:cd08937   152 SAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPR 193
PRK07832 PRK07832
SDR family oxidoreductase;
22-220 2.17e-13

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 68.53  E-value: 2.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASediYDKIKTGLAGLE-----IG 96
Cdd:PRK07832    4 FVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPEHRALDISD---YDAVAAFAADIHaahgsMD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSYeypeyFLDVPDLDNV-IKKMININILSVCKMTQLVLPGMVERSKGA-ILNISSGSGMLPVPLLTIYSATK 174
Cdd:PRK07832   81 VVMNIAGISA-----WGTVDRLTHEqWRRMVDVNLMGPIHVIETFVPPMVAAGRGGhLVNVSSAAGLVALPWHAAYSASK 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1034574112 175 TFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK-IRKPTLDKPSP 220
Cdd:PRK07832  156 FGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNtVEIAGVDREDP 202
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 23-200 2.36e-13

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 68.05  E-value: 2.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSkDKLDQVSSEIKEKfKVETRTIAVDF-ASEDIYDKIKTGLAGL-EIGILVN 100
Cdd:PRK12823   13 VTGAAQGIGRGVALRAAAEGARVVLVDRS-ELVHEVAAELRAA-GGEALALTADLeTYAGAQAAMAAAVEAFgRIDVLIN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMS--------YEYPEyfldvpdldnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGS--GMLPVPlltiY 170
Cdd:PRK12823   91 NVGGTiwakpfeeYEEEQ-----------IEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSIAtrGINRVP----Y 155

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034574112 171 SATKTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK12823  156 SAAKGGVNALTASLAFEYAEHGIRVNAVAP 185
PRK06172 PRK06172
SDR family oxidoreductase;
23-209 2.60e-13

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 67.85  E-value: 2.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIK----EKFKVETrTIAVDFASEDIYDKIKTGLAGLEIGIl 98
Cdd:PRK06172   12 VTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIReaggEALFVAC-DVTRDAEVKALVEQTIAAYGRLDYAF- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 vNNVGMSYEYPEYFLDVPDLDNVIkkmININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVD 178
Cdd:PRK06172   90 -NNAGIEIEQGRLAEGSEAEFDAI---MGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKHAVI 165

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:PRK06172  166 GLTKSAAIEYAKKGIRVNAVCPAVIDTDMFR 196
PRK06194 PRK06194
hypothetical protein; Provisional
 23-222 5.70e-13

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 67.35  E-value: 5.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASEDIYDKIktGLAGLE----IGIL 98
Cdd:PRK06194   11 ITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQ-GAEVLGVRTDVSDAAQVEAL--ADAALErfgaVHLL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEYPEYFLDVPDLDNVIkkmiNINILSVCKMTQLVLPGMVERSK------GAILNISSGSGMLPVPLLTIYSA 172
Cdd:PRK06194   88 FNNAGVGAGGLVWENSLADWEWVL----GVNLWGVIHGVRAFTPLMLAAAEkdpayeGHIVNTASMAGLLAPPAMGIYNV 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034574112 173 TKTFVDFFSQCLHEEYRSKGVFVQ-SVL-PYFVATKLA---KIRKPTLDKPSPET 222
Cdd:PRK06194  164 SKHAVVSLTETLYQDLSLVTDQVGaSVLcPYFVPTGIWqseRNRPADLANTAPPT 218
PRK05693 PRK05693
SDR family oxidoreductase;
22-209 9.78e-13

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 66.74  E-value: 9.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRskdKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKIKTGLAGLEIgiLVNN 101
Cdd:PRK05693    5 LITGCSSGIGRALADAFKAAGYEVWATAR---KAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEHGGLDV--LINN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 102 VGmsyeypeYFLDVPDLDNVIKKMIN---INILSVCKMTQLVLPGMvERSKGAILNISSGSGMLPVPLLTIYSATKTFVD 178
Cdd:PRK05693   80 AG-------YGAMGPLLDGGVEAMRRqfeTNVFAVVGVTRALFPLL-RRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVH 151

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:PRK05693  152 ALSDALRLELAPFGVQVMEVQPGAIASQFAS 182
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 23-217 1.05e-12

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 66.41  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfkvETRTIAV--DFASE-DIYDKIKTGLAGL-EIGIL 98
Cdd:PRK06113   16 ITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQL---GGQAFACrcDITSEqELSALADFALSKLgKVDIL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEYPeyfLDVPdLDNVIKKMiNINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVD 178
Cdd:PRK06113   93 VNNAGGGGPKP---FDMP-MADFRRAY-ELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAAS 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVLPYFVATK-LAKIRKPTLDK 217
Cdd:PRK06113  168 HLVRNMAFDLGEKNIRVNGIAPGAILTDaLKSVITPEIEQ 207
PRK07775 PRK07775
SDR family oxidoreductase;
3-200 1.19e-12

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 66.32  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112   3 PVSRPAassvtrcppwfapFVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDqvssEIKEKFKV---ETRTIAVDFAS 79
Cdd:PRK07775    8 PDRRPA-------------LVAGASSGIGAATAIELAAAGFPVALGARRVEKCE----ELVDKIRAdggEAVAFPLDVTD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  80 ED-IYDKIKTGLAGL-EIGILVNNVGMSYEYPEYFLDVPDLDnvikKMININILSVCKMTQLVLPGMVERSKGAILNISS 157
Cdd:PRK07775   71 PDsVKSFVAQAEEALgEIEVLVSGAGDTYFGKLHEISTEQFE----SQVQIHLVGANRLATAVLPGMIERRRGDLIFVGS 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034574112 158 GSGMLPVPLLTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK07775  147 DVALRQRPHMGAYGAAKAGLEAMVTNLQMELEGTGVRASIVHP 189
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 20-207 1.27e-12

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 65.92  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  20 APFVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKL-DQVSSEIKEKfkvETRTIAVDFASED------IYDKIKTGLAG 92
Cdd:PRK12937    7 VAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAaDELVAEIEAA---GGRAIAVQADVADaaavtrLFDAAETAFGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  93 leIGILVNNVGMSYEYPEYFLDVPDLDnvikKMININILSVCKMTQLVLPGMveRSKGAILNISSGSGMLPVPLLTIYSA 172
Cdd:PRK12937   84 --IDVLVNNAGVMPLGTIADFDLEDFD----RTIATNLRGAFVVLREAARHL--GQGGRIINLSTSVIALPLPGYGPYAA 155

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034574112 173 TKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK12937  156 SKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 23-195 4.22e-12

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: 64.55  E-value: 4.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAK----HGMKVVLISRSKDKLDQVSSEI-KEKFKVETRTIAVDFASE-DIYDKIKTGLA----- 91
Cdd:TIGR01500   5 VTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIgAERSGLRVVRVSLDLGAEaGLEQLLKALRElprpk 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  92 GLEIGILVNNVGMSYEYPEYFLDVPDLDNvIKKMININILSVCKMTQLVLPGMVER--SKGAILNISSGSGMLPVPLLTI 169
Cdd:TIGR01500  85 GLQRLLLINNAGTLGDVSKGFVDLSDSTQ-VQNYWALNLTSMLCLTSSVLKAFKDSpgLNRTVVNISSLCAIQPFKGWAL 163

                         170       180
                  ....*....|....*....|....*.
gi 1034574112 170 YSATKTFVDFFSQCLHEEYRSKGVFV 195
Cdd:TIGR01500 164 YCAGKAARDMLFQVLALEEKNPNVRV 189
PRK08219 PRK08219
SDR family oxidoreductase;
23-205 5.69e-12

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 63.80  E-value: 5.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHgMKVVLISRSKDKLDQVSSEIKEkfkveTRTIAVDFASediYDKIKTGLAGL-EIGILVNN 101
Cdd:PRK08219    8 ITGASRGIGAAIARELAPT-HTLLLGGRPAERLDELAAELPG-----ATPFPVDLTD---PEAIAAAVEQLgRLDVLVHN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 102 VGMSYEYPeyfldVPDLD-NVIKKMININILSVCKMTQLVLPGmVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFF 180
Cdd:PRK08219   79 AGVADLGP-----VAESTvDEWRATLEVNVVAPAELTRLLLPA-LRAAHGHVVFINSGAGLRANPGWGSYAASKFALRAL 152

                         170       180
                  ....*....|....*....|....*
gi 1034574112 181 SQCLHEEYRSKgVFVQSVLPYFVAT 205
Cdd:PRK08219  153 ADALREEEPGN-VRVTSVHPGRTDT 176
PRK08589 PRK08589
SDR family oxidoreductase;
23-217 5.80e-12

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 64.41  E-value: 5.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSkDKLDQVSSEIKEKFKvETRTIAVDFASE----DIYDKIKTGLAglEIGIL 98
Cdd:PRK08589   11 ITGASTGIGQASAIALAQEGAYVLAVDIA-EAVSETVDKIKSNGG-KAKAYHVDISDEqqvkDFASEIKEQFG--RVDVL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMS------YEYPeyfLDVPDldnvikKMININILSVCKMTQLVLPGMVERSkGAILNISSGSGMLPVPLLTIYSA 172
Cdd:PRK08589   87 FNNAGVDnaagriHEYP---VDVFD------KIMAVDMRGTFLMTKMLLPLMMEQG-GSIINTSSFSGQAADLYRSGYNA 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034574112 173 TKTFVDFFSQCLHEEYRSKGVFVQSVLPyfvatklAKIRKPTLDK 217
Cdd:PRK08589  157 AKGAVINFTKSIAIEYGRDGIRANAIAP-------GTIETPLVDK 194
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
22-200 6.22e-12

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 65.64  E-value: 6.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVetRTIAVDFASEdiyDKIKTGL--AGLEIG--- 96
Cdd:PRK08324  426 LVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPDRA--LGVACDVTDE---AAVQAAFeeAALAFGgvd 500

