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Conserved domains on  [gi|157836251|pdb|2QQ5|A]
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Chain A, Dehydrogenase/reductase SDR family member 1

Protein Classification

dehydrogenase/reductase SDR family member 1( domain architecture ID 10176799)

dehydrogenase/reductase SDR family member 1 (DHRS1) is an uncharacterized enzyme from the short-chain dehydrogenases/reductases (SDR) family of NAD(P)(H)-dependent oxidoreductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 3-260 5.71e-164

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: 454.60  E-value: 5.71e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQ 81
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTiLPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       82 GRLDVLVNNAYAGVQTILNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNVPY 161
Cdd:cd09763  81 GRLDILVNNAYAAVQLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVAY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVlqdPVLKQFKSAFSSAETTELSGKCVVALATDP 241
Cdd:cd09763 161 GVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEG---SWHAKERDAFLNGETTEYSGRCVVALAADP 237

                       250
                ....*....|....*....
2QQ5_A      242 NILSLSGKVLPSCDLARRY 260
Cdd:cd09763 238 DLMELSGRVLITGELAREY 256
 
Name Accession Description Interval E-value
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 3-260 5.71e-164

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: 454.60  E-value: 5.71e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQ 81
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTiLPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       82 GRLDVLVNNAYAGVQTILNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNVPY 161
Cdd:cd09763  81 GRLDILVNNAYAAVQLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVAY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVlqdPVLKQFKSAFSSAETTELSGKCVVALATDP 241
Cdd:cd09763 161 GVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEG---SWHAKERDAFLNGETTEYSGRCVVALAADP 237

                       250
                ....*....|....*....
2QQ5_A      242 NILSLSGKVLPSCDLARRY 260
Cdd:cd09763 238 DLMELSGRVLITGELAREY 256
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-210 4.57e-57

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: 182.68  E-value: 4.57e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        1 APMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQ 80
Cdd:COG1028   2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAA-VAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       81 QGRLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQ-YMFNV 159
Cdd:COG1028  81 FGRLDILVNN--AGI-----TPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRgSPGQA 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
2QQ5_A      160 PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVLQ 210
Cdd:COG1028 154 AYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVRE 204
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 1-260 5.22e-50

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 166.33  E-value: 5.22e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         1 APMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHL----------DTLRVVAQEAQSLGGQCVPVVCDSSQESEVR 70
Cdd:PRK08303   4 KPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTrarrseydrpETIEETAELVTAAGGRGIAVQVDHLVPEQVR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        71 SLFEQVDREqQGRLDVLVNNAYAGvqTILNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSp 150
Cdd:PRK08303  84 ALVERIDRE-QGRLDILVNDIWGG--EKLFEWGKPVWEHSLDKGLRMLRLAIDTHLITSHFALPLLIRRPGGLVVEITD- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       151 GSLQ-----YMFNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMA-KEEVLQDPVLKQfkSAFSSA 224
Cdd:PRK08303 160 GTAEynathYRLSVFYDLAKTSVNRLAFSLAHELAPHGATAVALTPGWLRSEMMLDAFGvTEENWRDALAKE--PHFAIS 237

                        250       260       270
                 ....*....|....*....|....*....|....*.
2QQ5_A       225 ETTELSGKCVVALATDPNILSLSGKVLPSCDLARRY 260
Cdd:PRK08303 238 ETPRYVGRAVAALAADPDVARWNGQSLSSGQLARVY 273
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 6-201 1.32e-44

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 148.92  E-value: 1.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A          6 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLD 85
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQA-VERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         86 VLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNVP-YGVG 164
Cdd:pfam00106  80 ILVNN--AGI-----TGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSaYSAS 152

                         170       180       190
                  ....*....|....*....|....*....|....*..
2QQ5_A        165 KAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKE 201
Cdd:pfam00106 153 KAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKE 189
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 5-201 5.07e-14