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSYEYPeyFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSK-GAILNISSGSGMLPVPLLTIYSATKT 175
Cdd:PRK08324  501 IVVSNAGIAISGP--IEETSDED--WRRSFDVNATGHFLVAREAVRIMKAQGLgGSIVFIASKNAVNPGPNFGAYGAAKA 576

                         170       180
                  ....*....|....*....|....*
gi 1034574112 176 FVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK08324  577 AELHLVRQLALELGPDGIRVNGVNP 601
PRK06138 PRK06138
SDR family oxidoreductase;
23-200 6.40e-12

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 64.02  E-value: 6.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFAS--EDIYDKIKTGLAGLEigILVN 100
Cdd:PRK06138   10 VTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAGGRAFARQGDVGSAEavEALVDFVAARWGRLD--VLVN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSYEYPEYFLDVPDLDNVIKkminINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFF 180
Cdd:PRK06138   88 NAGFGCGGTVVTTDEADWDAVMR----VNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAIASL 163

                         170       180
                  ....*....|....*....|
gi 1034574112 181 SQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK06138  164 TRAMALDHATDGIRVNAVAP 183
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
22-205 6.87e-12

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 63.98  E-value: 6.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKekfKVETRTIAV--DFASED----IYDKIKTGLAGLEi 95
Cdd:PRK08643    6 LVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLS---KDGGKAIAVkaDVSDRDqvfaAVRQVVDTFGDLN- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 gILVNNVGMSyeyPEYFLD--VPDldnVIKKMININILSVCKMTQLVLPGMVERSKGA-ILNISSGSGMLPVPLLTIYSA 172
Cdd:PRK08643   82 -VVVNNAGVA---PTTPIEtiTEE---QFDKVYNINVGGVIWGIQAAQEAFKKLGHGGkIINATSQAGVVGNPELAVYSS 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034574112 173 TKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK08643  155 TKFAVRGLTQTAARDLASEGITVNAYAPGIVKT 187
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 22-207 1.06e-11

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 63.55  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVL-ISRSKDKLDQVSSEIKEKFKvETRTIAVDFAS----EDIYDKIKTGL----AG 92
Cdd:PRK12747    8 LVTGASRGIGRAIAKRLANDGALVAIhYGNRKEEAEETVYEIQSNGG-SAFSIGANLESlhgvEALYSSLDNELqnrtGS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  93 LEIGILVNNVGMSyeyPEYFLDvPDLDNVIKKMININILSVCKMTQLVLPGMVERSKgaILNISSGSGMLPVPLLTIYSA 172
Cdd:PRK12747   87 TKFDILINNAGIG---PGAFIE-ETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNSR--IINISSAATRISLPDFIAYSM 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034574112 173 TKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK12747  161 TKGAINTMTFTLAKQLGARGITVNAILPGFIKTDM 195
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 22-234 1.61e-11

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 63.05  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkfkVETRTIAVDFASEDiYDKIKTGLAGL-----EIG 96
Cdd:PRK07576   13 VVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQ---AGPEGLGVSADVRD-YAAVEAAFAQIadefgPID 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNN---------VGMSyeypeyfldvpdlDNVIKKMININILSVCKMTQLVLPGMVeRSKGAILNISSGSGMLPVPLL 167
Cdd:PRK07576   89 VLVSGaagnfpapaAGMS-------------ANGFKTVVDIDLLGTFNVLKAAYPLLR-RPGASIIQISAPQAFVPMPMQ 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034574112 168 TIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVA-----TKLAkirkptldkPSPETfVKSAIKTVGLQ 234
Cdd:PRK07576  155 AHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPGPIAgtegmARLA---------PSPEL-QAAVAQSVPLK 216
PRK06114 PRK06114
SDR family oxidoreductase;
22-205 1.89e-11

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 62.88  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLIS-RSKDKLDQVSSEIkEKFKVETRTIAVDFAS----EDIYDKIKTGLAGLEIG 96
Cdd:PRK06114   12 FVTGAGSGIGQRIAIGLAQAGADVALFDlRTDDGLAETAEHI-EAAGRRAIQIAADVTSkadlRAAVARTEAELGALTLA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ilVNNVGMSYEYPEYFLDVPDLdnviKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTI--YSATK 174
Cdd:PRK06114   91 --VNAAGIANANPAEEMEEEQW----QTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNRGLLQahYNASK 164

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034574112 175 TFVDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK06114  165 AGVIHLSKSLAMEWVGRGIRVNSISPGYTAT 195
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
23-212 3.29e-11

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 62.01  E-value: 3.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEK----FKVETRTIA-VDFASEDIYDKIKtgLAGLEIGI 97
Cdd:PRK06924    6 ITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKLAEQYNSnltfHSLDLQDVHeLETNFNEILSSIQ--EDNVSSIH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMsyeypeyfldVPDLDNV-------IKKMININILSVCKMTQLVLPGMVERS-KGAILNISSGSGMLPVPLLTI 169
Cdd:PRK06924   84 LINNAGM----------VAPIKPIekaeseeLITNVHLNLLAPMILTSTFMKHTKDWKvDKRVINISSGAAKNPYFGWSA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034574112 170 YSATKTFVDFFSQCLHEEYRSK--GVFVQSVLPYFVATKL-AKIRK 212
Cdd:PRK06924  154 YCSSKAGLDMFTQTVATEQEEEeyPVKIVAFSPGVMDTNMqAQIRS 199
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 23-199 3.88e-11

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 61.63  E-value: 3.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASED----IYDKIKTGLAGLEIgiL 98
Cdd:cd05373     4 VVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDeviaLFDLIEEEIGPLEV--L 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEYPeyFLDVPDldNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVD 178
Cdd:cd05373    82 VYNAGANVWFP--ILETTP--RVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALR 157

                         170       180
                  ....*....|....*....|.
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVL 199
Cdd:cd05373   158 ALAQSMARELGPKGIHVAHVI 178
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 22-200 5.22e-11

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


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 61.20  E-value: 5.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFAS-EDIYDKIKTGLAGL-EIGILV 99
Cdd:cd08930     6 LITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVIALELDITSkESIKELIESYLEKFgRIDILI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NNVGMS-YEYPEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGML--------------PV 164
Cdd:cd08930    86 NNAYPSpKVWGSRFEEFPYEQ--WNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIapdfriyentqmysPV 163

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1034574112 165 plltIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:cd08930   164 ----EYSVIKAGIIHLTKYLAKYYADTGIRVNAISP 195
PRK06124 PRK06124
SDR family oxidoreductase;
23-205 6.32e-11

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 61.27  E-value: 6.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEK--------FKVETRTiAVDFASEDIyDKIKTGLagle 94
Cdd:PRK06124   16 VTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAggaaealaFDIADEE-AVAAAFARI-DAEHGRL---- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  95 iGILVNNVGMSYEYPEYFLDVPDldnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATK 174
Cdd:PRK06124   90 -DILVNNVGARDRRPLAELDDAA----IRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAK 164

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034574112 175 TFVDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK06124  165 QGLTGLMRALAAEFGPHGITSNAIAPGYFAT 195
PRK06101 PRK06101
SDR family oxidoreductase;
22-218 6.55e-11

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 61.04  E-value: 6.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLD---QVSSEIKekfkvetrTIAVDFASediYDKIKTGLAGL----E 94
Cdd:PRK06101    5 LITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDelhTQSANIF--------TLAFDVTD---HPGTKAALSQLpfipE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  95 IGILvnNVGmSYEYpeyfLDVPDLD-NVIKKMININILSVCKMTQLVLPGMVERSKGAIlnISSGSGMLPVPLLTIYSAT 173
Cdd:PRK06101   74 LWIF--NAG-DCEY----MDDGKVDaTLMARVFNVNVLGVANCIEGIQPHLSCGHRVVI--VGSIASELALPRAEAYGAS 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034574112 174 KTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKirKPTLDKP 218
Cdd:PRK06101  145 KAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTD--KNTFAMP 187
PRK07069 PRK07069
short chain dehydrogenase; Validated
 22-205 8.04e-11

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 60.88  E-value: 8.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLIS-RSKDKLDQVSSEIKEKFKVETRTIAV-DFASEDIYD----KIKTGLAGLEI 95
Cdd:PRK07069    3 FITGAAGGLGRAIARRMAEQGAKVFLTDiNDAAGLDAFAAEINAAHGEGVAFAAVqDVTDEAQWQallaQAADAMGGLSV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 giLVNNVGMSYEYPeyfldVPDLD-NVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATK 174
Cdd:PRK07069   83 --LVNNAGVGSFGA-----IEQIElDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASK 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034574112 175 TFVDFFSQ--CLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK07069  156 AAVASLTKsiALDCARRGLDVRCNSIHPTFIRT 188
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 23-208 8.69e-11

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 60.55  E-value: 8.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRT-IAVDfasEDIYDKIKTGLA-GLEIGILVN 100
Cdd:cd05326     9 ITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFVHCdVTVE---ADVRAAVDTAVArFGRLDIMFN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSYEYPEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFF 180
Cdd:cd05326    86 NAGVLGAPCYSILETSLEE--FERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHAVLGL 163

                         170       180
                  ....*....|....*....|....*...
gi 1034574112 181 SQCLHEEYRSKGVFVQSVLPYFVATKLA 208
Cdd:cd05326   164 TRSAATELGEHGIRVNCVSPYGVATPLL 191
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 23-200 1.01e-10

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 60.61  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKF-KVETRTIAVDFASE---DIYDKIKTGLAGlEIGIL 98
Cdd:cd05330     8 ITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIApDAEVLLIKADVSDEaqvEAYVDATVEQFG-RIDGF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMsyEYPEYFLDVPDLDnVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVD 178
Cdd:cd05330    87 FNNAGI--EGKQNLTEDFGAD-EFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHGVV 163

                         170       180
                  ....*....|....*....|..
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVLP 200
Cdd:cd05330   164 GLTRNSAVEYGQYGIRINAIAP 185
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 23-223 1.06e-10

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 60.54  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRS-KDKLDQVSSEIKEKfkvETRTIAV------DFASEDIYDKIKTGLAGlEI 95
Cdd:cd09763     8 VTGASRGIGRGIALQLGEAGATVYITGRTiLPQLPGTAEEIEAR---GGKCIPVrcdhsdDDEVEALFERVAREQQG-RL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 GILVNNV------GMSYEYPEYF-LDVPDLDNvikkMININILSVCKMTQLVLPGMVERSKGAILNISSG---SGMLPVP 165
Cdd:cd09763    84 DILVNNAyaavqlILVGVAKPFWeEPPTIWDD----INNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTgglEYLFNVA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034574112 166 lltiYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPSPETF 223
Cdd:cd09763   160 ----YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEGSWHAKE 213
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 22-205 1.19e-10

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 60.64  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKIKTGLAGL-EIGILVN 100
Cdd:PRK08339   12 FTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSYIVADLTKREDLERTVKELKNIgEPDIFFF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSyeYPEYF--LDVPDLDNVIKKMININILsvckMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVD 178
Cdd:PRK08339   92 STGGP--KPGYFmeMSMEDWEGAVKLLLYPAVY----LTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRISMA 165

                         170       180
                  ....*....|....*....|....*..
gi 1034574112 179 FFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK08339  166 GLVRTLAKELGPKGITVNGIMPGIIRT 192
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 23-200 1.81e-10

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 59.71  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEikEKFKVETRTIAVDFASED----IYDKIKTGLAGLEigIL 98
Cdd:cd08943     6 VTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEA--AQGGPRALGVQCDVTSEAqvqsAFEQAVLEFGGLD--IV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEYPeyFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGA-ILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:cd08943    82 VSNAGIATSSP--IAETSLED--WNRSMDINLTGHFLVSREAFRIMKSQGIGGnIVFNASKNAVAPGPNAAAYSAAKAAE 157

                         170       180
                  ....*....|....*....|...
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:cd08943   158 AHLARCLALEGGEDGIRVNTVNP 180
PRK07062 PRK07062
SDR family oxidoreductase;
23-199 2.89e-10

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 59.28  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKvETRTIAvdfASEDIYDK------IKTGLAGL-EI 95
Cdd:PRK07062   13 VTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFP-GARLLA---ARCDVLDEadvaafAAAVEARFgGV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 GILVNNVGMSYEYPeyFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKT 175
Cdd:PRK07062   89 DMLVNNAGQGRVST--FADTTDDA--WRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATSAARA 164

                         170       180
                  ....*....|....*....|....
gi 1034574112 176 FVDFFSQCLHEEYRSKGVFVQSVL 199
Cdd:PRK07062  165 GLLNLVKSLATELAPKGVRVNSIL 188
PRK07023 PRK07023
SDR family oxidoreductase;
23-211 3.09e-10

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 58.87  E-value: 3.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDkldqvsSEIKEKFKVETRTIAVD---------FASEDIydkIKTGLAGL 93
Cdd:PRK07023    6 VTGHSRGLGAALAEQLLQPGIAVLGVARSRH------PSLAAAAGERLAEVELDlsdaaaaaaWLAGDL---LAAFVDGA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  94 EIGILVNNVGMSYeyPEYFLDVPDLDNVIKKmININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSAT 173
Cdd:PRK07023   77 SRVLLINNAGTVE--PIGPLATLDAAAIARA-VGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSVYCAT 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034574112 174 KTFVDFFSQCLHEEYRsKGVFVQSVLPYFVATKL-AKIR 211
Cdd:PRK07023  154 KAALDHHARAVALDAN-RALRIVSLAPGVVDTGMqATIR 191
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 23-200 4.84e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 58.40  E-value: 4.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkFKVETRTIAVDFASEDiYDKIKTGLA-----GLEIGI 97
Cdd:PRK07478   11 ITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRA-EGGEAVALAGDVRDEA-YAKALVALAverfgGLDIAF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 lvNNVGMSYEypeyFLDVPDLD-NVIKKMININILSVCKMTQLVLPGMVERSKGAILNISS----GSGMlpvPLLTIYSA 172
Cdd:PRK07478   89 --NNAGTLGE----MGPVAEMSlEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTfvghTAGF---PGMAAYAA 159

                         170       180
                  ....*....|....*....|....*...
gi 1034574112 173 TKTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK07478  160 SKAGLIGLTQVLAAEYGAQGIRVNALLP 187
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 23-200 5.43e-10

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 58.49  E-value: 5.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVL---------ISRSKDKLDQVSSEIKEKFKvetrtIAV-DFASEDIYDKI-KTGLA 91
Cdd:cd05353    10 VTGAGGGLGRAYALAFAERGAKVVVndlggdrkgSGKSSSAADKVVDEIKAAGG-----KAVaNYDSVEDGEKIvKTAID 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  92 GL-EIGILVNNVG---------MSYEypeyfldvpDLDNVIKkminINILSVCKMTQLVLPGMVERSKGAILNISSGSGM 161
Cdd:cd05353    85 AFgRVDILVNNAGilrdrsfakMSEE---------DWDLVMR----VHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGL 151

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034574112 162 LPVPLLTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:cd05353   152 YGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAP 190
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
23-177 6.92e-10

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 58.11  E-value: 6.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKvetrTIAVDFASEDIYDKIKTGLAGL--EIGILVN 100
Cdd:PRK07067   11 LTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAI----AVSLDVTRQDSIDRIVAAAVERfgGIDILFN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMsyeypeyFLDVPDLD---NVIKKMININILSVCKMTQLVLPGMVERSKGA-ILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:PRK07067   87 NAAL-------FDMAPILDisrDSYDRLFAVNVKGLFFLMQAVARHMVEQGRGGkIINMASQAGRRGEALVSHYCATKAA 159


                  .
gi 1034574112 177 V 177
Cdd:PRK07067  160 V 160
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-200 8.25e-10

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 57.87  E-value: 8.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGST--DGIGKSYAEELAKHGMKVVLISRS-----------KDKLDQVSSEIkEKFKVETRTIAVDFASEDIY----DK 85
Cdd:PRK12859   11 VTGVSrlDGIGAAICKELAEAGADIFFTYWTaydkempwgvdQDEQIQLQEEL-LKNGVKVSSMELDLTQNDAPkellNK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  86 IKTGLAglEIGILVNNVGMSYEYPEYFLDVPDLDnvikKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVP 165
Cdd:PRK12859   90 VTEQLG--YPHILVNNAAYSTNNDFSNLTAEELD----KHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSGQFQGPMV 163

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034574112 166 LLTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK12859  164 GELAYAATKGAIDALTSSLAAEVAHLGITVNAINP 198
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 23-200 1.08e-09

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 57.58  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDF--ASEDIYDKIKTGLAGlEIGIL-- 98
Cdd:PRK08945   17 VTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIPLDLltATPQNYQQLADTIEE-QFGRLdg 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 -VNNVGMSYEY-PEYFLDVPDLDNVIKkminINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:PRK08945   96 vLHNAGLLGELgPMEQQDPEVWQDVMQ----VNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANWGAYAVSKFA 171

                         170       180
                  ....*....|....*....|....
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK08945  172 TEGMMQVLADEYQGTNLRVNCINP 195
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 23-205 1.13e-09

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 57.47  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDklDQVSSEIKEKFKVETRTIAVDF------ASEDIYDKIKTGLAGLEig 96
Cdd:cd05337     6 VTGASRGIGRAIATELAARGFDIAINDLPDD--DQATEVVAEVLAAGRRAIYFQAdigelsDHEALLDQAWEDFGRLD-- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSYEYPEYFLDV-PDldnVIKKMININILSVCKMTQLVLPGMVERSK------GAILNISSGSGMLPVPLLTI 169
Cdd:cd05337    82 CLVNNAGIAVRPRGDLLDLtED---SFDRLIAINLRGPFFLTQAVARRMVEQPDrfdgphRSIIFVTSINAYLVSPNRGE 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1034574112 170 YSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:cd05337   159 YCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHT 194
PRK06398 PRK06398
aldose dehydrogenase; Validated
 23-157 1.19e-09

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 57.53  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISrskdkldqvsseIKEKFKVETRTIAVDFASED-IYDKIK--TGLAGlEIGILV 99
Cdd:PRK06398   11 VTGGSQGIGKAVVNRLKEEGSNVINFD------------IKEPSYNDVDYFKVDVSNKEqVIKGIDyvISKYG-RIDILV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034574112 100 NNVGMSYEYPEYFLDVPDLDNVIkkmiNINILSVCKMTQLVLPGMVERSKGAILNISS 157
Cdd:PRK06398   78 NNAGIESYGAIHAVEEDEWDRII----NVNVNGIFLMSKYTIPYMLKQDKGVIINIAS 131
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 23-217 1.25e-09

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 57.47  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELA---KHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKIKTGLAGLEIGILV 99
Cdd:cd09806     5 ITGCSSGIGLHLAVRLAsdpSKRFKVYATMRDLKKKGRLWEAAGALAGGTLETLQLDVCDSKSVAAAVERVTERHVDVLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NNVGMSYEYPeyfLDVPDLDNViKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDF 179
Cdd:cd09806    85 CNAGVGLLGP---LEALSEDAM-ASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALEG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034574112 180 FSQCLHEEYRSKGVFVQSVLPYFVATKL--------AKIRKPTLDK 217
Cdd:cd09806   161 LCESLAVQLLPFNVHLSLIECGPVHTAFmekvlgspEEVLDRTADD 206
PRK07856 PRK07856
SDR family oxidoreductase;
23-208 1.31e-09