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


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 69.66  E-value: 5.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A          5 GQVCVVTGASRGIGRGIALQLCKAGATVYIT---------GRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQ 75
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVdlcaddpavGYPLATRAELDAVAAACPDQVLPVIADVRDPAALAAAVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         76 VdREQQGRLDVLVnnAYAGVqtILNTRnkAFWETPASMWDDINNVGLRGhyfcsVYG-ARLMVPA-------GQGLIVVI 147
Cdd:TIGR04504  81 A-VERWGRLDAAV--AAAGV--IAGGR--PLWETTDAELDLLLDVNLRG-----VWNlARAAVPAmlarpdpRGGRFVAV 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
2QQ5_A        148 SSPGSLQYMFNVP-YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKE 201
Cdd:TIGR04504 149 ASAAATRGLPHLAaYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLAA 203
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 7-91 1.06e-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: 39.00  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A           7 VCVVTGASRGIGRGIALQLCKAGA-TVYITGRH---LDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGArRLVLLSRSgpdAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAI-PAVEG 80


                   ....*....
2QQ5_A          83 RLDVLVNNA 91
Cdd:smart00822  81 PLTGVIHAA 89
 
Name Accession Description Interval E-value
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 3-260 5.71e-164

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: 454.60  E-value: 5.71e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQ 81
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTiLPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       82 GRLDVLVNNAYAGVQTILNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNVPY 161
Cdd:cd09763  81 GRLDILVNNAYAAVQLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVAY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVlqdPVLKQFKSAFSSAETTELSGKCVVALATDP 241
Cdd:cd09763 161 GVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEG---SWHAKERDAFLNGETTEYSGRCVVALAADP 237

                       250
                ....*....|....*....
2QQ5_A      242 NILSLSGKVLPSCDLARRY 260
Cdd:cd09763 238 DLMELSGRVLITGELAREY 256
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 3-260 2.49e-98

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: 287.75  E-value: 2.49e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHL--------DTLRVV----AQEAQSLGGQCVPVVCDSSQESEVR 70
Cdd:cd05338   1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTAsegdngsaKSLPGTieetAEEIEAAGGQALPIVVDVRDEDQVR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       71 SLFEQVDrEQQGRLDVLVNNAYAGVQTIlntrnkaFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSP 150
Cdd:cd05338  81 ALVEATV-DQFGRLDILVNNAGAIWLSL-------VEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPP 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      151 GSLQYMF-NVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTellkehmakeevlqdpvlkqfksafsSAETTEL 229
Cdd:cd05338 153 LSLRPARgDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIE--------------------------TPAATEL 206

                       250       260       270
                ....*....|....*....|....*....|.
2QQ5_A      230 SGKCVVALATDPNILSLSGKVLPSCDLARRY 260
Cdd:cd05338 207 SGGSDPARARSPEILSDAVLAILSRPAAERT 237
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-210 4.57e-57

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: 182.68  E-value: 4.57e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        1 APMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQ 80
Cdd:COG1028   2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAA-VAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       81 QGRLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQ-YMFNV 159
Cdd:COG1028  81 FGRLDILVNN--AGI-----TPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRgSPGQA 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
2QQ5_A      160 PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVLQ 210
Cdd:COG1028 154 AYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVRE 204
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 1-260 5.22e-50

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 166.33  E-value: 5.22e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         1 APMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHL----------DTLRVVAQEAQSLGGQCVPVVCDSSQESEVR 70
Cdd:PRK08303   4 KPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTrarrseydrpETIEETAELVTAAGGRGIAVQVDHLVPEQVR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        71 SLFEQVDREqQGRLDVLVNNAYAGvqTILNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSp 150
Cdd:PRK08303  84 ALVERIDRE-QGRLDILVNDIWGG--EKLFEWGKPVWEHSLDKGLRMLRLAIDTHLITSHFALPLLIRRPGGLVVEITD- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       151 GSLQ-----YMFNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMA-KEEVLQDPVLKQfkSAFSSA 224
Cdd:PRK08303 160 GTAEynathYRLSVFYDLAKTSVNRLAFSLAHELAPHGATAVALTPGWLRSEMMLDAFGvTEENWRDALAKE--PHFAIS 237

                        250       260       270
                 ....*....|....*....|....*....|....*.
2QQ5_A       225 ETTELSGKCVVALATDPNILSLSGKVLPSCDLARRY 260
Cdd:PRK08303 238 ETPRYVGRAVAALAADPDVARWNGQSLSSGQLARVY 273
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 2-241 7.38e-47