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 57.25  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSkdkldqvsseikEKFKVETRTiaVDFASEDIYD--KIKTGLAGLE-----I 95
Cdd:PRK07856   11 VTGGTRGIGAGIARAFLAAGATVVVCGRR------------APETVDGRP--AEFHAADVRDpdQVAALVDAIVerhgrL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 GILVNNVGMS-----YEYPEYFLDvpdldnvikKMININILSVCKMTQLVLPGMVER-SKGAILNISSGSGMLPVPLLTI 169
Cdd:PRK07856   77 DVLVNNAGGSpyalaAEASPRFHE---------KIVELNLLAPLLVAQAANAVMQQQpGGGSIVNIGSVSGRRPSPGTAA 147

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034574112 170 YSATKTFVDFFSQCLHEEYRSKgVFVQSVLPYFVATKLA 208
Cdd:PRK07856  148 YGAAKAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQS 185
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 23-174 1.44e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 57.32  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMK-VVLISRSKDKLDQVSSEIkEKFKVETRTIAVDFAS-EDIYDKIKTGLAGL-EIGILV 99
Cdd:PRK06198   11 VTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAEL-EALGAKAVFVQADLSDvEDCRRVVAAADEAFgRLDALV 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034574112 100 NNVGMSYEypEYFLDV-PDLdnvIKKMININILSVCKMTQLVLPGMVERS-KGAILNISSGSGMLPVPLLTIYSATK 174
Cdd:PRK06198   90 NAAGLTDR--GTILDTsPEL---FDRHFAVNVRAPFFLMQEAIKLMRRRKaEGTIVNIGSMSAHGGQPFLAAYCASK 161
PRK07074 PRK07074
SDR family oxidoreductase;
23-206 1.73e-09

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 57.09  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVetrTIAVDFASE-DIYDKIKTGLAGL-EIGILVN 100
Cdd:PRK07074    7 VTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARFV---PVACDLTDAaSLAAALANAAAERgPVDVLVA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSYEypeyfLDVPDLDNVIKKM---ININILSVCkmTQLVLPGMVERSKGAILNISSGSGM--LPVPlltIYSATKT 175
Cdd:PRK07074   84 NAGAARA-----ASLHDTTPASWRAdnaLNLEAAYLC--VEAVLEGMLKRSRGAVVNIGSVNGMaaLGHP---AYSAAKA 153

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034574112 176 FVDFFSQCLHEEYRSKGVFVQSVLPYFVATK 206
Cdd:PRK07074  154 GLIHYTKLLAVEYGRFGIRANAVAPGTVKTQ 184
PRK08703 PRK08703
SDR family oxidoreductase;
22-188 2.56e-09

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 56.48  E-value: 2.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDF--ASEDIYDKIKTGLAGLEIGILv 99
Cdd:PRK08703   10 LVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPEPFAIRFDLmsAEEKEFEQFAATIAEATQGKL- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 nnVGMSYEYPEYFLDVPDLDNVIKKMIN---INILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:PRK08703   89 --DGIVHCAGYFYALSPLDFQTVAEWVNqyrINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGGFGASKAA 166

                         170
                  ....*....|..
gi 1034574112 177 VDFFSQCLHEEY 188
Cdd:PRK08703  167 LNYLCKVAADEW 178
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
23-205 3.02e-09

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 56.42  E-value: 3.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVV--LISRSKDKLDQVSSEIKEKFKVETRTIAVDfASEDIYDKIKTGLAglEIGILVN 100
Cdd:PRK08993   15 VTGCDTGLGQGMALGLAEAGCDIVgiNIVEPTETIEQVTALGRRFLSLTADLRKID-GIPALLERAVAEFG--HIDILVN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGM-----SYEYPEyfldvPDLDNVIkkmiNINILSVCKMTQLVLPGMVERSKGA-ILNISSG---SGMLPVPlltIYS 171
Cdd:PRK08993   92 NAGLirredAIEFSE-----KDWDDVM----NLNIKSVFFMSQAAAKHFIAQGNGGkIINIASMlsfQGGIRVP---SYT 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034574112 172 ATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK08993  160 ASKSGVMGVTRLMANEWAKHNINVNAIAPGYMAT 193
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 23-200 3.24e-09

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


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 56.34  E-value: 3.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFkvETRTIAVDFASEDIYDKIKTGLAGLE--IGILVN 100
Cdd:cd08942    11 VTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYG--ECIAIPADLSSEEGIEALVARVAERSdrLDVLVN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSY-----EYPEYFLDvpdldnvikKMININILSVCKMTQLVLPgMVERSKGA-----ILNISSGSGMLpVPLLTIY 170
Cdd:cd08942    89 NAGATWgapleAFPESGWD---------KVMDINVKSVFFLTQALLP-LLRAAATAenparVINIGSIAGIV-VSGLENY 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 171 S--ATKTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:cd08942   158 SygASKAAVHQLTRKLAKELAGEHITVNAIAP 189
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 23-174 3.30e-09

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 56.14  E-value: 3.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSS-EIKEKFkvetrtIAVDFASE-DIYDKIKTGLAGL-EIGILV 99
Cdd:cd05371     7 VTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAKlGDNCRF------VPVDVTSEkDVKAALALAKAKFgRLDIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 100 NNVGMSYEYPEYFLD--VPDLDNVIKKMININILSVCKMTQLVLPGMVERS------KGAILNISSGSGMLPVPLLTIYS 171
Cdd:cd05371    81 NCAGIAVAAKTYNKKgqQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEpdqggeRGVIINTASVAAFEGQIGQAAYS 160


                  ...
gi 1034574112 172 ATK 174
Cdd:cd05371   161 ASK 163
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-210 3.76e-09

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 56.77  E-value: 3.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVL--ISRSKDKLDQVSSEIKekfkveTRTIAVDFASEDIYDKIKTGLA--GLEIGIL 98
Cdd:PRK08261  215 VTGAARGIGAAIAEVLARDGAHVVCldVPAAGEALAAVANRVG------GTALALDITAPDAPARIAEHLAerHGGLDIV 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYeypeyfldvpdlDNVIKKM--------ININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIY 170
Cdd:PRK08261  289 VHNAGITR------------DKTLANMdearwdsvLAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQTNY 356

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034574112 171 SATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKL-AKI 210
Cdd:PRK08261  357 AASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMtAAI 397
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 23-207 3.82e-09

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


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 56.00  E-value: 3.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKI--KTGLAGLEIGILVN 100
Cdd:cd08933    14 VTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKFVPCDVTKEEDIKTLisVTVERFGRIDCLVN 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGmsYEYPEYFLDVPDLDNvIKKMININILSVCKMTQLVLPGMvERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFF 180
Cdd:cd08933    94 NAG--WHPPHQTTDETSAQE-FRDLLNLNLISYFLASKYALPHL-RKSQGNIINLSSLVGSIGQKQAAPYVATKGAITAM 169

                         170       180
                  ....*....|....*....|....*..
gi 1034574112 181 SQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:cd08933   170 TKALAVDESRYGVRVNCISPGNIWTPL 196
PRK12746 PRK12746
SDR family oxidoreductase;
22-227 5.63e-09

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 55.43  E-value: 5.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVL-ISRSKDKLDQVSSEIK----EKFKVETRTIAVDFAS---EDIYDKIKTGLAGL 93
Cdd:PRK12746   10 LVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIEsnggKAFLIEADLNSIDGVKklvEQLKNELQIRVGTS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  94 EIGILVNNVGMSYEypeyfldvPDLDN----VIKKMININILSVCKMTQLVLPGMveRSKGAILNISSGSGMLPVPLLTI 169
Cdd:PRK12746   90 EIDILVNNAGIGTQ--------GTIENtteeIFDEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRLGFTGSIA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034574112 170 YSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATklaKIRKPTLDKPSPETFVKSA 227
Cdd:PRK12746  160 YGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKT---DINAKLLDDPEIRNFATNS 214
PRK05867 PRK05867
SDR family oxidoreductase;
22-209 7.47e-09

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 55.04  E-value: 7.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKekfKVETRTIAV--DFASED----IYDKIKTGLAGLEI 95
Cdd:PRK05867   13 LITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIG---TSGGKVVPVccDVSQHQqvtsMLDQVTAELGGIDI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 GilVNNVGMSYEYPeyFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSK-GAILNISSGSG-MLPVP-LLTIYSA 172
Cdd:PRK05867   90 A--VCNAGIITVTP--MLDMPLEE--FQRLQNTNVTGVFLTAQAAAKAMVKQGQgGVIINTASMSGhIINVPqQVSHYCA 163

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1034574112 173 TKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:PRK05867  164 SKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVE 200
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 23-207 1.08e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 55.04  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASE----DIYDKIKTGLAGLEIgiL 98
Cdd:PRK06701   51 ITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDANETKQRVEKEGVKCLLIPGDVSDEafckDAVEETVRELGRLDI--L 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGmsYEYP-EYFLDVPD--LDNVIKkminINILSVCKMTQLVLPGMveRSKGAILNISSGSGMLPVPLLTIYSATKT 175
Cdd:PRK06701  129 VNNAA--FQYPqQSLEDITAeqLDKTFK----TNIYSYFHMTKAALPHL--KQGSAIINTGSITGYEGNETLIDYSATKG 200

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 176 FVDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK06701  201 AIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPL 232
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 23-160 1.08e-08

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 54.63  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKfkveTRTIAVDFAS-EDIYDKIKTGLAGL-EIGILVN 100
Cdd:PRK08265   11 VTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGER----ARFIATDITDdAAIERAVATVVARFgRVDILVN 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034574112 101 NvGMSYeypeyfldvpdLDNVIK-------KMININILSVCKMTQLVLPGMVeRSKGAILNISSGSG 160
Cdd:PRK08265   87 L-ACTY-----------LDDGLAssradwlAALDVNLVSAAMLAQAAHPHLA-RGGGAIVNFTSISA 140
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
23-198 1.17e-08

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 54.34  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLI-SRSKDKLDQVSSEIkEKFKVETRTIAVDFASE----DIYDKIKTGLAGLEigI 97
Cdd:PRK08063    9 VTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEI-EALGRKALAVKANVGDVekikEMFAQIDEEFGRLD--V 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYPEYFLDVPDLDnvikKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:PRK08063   86 FVNNAASGVLRPAMELEESHWD----WTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYTTVGVSKAAL 161

                         170       180
                  ....*....|....*....|.
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSV 198
Cdd:PRK08063  162 EALTRYLAVELAPKGIAVNAV 182
PLN02253 PLN02253
xanthoxin dehydrogenase
 23-208 1.45e-08

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 54.44  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKV----------ETRTIAVDFASediyDKIKTglag 92
Cdd:PLN02253   23 VTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVcffhcdvtveDDVSRAVDFTV----DKFGT---- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  93 leIGILVNNVGMSYEypeyflDVPDLDNV----IKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLT 168
Cdd:PLN02253   95 --LDIMVNNAGLTGP------PCPDIRNVelseFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPH 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034574112 169 IYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLA 208
Cdd:PLN02253  167 AYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALA 206
PRK08340 PRK08340
SDR family oxidoreductase;
23-199 1.54e-08

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 54.43  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVEtrTIAVDFAS-EDIYDKIKTGLAGL-EIGILVN 100
Cdd:PRK08340    5 VTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYGEVY--AVKADLSDkDDLKNLVKEAWELLgGIDALVW 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSYEYPEYFLDVPDLDNVikKMININILSVCKMTQLVLPGMVERS-KGAILNISSGSGMLPVPLLTIYSATKTFVDF 179
Cdd:PRK08340   83 NAGNVRCEPCMLHEAGYSDWL--EAALLHLVAPGYLTTLLIQAWLEKKmKGVLVYLSSVSVKEPMPPLVLADVTRAGLVQ 160

                         170       180
                  ....*....|....*....|
gi 1034574112 180 FSQCLHEEYRSKGVFVQSVL 199
Cdd:PRK08340  161 LAKGVSRTYGGKGIRAYTVL 180
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 23-200 2.01e-08

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 53.62  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVL-ISRSKDKLDQVSSEIKEkfkvetRTIAVDFASEDiYDKIKTGLAGLE-----IG 96
Cdd:cd05349     5 VTGASRGLGAAIARSFAREGARVVVnYYRSTESAEAVAAEAGE------RAIAIQADVRD-RDQVQAMIEEAKnhfgpVD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSYEY-PEYFLDVPDLD-NVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATK 174
Cdd:cd05349    78 TIVNNALIDFPFdPDQRKTFDTIDwEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTAK 157

                         170       180
                  ....*....|....*....|....*.
gi 1034574112 175 TFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:cd05349   158 AALLGFTRNMAKELGPYGITVNMVSG 183
PRK12743 PRK12743
SDR family oxidoreductase;
23-205 2.68e-08

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 53.50  E-value: 2.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFA----SEDIYDKIKTGLAGleIGIL 98
Cdd:PRK12743    7 VTASDSGIGKACALLLAQQGFDIGITWHSDEEGAKETAEEVRSHGVRAEIRQLDLSdlpeGAQALDKLIQRLGR--IDVL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEYPeyFLDVpDLDNvIKKMININILSVCKMTQLVLPGMVERSKGA-ILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:PRK12743   85 VNNAGAMTKAP--FLDM-DFDE-WRKIFTVDVDGAFLCSQIAARHMVKQGQGGrIINITSVHEHTPLPGASAYTAAKHAL 160

                         170       180
                  ....*....|....*....|....*...
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK12743  161 GGLTKAMALELVEHGILVNAVAPGAIAT 188
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 23-205 1.00e-07

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 50.98  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGM-KVVLISRskdkldqvsseikekfkvetRTIAVDFASediydkikTGLAGLEIGilvnn 101
Cdd:cd02266     3 VTGGSGGIGGAIARWLASRGSpKVLVVSR--------------------RDVVVHNAA--------ILDDGRLID----- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 102 vgMSYEYPEYFLDvpdldnvikkminINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFFS 181
Cdd:cd02266    50 --LTGSRIERAIR-------------ANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114

                         170       180
                  ....*....|....*....|....
gi 1034574112 182 QCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:cd02266   115 QQWASEGWGNGLPATAVACGTWAG 138
PRK06139 PRK06139
SDR family oxidoreductase;
23-205 1.02e-07

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 52.03  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkfkVETRTIAV--DFASEDIYDKIKTGLAGL--EIGIL 98
Cdd:PRK06139   12 ITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRA---LGAEVLVVptDVTDADQVKALATQAASFggRIDVW 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSyeYPEYFLDVPdLDnVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVD 178
Cdd:PRK06139   89 VNNVGVG--AVGRFEETP-IE-AHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASKFGLR 164

                         170       180
                  ....*....|....*....|....*...
gi 1034574112 179 FFSQCLHEEYRSK-GVFVQSVLPYFVAT 205
Cdd:PRK06139  165 GFSEALRGELADHpDIHVCDVYPAFMDT 192
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 22-162 1.27e-07

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 51.12  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKdkldqvsseiKEKFKVETRTIAVDFAS--EDIYDKIKTglagleIGILV 99
Cdd:PRK06550    9 LITGAASGIGLAQARAFLAQGAQVYGVDKQD----------KPDLSGNFHFLQLDLSDdlEPLFDWVPS------VDILC 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034574112 100 NNVGMSYEYpEYFLDVPDLDnvIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGML 162
Cdd:PRK06550   73 NTAGILDDY-KPLLDTSLEE--WQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFV 132
PRK07985 PRK07985
SDR family oxidoreductase;
22-207 1.47e-07

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 51.53  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVL--ISRSKDKLDQVSSEIKEKFKvETRTIAVDFASE----DIYDKIKTGLAGLEI 95
Cdd:PRK07985   53 LVTGGDSGIGRAAAIAYAREGADVAIsyLPVEEEDAQDVKKIIEECGR-KAVLLPGDLSDEkfarSLVHEAHKALGGLDI 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 GILVnnVGMSYEYPeyflDVPDLDN-VIKKMININILSVCKMTQLVLPGMverSKGA-ILNISSGSGMLPVPLLTIYSAT 173
Cdd:PRK07985  132 MALV--AGKQVAIP----DIADLTSeQFQKTFAINVFALFWLTQEAIPLL---PKGAsIITTSSIQAYQPSPHLLDYAAT 202

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034574112 174 KTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK07985  203 KAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAL 236
PRK07024 PRK07024
SDR family oxidoreductase;
22-258 1.69e-07

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 51.08  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVET-----------RTIAVDFASEdiydkiktgl 90
Cdd:PRK07024    6 FITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAARVSVyaadvrdadalAAAAADFIAA---------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  91 AGLeIGILVNNVGMSY----EYPEyfldvpDLDnVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPL 166
Cdd:PRK07024   76 HGL-PDVVIANAGISVgtltEERE------DLA-VFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 167 LTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKI---RKPTLdkPSPETFVKSAIKTVGLQSRtngYLI- 242
Cdd:PRK07024  148 AGAYSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPMTAHnpyPMPFL--MDADRFAARAARAIARGRR---FRVi 222

                         250
                  ....*....|....*....
gi 1034574112 243 ---HALMGSIISNLPSWIY 258
Cdd:PRK07024  223 pwqMGVVAKLLRVLPRWLY 241
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
23-205 1.81e-07

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 51.06  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRskdkldQVSSEIKEKFKVETR---TIAVDFASEDIYDKI---KTGLAGlEIG 96
Cdd:PRK12481   13 ITGCNTGLGQGMAIGLAKAGADIVGVGV------AEAPETQAQVEALGRkfhFITADLIQQKDIDSIvsqAVEVMG-HID 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSYEYPEYFLDVPDLDNVikkmININILSVCKMTQLVLPGMVER-SKGAILNISSG---SGMLPVPlltIYSA 172
Cdd:PRK12481   86 ILINNAGIIRRQDLLEFGNKDWDDV----ININQKTVFFLSQAVAKQFVKQgNGGKIINIASMlsfQGGIRVP---SYTA 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034574112 173 TKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK12481  159 SKSAVMGLTRALATELSQYNINVNAIAPGYMAT 191
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 22-200 2.86e-07

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 50.16  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDqvssEIKEKFKVETRTIAVDFASEDIYDKIKTGLAGLEIgiLVNN 101
Cdd:cd05331     2 IVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLL----EYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDA--LVNC 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 102 VGMSYEYPEYFLDVPDLDNVIkkmiNINILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFFS 181
Cdd:cd05331    76 AGVLRPGATDPLSTEDWEQTF----AVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLS 151

                         170
                  ....*....|....*....
gi 1034574112 182 QCLHEEYRSKGVFVQSVLP 200
Cdd:cd05331   152 KCLGLELAPYGVRCNVVSP 170
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 23-209 4.05e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 50.11  E-value: 4.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFkvetrtIAVDFASED----IYDKIKTGLAGLEIGIl 98
Cdd:PRK06057   12 ITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGLF------VPTDVTDEDavnaLFDTAAETYGSVDIAF- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 vNNVGMSyeypeyfldvPDLDNVI--------KKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTI- 169
Cdd:PRK06057   85 -NNAGIS----------PPEDDSIlntgldawQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSQIs 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034574112 170 YSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK 209
Cdd:PRK06057  154 YTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQ 193
PRK06128 PRK06128
SDR family oxidoreductase;
23-235 4.70e-07