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: 156.11  E-value: 7.38e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLGGQCVPVVCDSSQESEVRSLFEQVdREQQ 81
Cdd:COG4221   2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAE---LGGRALAVPLDVTDEAAVEAAVAAA-VAEF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       82 GRLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQ-YMFNVP 160
Cdd:COG4221  78 GRLDVLVNN--AGV-----ALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRpYPGGAV 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      161 YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLkEHMAKEEVLQDPVLKQFKSAFSSAETTElsgkCVVALATD 240
Cdd:COG4221 151 YAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFL-DSVFDGDAEAAAAVYEGLEPLTPEDVAE----AVLFALTQ 225


                .
2QQ5_A      241 P 241
Cdd:COG4221 226 P 226
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 8-207 1.78e-46

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: 154.75  E-value: 1.78e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        8 CVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAqEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDVL 87
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELA-AIEALGGNAVAVQADVSDEEDVEALVEEA-LEEFGRLDIL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       88 VNNayAGVQtilntRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQ-YMFNVPYGVGKA 166
Cdd:cd05233  79 VNN--AGIA-----RPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRpLPGQAAYAASKA 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
2QQ5_A      167 ACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEE 207
Cdd:cd05233 152 ALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEA 192
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 6-201 1.32e-44

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 148.92  E-value: 1.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A          6 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLD 85
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQA-VERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         86 VLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNVP-YGVG 164
Cdd:pfam00106  80 ILVNN--AGI-----TGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSaYSAS 152

                         170       180       190
                  ....*....|....*....|....*....|....*..
2QQ5_A        165 KAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKE 201
Cdd:pfam00106 153 KAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKE 189
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
3-198 2.86e-44

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 149.63  E-value: 2.86e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:COG0300   3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAV-LARFG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       83 RLDVLVNNayAGVQTIlntrnKAFWETPASMWDDINNVGLRGHyfcsVYGARL----MVPAGQGLIVVISSPGSLQYM-F 157
Cdd:COG0300  82 PIDVLVNN--AGVGGG-----GPFEELDLEDLRRVFEVNVFGP----VRLTRAllplMRARGRGRIVNVSSVAGLRGLpG 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
2QQ5_A      158 NVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:COG0300 151 MAAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPF 191
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
2-211 1.91e-38

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 134.85  E-value: 1.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQ 80
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQID-EE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        81 QGRLDVLVNNAYAGVqtilntrNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNVP 160
Cdd:PRK08063  80 FGRLDVFVNNAASGV-------LRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYT 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
2QQ5_A       161 Y-GVGKAACDKLAADCAHELRRHG--VSCVSlwPGIVQTELLKEHMAKEEVLQD 211
Cdd:PRK08063 153 TvGVSKAALEALTRYLAVELAPKGiaVNAVS--GGAVDTDALKHFPNREELLED 204
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 5-211 4.62e-37

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: 130.94  E-value: 4.62e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRL 84
Cdd:cd05347   5 GKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEED-FGKI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       85 DVLVNNayAGVQtilntRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNVP-YGV 163
Cdd:cd05347  84 DILVNN--AGII-----RRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPaYAA 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
2QQ5_A      164 GKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVLQD 211
Cdd:cd05347 157 SKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVVADPEFNDD 204
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
3-210 6.10e-37

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 130.67  E-value: 6.10e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQG 82
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAV-EAFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQ-YMFNVPY 161
Cdd:PRK05653  82 ALDILVNN--AGI-----TRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTgNPGQTNY 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
2QQ5_A       162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKE--HMAKEEVLQ 210
Cdd:PRK05653 155 SAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDMTEGlpEEVKAEILK 205
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-200 2.10e-35

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 126.50  E-value: 2.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         4 NGQVCVVTGASRGIGRGIALQLCKAGATVYITG-RHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQG 82
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYdINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIV-EKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNayAGVQTIlntrnKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFN-VPY 161
Cdd:PRK05565  83 KIDILVNN--AGISNF-----GLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCeVLY 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
2QQ5_A       162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLK 200
Cdd:PRK05565 156 SASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWS 194
PRK07035 PRK07035
SDR family oxidoreductase;
5-240 8.48e-35

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 125.13  E-value: 8.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:PRK07035   8 GKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHI-RERHGRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNAYAGVQ--TILNTRNKAFWETpasmwddiNNVGLRGHYFCSVYGARLMVPAGQGLIVVISS-----PGSLQYMf 157
Cdd:PRK07035  87 DILVNNAAANPYfgHILDTDLGAFQKT--------VDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASvngvsPGDFQGI- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       158 nvpYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTE----LLKEHMAKEEVLQDPVLKQFksafssAETTELSGkC 233
Cdd:PRK07035 158 ---YSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKfasaLFKNDAILKQALAHIPLRRH------AEPSEMAG-A 227