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 50.24  E-value: 4.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDqvSSEIKEKFKVETR-TIAV--DFASE----DIYDKIKTGLAGLEI 95
Cdd:PRK06128   60 ITGADSGIGRATAIAFAREGADIALNYLPEEEQD--AAEVVQLIQAEGRkAVALpgDLKDEafcrQLVERAVKELGGLDI 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 giLVNNVGMSyEYPEYFLDVP--DLDNVIKKminiNILSVCKMTQLVLPGMverSKGA-ILNISSGSGMLPVPLLTIYSA 172
Cdd:PRK06128  138 --LVNIAGKQ-TAVKDIADITteQFDATFKT----NVYAMFWLCKAAIPHL---PPGAsIINTGSIQSYQPSPTLLDYAS 207

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034574112 173 TKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLakirKPTLDKPsPETfvksaIKTVGLQS 235
Cdd:PRK06128  208 TKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPL----QPSGGQP-PEK-----IPDFGSET 260
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 23-155 6.26e-07

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 49.29  E-value: 6.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIkEKFKVETRTIAVDFAS-EDIYDKIKTGLAGL-EIGILVN 100
Cdd:PRK07677    6 ITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEI-EQFPGQVLTVQMDVRNpEDVQKMVEQIDEKFgRIDALIN 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034574112 101 NVGMSYEYPEYFLDVpdldNVIKKMININILSVCKMTQLVLPGMVERS-KGAILNI 155
Cdd:PRK07677   85 NAAGNFICPAEDLSV----NGWNSVIDIVLNGTFYCSQAVGKYWIEKGiKGNIINM 136
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 22-205 6.88e-07

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 49.19  E-value: 6.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDklDQVSSEIKEKFKVETRTIAVDF------ASEDIYDKIKTGLAGLEi 95
Cdd:PRK12745    6 LVTGGRRGIGLGIARALAAAGFDLAINDRPDD--EELAATQQELRALGVEVIFFPAdvadlsAHEAMLDAAQAAWGRID- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 gILVNNVGMSYEYPEYFLDV-PD-LDNVikkmININILSVCKMTQLVLPGMVERSK------GAILNISSGSGMLPVPLL 167
Cdd:PRK12745   83 -CLVNNAGVGVKVRGDLLDLtPEsFDRV----LAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVSSVNAIMVSPNR 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034574112 168 TIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:PRK12745  158 GEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKT 195
PRK06482 PRK06482
SDR family oxidoreductase;
22-174 9.51e-07

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 48.96  E-value: 9.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKiktGLAGLE-IGILVN 100
Cdd:PRK06482    6 FITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDRLWVLQLDVTDSAAVRAVVDR---AFAALGrIDVVVS 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034574112 101 NVGMSYEYPEYFLDvpdlDNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATK 174
Cdd:PRK06482   83 NAGYGLFGAAEELS----DAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATK 152
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 23-205 1.02e-06

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 48.77  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkfkvETRTIAVDFASEDIYDKIKTGLAGL--EIGILVN 100
Cdd:cd05363     8 ITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGP----AACAISLDVTDQASIDRCVAALVDRwgSIDILVN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMsyeypeyFLDVPDLD---NVIKKMININILSVCKMTQLVLPGMVERSKGA-ILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:cd05363    84 NAAL-------FDLAPIVDitrESYDRLFAINVSGTLFMMQAVARAMIAQGRGGkIINMASQAGRRGEALVGVYCATKAA 156

                         170       180
                  ....*....|....*....|....*....
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVAT 205
Cdd:cd05363   157 VISLTQSAGLNLIRHGINVNAIAPGVVDG 185
PRK08628 PRK08628
SDR family oxidoreductase;
23-157 1.79e-06

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 48.03  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKlDQVSSEIKEKfKVETRTIAVDFASED-IYDKIKTGLAGL-EIGILVN 100
Cdd:PRK08628   12 VTGGASGIGAAISLRLAEEGAIPVIFGRSAPD-DEFAEELRAL-QPRAEFVQVDLTDDAqCRDAVEQTVAKFgRIDGLVN 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSyeypeyflDVPDLDNVIKKMI---NINILSVCKMTQLVLPGMvERSKGAILNISS 157
Cdd:PRK08628   90 NAGVN--------DGVGLEAGREAFVaslERNLIHYYVMAHYCLPHL-KASRGAIVNISS 140
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 22-184 3.04e-06

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 47.19  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQvsseikEKFKVETRTIAVDFASEDIYDKIKTGLAGLEIgiLVNN 101
Cdd:PRK08220   12 WVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQED------YPFATFVLDVSDAAAVAQVCQRLLAETGPLDV--LVNA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 102 VGMsyeypeyfLDVPDLDNV----IKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFV 177
Cdd:PRK08220   84 AGI--------LRMGATDSLsdedWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAAL 155


                  ....*..
gi 1034574112 178 DFFSQCL 184
Cdd:PRK08220  156 TSLAKCV 162
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-157 3.53e-06

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 47.01  E-value: 3.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVL-ISRSKDKLDQVSSEIKEkfkvetRTIAV-----DFasEDIYDKIKTGLA--GLE 94
Cdd:PRK08642   10 VTGGSRGLGAAIARAFAREGARVVVnYHQSEDAAEALADELGD------RAIALqadvtDR--EQVQAMFATATEhfGKP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034574112  95 IGILVNNVGMSYEY-PEYFLDVPDL---------DNVIKKMINInilsvckmTQLVLPGMVERSKGAILNISS 157
Cdd:PRK08642   82 ITTVVNNALADFSFdGDARKKADDItwedfqqqlEGSVKGALNT--------IQAALPGMREQGFGRIINIGT 146
PRK05993 PRK05993
SDR family oxidoreductase;
22-212 4.42e-06

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 46.94  E-value: 4.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKV-----ETRTIAVDFASEdiydkiktgLAGLEIG 96
Cdd:PRK05993    8 LITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEAEGLEAFQLdyaepESIAALVAQVLE---------LSGGRLD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNvGmSYEYPEYFLDVPDldNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:PRK05993   79 ALFNN-G-AYGQPGAVEDLPT--EALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNASKFA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLP-----YFVATKLAKIRK 212
Cdd:PRK05993  155 IEGLSLTLRMELQGSGIHVSLIEPgpietRFRANALAAFKR 195
PRK06947 PRK06947
SDR family oxidoreductase;
23-207 6.10e-06

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 46.34  E-value: 6.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKV-VLISRSKDKLDQVSSEIKEKfKVETRTIAVDFASED----IYDKIKTGLAGLEigI 97
Cdd:PRK06947    7 ITGASRGIGRATAVLAAARGWSVgINYARDAAAAEETADAVRAA-GGRACVVAGDVANEAdviaMFDAVQSAFGRLD--A 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSYEYpeyfLDVPDLD-NVIKKMININILSvckmTQLVLPGMVER-------SKGAILNISSGSGMLPVPLLTI 169
Cdd:PRK06947   84 LVNNAGIVAPS----MPLADMDaARLRRMFDTNVLG----AYLCAREAARRlstdrggRGGAIVNVSSIASRLGSPNEYV 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034574112 170 -YSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK06947  156 dYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 23-174 8.06e-06

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 45.73  E-value: 8.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVL-ISRSKDKLDQVSSEIkEKFKVETRTIAVDF----ASEDIYDKIKTGLAGLEigI 97
Cdd:cd05357     5 VTGAAKRIGRAIAEALAAEGYRVVVhYNRSEAEAQRLKDEL-NALRNSAVLVQADLsdfaACADLVAAAFRAFGRCD--V 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034574112  98 LVNNVgmSYEYPEYFLDVPdlDNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATK 174
Cdd:cd05357    82 LVNNA--SAFYPTPLGQGS--EDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSK 154
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 20-207 8.65e-06

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 46.10  E-value: 8.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  20 APFVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIK-EKFKVETRTIAVDFASE--DIYDKIKTGLAGLEig 96
Cdd:PRK05876    8 GAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRaEGFDVHGVMCDVRHREEvtHLADEAFRLLGHVD-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  97 ILVNNVGMSYEYPEYFLDVPDLdnviKKMININILSVCKMTQLVLPGMVERSKGA-ILNISSGSGMLPVPLLTIYSATKT 175
Cdd:PRK05876   86 VVFSNAGIVVGGPIVEMTHDDW----RWVIDVDLWGSIHTVEAFLPRLLEQGTGGhVVFTASFAGLVPNAGLGAYGVAKY 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 176 FVDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK05876  162 GVVGLAETLAREVTADGIGVSVLCPMVVETNL 193
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 22-208 9.41e-06

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 45.87  E-value: 9.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLIS----RSKDKLDQVSSEIKEKfkvETRTIAVDFASEDiYDKIKTGLAGL--EI 95
Cdd:PRK12827   10 LITGGSGGLGRAIAVRLAADGADVIVLDihpmRGRAEADAVAAGIEAA---GGKALGLAFDVRD-FAATRAALDAGveEF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  96 G---ILVNNVGMSYEYPEYFLDVPDLDNVikkmININILSVCKMTQLVLPGMVE-RSKGAILNISSGSGMLPVPLLTIYS 171
Cdd:PRK12827   86 GrldILVNNAGIATDAAFAELSIEEWDDV----IDVNLDGFFNVTQAALPPMIRaRRGGRIVNIASVAGVRGNRGQVNYA 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1034574112 172 ATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLA 208
Cdd:PRK12827  162 ASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMA 198
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 22-243 9.43e-06

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 45.95  E-value: 9.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEkfkVETRTIAvDFASEDIYDKIKTGLAGL-EIGILVN 100
Cdd:cd08951    11 FITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPG---AAGVLIG-DLSSLAETRKLADQVNAIgRFDAVIH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMsyeYPEYFLDVPDLDnvIKKMININILSvckmtQLVLPGMVERSKGAILnISSG---------SGML----PVPLL 167
Cdd:cd08951    87 NAGI---LSGPNRKTPDTG--IPAMVAVNVLA-----PYVLTALIRRPKRLIY-LSSGmhrggnaslDDIDwfnrGENDS 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034574112 168 TIYSATKTFVDFFSQCLheEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPSPETFVKSAIKTVGLQSRTNGYLIH 243
Cdd:cd08951   156 PAYSDSKLHVLTLAAAV--ARRWKDVSSNAVHPGWVPTKMGGAGAPDDLEQGHLTQVWLAESDDPQALTSGGYFYH 229
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 23-200 9.85e-06

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 45.80  E-value: 9.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKF-KVETRTIAVDFASE-----------DIYDKIKtgl 90
Cdd:PRK12384    7 VIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYgEGMAYGFGADATSEqsvlalsrgvdEIFGRVD--- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  91 agleigILVNNVGMSYEYPEYFLDVPDLDNVIKkmININILSVC-KMTQLVlpgMVERS-KGAILNISSGSGMLPVPLLT 168
Cdd:PRK12384   84 ------LLVYNAGIAKAAFITDFQLGDFDRSLQ--VNLVGYFLCaREFSRL---MIRDGiQGRIIQINSKSGKVGSKHNS 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034574112 169 IYSATKTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK12384  153 GYSAAKFGGVGLTQSLALDLAEYGITVHSLML 184
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-228 1.71e-05

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 45.14  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVetRTIAVDFAS----EDIYDKIKTGLAGLEigIL 98
Cdd:PRK05786   10 IIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYGNI--HYVVGDVSStesaRNVIEKAAKVLNAID--GL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  99 VNNVGMSYEYPeyFLDVPDLDNVIKKMININILSVckmtQLVLPGMVERSkgAILNISSGSGML-PVPLLTIYSATKTFV 177
Cdd:PRK05786   86 VVTVGGYVEDT--VEEFSGLEEMLTNHIKIPLYAV----NASLRFLKEGS--SIVLVSSMSGIYkASPDQLSYAVAKAGL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034574112 178 DFFSQCLHEEYRSKGVFVQSVLPYFVATKL------AKIRKPTLDKPSPETFVKSAI 228
Cdd:PRK05786  158 AKAVEILASELLGRGIRVNGIAPTTISGDFepernwKKLRKLGDDMAPPEDFAKVII 214
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 23-160 1.72e-05

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 45.18  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLIsrskdkldqvssEIKEKF-KVETRTIA-VDFASEDIYDKIKTGLAGleigiLVN 100
Cdd:cd05328     4 ITGAASGIGAATAELLEDAGHTVIGI------------DLREADvIADLSTPEgRAAAIADVLARCSGVLDG-----LVN 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSYEYPeyfldvpdLDNVIKkminINILSVCKMTQLVLPGMVERSKGAILNISSGSG 160
Cdd:cd05328    67 CAGVGGTTV--------AGLVLK----VNYFGLRALMEALLPRLRKGHGPAAVVVSSIAG 114
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 22-200 2.59e-05

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 44.36  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKD---KLD----QVSSEIkEKFKVETRTIAVDFASED-IYDKIKTGLAGL 93
Cdd:cd09762     7 FITGASRGIGKAIALKAARDGANVVIAAKTAEphpKLPgtiyTAAEEI-EAAGGKALPCIVDIRDEDqVRAAVEKAVEKF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  94 -EIGILVNNVgmSYEYPEYFLDVP----DLdnvikkMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLL- 167
Cdd:cd09762    86 gGIDILVNNA--SAISLTGTLDTPmkryDL------MMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLNPKWFKn 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034574112 168 -TIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:cd09762   158 hTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PRK06123 PRK06123
SDR family oxidoreductase;
23-207 2.66e-05

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 44.38  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVL-ISRSKDKLDQVSSEIKEKfKVETRTIAVDFASED----IYDKIKTGLAGLEigI 97
Cdd:PRK06123    7 ITGASRGIGAATALLAAERGYAVCLnYLRNRDAAEAVVQAIRRQ-GGEALAVAADVADEAdvlrLFEAVDRELGRLD--A 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMSyeypEYFLDVPDLDNV-IKKMININILSVCKMTQLVLPGMVER---SKGAILNISSGSGMLPVPLLTI-YSA 172
Cdd:PRK06123   84 LVNNAGIL----EAQMRLEQMDAArLTRIFATNVVGSFLCAREAVKRMSTRhggRGGAIVNVSSMAARLGSPGEYIdYAA 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034574112 173 TKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK06123  160 SKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEI 194
PRK12742 PRK12742
SDR family oxidoreductase;
23-200 2.79e-05

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 44.36  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLI-SRSKDKldqvsseiKEKFKVETRTIAVDFASEDIYDKIKTGLAGLEIGILVNN 101
Cdd:PRK12742   11 VLGGSRGIGAAIVRRFVTDGANVRFTyAGSKDA--------AERLAQETGATAVQTDSADRDAVIDVVRKSGALDILVVN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 102 VGMSYeypeyFLDVPDLD-NVIKKMININILSvckmtqlvlP--GMVERSK-----GAILNISSGSG-MLPVPLLTIYSA 172
Cdd:PRK12742   83 AGIAV-----FGDALELDaDDIDRLFKINIHA---------PyhASVEAARqmpegGRIIIIGSVNGdRMPVAGMAAYAA 148

                         170       180
                  ....*....|....*....|....*...
gi 1034574112 173 TKTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK12742  149 SKSALQGMARGLARDFGPRGITINVVQP 176
PRK07041 PRK07041
SDR family oxidoreductase;
23-81 3.42e-05

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 43.87  E-value: 3.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVetRTIAVDFASED 81
Cdd:PRK07041    2 VVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGAPV--RTAALDITDEA 58
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 23-162 3.97e-05

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 44.12  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEI-KEKFKVETRTIAVDFA-SEDIYDKIKT-GLAGLEIGILV 99
Cdd:cd09808     6 ITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIeTESGNQNIFLHIVDMSdPKQVWEFVEEfKEEGKKLHVLI 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034574112 100 NNVGMSYEYPEYFLDvpdldnVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGsGML 162
Cdd:cd09808    86 NNAGCMVNKRELTED------GLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSSG-GML 141
PRK09730 PRK09730
SDR family oxidoreductase;
23-207 4.50e-05

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 43.69  E-value: 4.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVL-----ISRSKDKLDQVSSEIKEKFKV------ETRTIAVdFASEDIYDKiktgla 91
Cdd:PRK09730    6 VTGGSRGIGRATALLLAQEGYTVAVnyqqnLHAAQEVVNLITQAGGKAFVLqadisdENQVVAM-FTAIDQHDE------ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  92 glEIGILVNNVGMSYEYPEyfldvpdLDNV----IKKMININILSVCKMTQLVLPGMVER---SKGAILNISSGSGMLPV 164
Cdd:PRK09730   79 --PLAALVNNAGILFTQCT-------VENLtaerINRVLSTNVTGYFLCCREAVKRMALKhggSGGAIVNVSSAASRLGA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034574112 165 PLLTI-YSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK09730  150 PGEYVdYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEM 193
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 23-94 5.28e-05

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


Pssm-ID: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 43.15  E-value: 5.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETR---TIAVDFASEDIYDK---IKTGLAGLE 94
Cdd:cd01078    33 VLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAADSLRARFGEGVGaveTSDDAARAAAIKGAdvvFAAGAAGVE 110
PRK08017 PRK08017
SDR family oxidoreductase;
22-218 5.61e-05

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 43.54  E-value: 5.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIA-VDFASEDIYDKIKTGLAGLeigilVN 100
Cdd:PRK08017    6 LITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARMNSLGFTGILLDLDDPEsVERAADEVIALTDNRLYGL-----FN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 NVGMSYEYPeyfldvpdLDNV----IKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTF 176
Cdd:PRK08017   81 NAGFGVYGP--------LSTIsrqqMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYA 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAK-IRKPTLDKP 218
Cdd:PRK08017  153 LEAWSDALRMELRHSGIKVSLIEPGPIRTRFTDnVNQTQSDKP 195
PRK06500 PRK06500
SDR family oxidoreductase;
23-207 6.11e-05

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 43.41  E-value: 6.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVeTRTIAVDFASE-DIYDKIKTglAGLEIGILVNN 101
Cdd:PRK06500   11 ITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALV-IRADAGDVAAQkALAQALAE--AFGRLDAVFIN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 102 VGMSyeypeYFLDVPDLDNVI-KKMININILSVCKMTQLVLPGMverSKGA--ILN--ISSGSGMlpvPLLTIYSATKTF 176
Cdd:PRK06500   88 AGVA-----KFAPLEDWDEAMfDRSFNTNVKGPYFLIQALLPLL---ANPAsiVLNgsINAHIGM---PNSSVYAASKAA 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034574112 177 VDFFSQCLHEEYRSKGVFVQSVLPYFVATKL 207
Cdd:PRK06500  157 LLSLAKTLSGELLPRGIRVNAVSPGPVQTPL 187
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-200 8.24e-05

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 43.14  E-value: 8.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGST--DGIGKSYAEELAKHGMKVVLISRSKDKLDQ-----------VSSEIKEK-FKVETRTI--AVDFASEDIYDKI 86
Cdd:PRK12748   10 VTGASrlNGIGAAVCRRLAAKGIDIFFTYWSPYDKTMpwgmhdkepvlLKEEIESYgVRCEHMEIdlSQPYAPNRVFYAV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  87 KTGLAGLEIgiLVNNVGMSYEYPEYFLDVPDLDnvikKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPL 166
Cdd:PRK12748   90 SERLGDPSI--LINNAAYSTHTRLEELTAEQLD----KHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTSGQSLGPMPD 163

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034574112 167 LTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK12748  164 ELAYAATKGAIEAFTKSLAPELAEKGITVNAVNP 197
PRK08278 PRK08278
SDR family oxidoreductase;
22-200 1.21e-04

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 42.58  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKD---KLD----QVSSEIKEKfKVETRTIAVDFASED-IYDKIKTGLAGL 93
Cdd:PRK08278   10 FITGASRGIGLAIALRAARDGANIVIAAKTAEphpKLPgtihTAAEEIEAA-GGQALPLVGDVRDEDqVAAAVAKAVERF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  94 -EIGILVNNVGMSYEYPeyFLDVP----DLdnvikkMININILSVCKMTQLVLPGMVERSKGAILNISSgsgmlPVPL-- 166
Cdd:PRK08278   89 gGIDICVNNASAINLTG--TEDTPmkrfDL------MQQINVRGTFLVSQACLPHLKKSENPHILTLSP-----PLNLdp 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034574112 167 -----LTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:PRK08278  156 kwfapHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 22-103 1.22e-04

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 43.37  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFkVETRTIAVDFASEDI-YDKIKTGLAGLEIGILVN 100
Cdd:COG3347   429 LVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGY-GADAVDATDVDVTAEaAVAAAFGFAGLDIGGSDI 507


                  ...
gi 1034574112 101 NVG 103
Cdd:COG3347   508 GVA 510
PRK05854 PRK05854
SDR family oxidoreductase;
23-103 2.16e-04

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 41.98  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKF---KVETRtiAVDFAS----EDIYDKIKTglAGLEI 95
Cdd:PRK05854   19 VTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTAVpdaKLSLR--ALDLSSlasvAALGEQLRA--EGRPI 94


                  ....*...
gi 1034574112  96 GILVNNVG 103
Cdd:PRK05854   95 HLLINNAG 102
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 23-106 3.17e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 41.55  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFK-VETRTIAVDFASediYDKIKTGLAGLE-----IG 96
Cdd:PRK06197   21 VTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAATPgADVTLQELDLTS---LASVRAAADALRaayprID 97

                          90
                  ....*....|
gi 1034574112  97 ILVNNVGMSY 106
Cdd:PRK06197   98 LLINNAGVMY 107
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 23-104 9.99e-04

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 39.76  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIkekfKVETRTIAV-----DFASED-IYDKIKTGLAGLE-I 95
Cdd:cd09807     6 ITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEI----RRDTLNHEVivrhlDLASLKsIRAFAAEFLAEEDrL 81


                  ....*....
gi 1034574112  96 GILVNNVGM 104
Cdd:cd09807    82 DVLINNAGV 90
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 23-174 1.38e-03

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


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 39.37  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASE-----------DIYDKIKTgla 91
Cdd:cd05322     7 VIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYGFGADATNEqsvialskgvdEIFKRVDL--- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  92 gleigiLVNNVGMSYEYPEYFLDVPDLDNVIKkmININILSVC--KMTQLvlpgMVER-SKGAILNISSGSGMLPVPLLT 168
Cdd:cd05322    84 ------LVYSAGIAKSAKITDFELGDFDRSLQ--VNLVGYFLCarEFSKL----MIRDgIQGRIIQINSKSGKVGSKHNS 151


                  ....*.
gi 1034574112 169 IYSATK 174
Cdd:cd05322   152 GYSAAK 157
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
 23-145 1.98e-03

atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187540 [Multi-domain]  Cd Length: 302  Bit Score: 38.85  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSeikekfkvetrtiaVDFASEDIYDKIKTGLAGLEIGILVNNV 102
Cdd:cd05229     4 VLGASGPIGREVARELRRRGWDVRLVSRSGSKLAWLPG--------------VEIVAADAMDASSVIAAARGADVIYHCA 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1034574112 103 GMSY-EYPEYFLdvPDLDNVIKkmininilsVCKMT--QLVLPGMV 145
Cdd:cd05229    70 NPAYtRWEELFP--PLMENVVA---------AAEANgaKLVLPGNV 104
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 22-195 2.16e-03

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 38.82  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSkdkldqvSSEIKEKFKVETRTIAVDFASEDIYDKIktgLAGLEIGILVN- 100
Cdd:pfam01370   2 LVTGATGFIGSHLVRRLLEKGYEVIGLDRL-------TSASNTARLADLRFVEGDLTDRDALEKL---LADVRPDAVIHl 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112 101 ----NVGMSYEYPEYFLDVpdldNVikkMININILSVCK---MTQLVLPGMVER-SKGAILNISSGSGMLPVPLLTIYSA 172
Cdd:pfam01370  72 aavgGVGASIEDPEDFIEA----NV---LGTLNLLEAARkagVKRFLFASSSEVyGDGAEIPQEETTLTGPLAPNSPYAA 144

                         170       180
                  ....*....|....*....|...
gi 1034574112 173 TKTFVDFFSQCLHEEYRSKGVFV 195
Cdd:pfam01370 145 AKLAGEWLVLAYAAAYGLRAVIL 167
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 23-200 2.34e-03

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 38.73  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKF-KVETRTIAVDFAS----EDIYDKIKTglAGLEIGI 97
Cdd:cd09809     6 ITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEEWhKARVEAMTLDLASlrsvQRFAEAFKA--KNSPLHV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  98 LVNNVGMsYEYPeYFLDVPDLDNVIKkminINILSVCKMTQLVLPGMVERSKGAILNISSGS----------GMLPVPLL 167
Cdd:cd09809    84 LVCNAAV-FALP-WTLTEDGLETTFQ----VNHLGHFYLVQLLEDVLRRSAPARVIVVSSEShrftdlpdscGNLDFSLL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034574112 168 T----------IYSATKTFVDFFSQCLHEEYRSKGVFVQSVLP 200
Cdd:cd09809   158 SppkkkywsmlAYNRAKLCNILFSNELHRRLSPRGITSNSLHP 200
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 23-174 2.61e-03

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


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 38.33  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLIsrskDKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKIKTGLAGL--EIGILVN 100
Cdd:cd09761     6 VTGGGHGIGKQICLDFLEAGDKVVFA----DIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKlgRIDVLVN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034574112 101 NVGMSYEYPEYFLDVPDLDNVIKkminINILSVCKMTQLVLPGMVeRSKGAILNISSGSGMLPVPLLTIYSATK 174
Cdd:cd09761    82 NAARGSKGILSSLLLEEWDRILS----VNLTGPYELSRYCRDELI-KNKGRIINIASTRAFQSEPDSEAYAASK 150
PRK08416 PRK08416
enoyl-ACP reductase;
22-83 2.84e-03

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 38.21  E-value: 2.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKL-DQVSSEIKEKFKVETRTIAVDFASEDIY 83
Cdd:PRK08416   12 VISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVEEaNKIAEDLEQKYGIKAKAYPLNILEPETY 74
COG3268 COG3268
Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];
35-76 3.55e-03

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


Pssm-ID: 442499 [Multi-domain]  Cd Length: 368  Bit Score: 38.29  E-value: 3.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034574112  35 AEELAKHGMKVVLISRSKDKLDQVSSEIKEKfKVETRTIAVD 76
Cdd:COG3268    22 AEYLARRGLRPALAGRNAAKLEAVAAELGAA-DLPLRVADLD 62
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 23-51 4.43e-03

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 37.08  E-value: 4.43e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034574112   23 VTGSTDGIGKSYAEELAKHGM-KVVLISRS 51
Cdd:smart00822   5 ITGGLGGLGRALARWLAERGArRLVLLSRS 34
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 23-81 7.14e-03

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 36.77  E-value: 7.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMK-VVLISRSKDKLDQVSSEIKE--KFKVETRTIAVDFASED 81
Cdd:pfam08659   5 ITGGLGGLGRELARWLAERGARhLVLLSRSAAPRPDAQALIAEleARGVEVVVVACDVSDPD 66
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 23-63 7.20e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 37.09  E-value: 7.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1034574112  23 VTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIK 63
Cdd:PRK05875   12 VTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIE 52
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
 22-56 7.78e-03

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 37.35  E-value: 7.78e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLD 56
Cdd:cd05263     2 FVTGGTGFLGRHLVKRLLENGFKVLVLVRSESLGE 36
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
 22-82 9.04e-03

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 36.83  E-value: 9.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMK-VVLISRSKDKLDQVSSEIKEKFK-VETRTIAVDFASEDI 82
Cdd:cd05237     6 LVTGGAGSIGSELVRQILKFGPKkLIVFDRDENKLHELVRELRSRFPhDKLRFIIGDVRDKER 68
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
 22-85 9.35e-03

aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 36.86  E-value: 9.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKF---KVETrTIAVDFASEDIYDK 85
Cdd:cd05227     3 LVTGATGFIASHIVEQLLKAGYKVRGTVRSLSKSAKLKALLKAAGyndRLEF-VIVDDLTAPNAWDE 68
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 22-174 9.94e-03

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 36.86  E-value: 9.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034574112  22 FVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVetrtIAVDFASEDIYDK-IKTGLAGL-EIGILV 99
Cdd:PRK06200   10 LITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLV----VEGDVTSYADNQRaVDQTVDAFgKLDCFV 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034574112 100 NNVGMsYEYPEYFLDVPD--LDNVIKKMININILSVCKMTQLVLPGMVErSKGAILNISSGSGMLPVPLLTIYSATK 174
Cdd:PRK06200   86 GNAGI-WDYNTSLVDIPAetLDTAFDEIFNVNVKGYLLGAKAALPALKA-SGGSMIFTLSNSSFYPGGGGPLYTASK 160
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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