                 ....*..
2QQ5_A       234 VVALATD 240
Cdd:PRK07035 228 VLYLASD 234
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 3-217 3.69e-34

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 123.38  E-value: 3.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTL-RVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQ 81
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGaEALVAEIGALGGKALAVQGDVSDAESVERAVDEA-KAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        82 GRLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFN-VP 160
Cdd:PRK05557  82 GGVDILVNN--AGI-----TRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGqAN 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       161 YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL---LKEHMaKEEVLQDPVLKQF 217
Cdd:PRK05557 155 YAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDMtdaLPEDV-KEAILAQIPLGRL 213
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 10-200 1.37e-32

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: 119.38  E-value: 1.37e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       10 VTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDVLV 88
Cdd:cd05359   3 VTGGSRGIGKAIALRLAERGADVVINYRKsKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAV-KERFGRLDVLV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       89 NNAYAGVQtilntrnKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFN-VPYGVGKAA 167
Cdd:cd05359  82 SNAAAGAF-------RPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNyLAVGTAKAA 154

                       170       180       190
                ....*....|....*....|....*....|....*
2QQ5_A      168 CDKLAADCAHELRRHG--VSCVSlwPGIVQTELLK 200
Cdd:cd05359 155 LEALVRYLAVELGPRGirVNAVS--PGVIDTDALA 187
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 5-240 9.81e-32

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: 117.10  E-value: 9.81e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGR-HLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQGR 83
Cdd:cd05358   3 GKVALVTGASSGIGKAIAIRLATAGANVVVNYRsKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAI-KEFGT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       84 LDVLVNNayAGVQtilntRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMV-PAGQGLIVVISS-----PGSlqymF 157
Cdd:cd05358  82 LDILVNN--AGLQ-----GDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRkSKIKGKIINMSSvhekiPWP----G 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      158 NVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVLQDpVLKqfKSAFSSAETTELSGKCVVAL 237
Cdd:cd05358 151 HVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQRAD-LLS--LIPMGRIGEPEEIAAAAAWL 227


                ...
2QQ5_A      238 ATD 240
Cdd:cd05358 228 ASD 230
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 6-216 1.04e-31

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: 116.88  E-value: 1.04e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        6 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRLD 85
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAE-FGPVD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       86 VLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS-------PGslQymfn 158
Cdd:cd05333  80 ILVNN--AGI-----TRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSvvglignPG--Q---- 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
2QQ5_A      159 VPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKehmAKEEVLQDPVLKQ 216
Cdd:cd05333 147 ANYAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTD---ALPEKVKEKILKQ 201
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-212 1.08e-31

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 116.89  E-value: 1.08e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGR-HLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQvDREQ 80
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAA-AVER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        81 QGRLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYfcsvYGARLMVP----AGQGLIVVISSPGSLQ-Y 155
Cdd:PRK12825  82 FGRIDILVNN--AGI-----FEDKPLADMSDDEWDEVIDVNLSGVF----HLLRAVVPpmrkQRGGRIVNISSVAGLPgW 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
2QQ5_A       156 MFNVPYGVGKAACDKLAADCAHELRRHG--VSCVSlwPGIVQTELLKEHMAKEEVLQDP 212
Cdd:PRK12825 151 PGRSNYAAAKAGLVGLTKALARELAEYGitVNMVA--PGDIDTDMKEATIEEAREAKDA 207
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 5-240 9.04e-31

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: 114.74  E-value: 9.04e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQE-AQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGR 83
Cdd:cd05352   8 GKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEElAKKYGVKTKAYKCDVSSQESVEKTFKQIQKD-FGK 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       84 LDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSlqYMFNVP--- 160
Cdd:cd05352  87 IDILIAN--AGI-----TVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSG--TIVNRPqpq 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      161 --YGVGKAACDKLAADCAHELRRHG--VSCVSlwPGIVQTELLKEHMAKEEVLQDPVLKQFKsafsSAETTELSGKCVVa 236
Cdd:cd05352 158 aaYNASKAAVIHLAKSLAVEWAKYFirVNSIS--PGYIDTDLTDFVDKELRKKWESYIPLKR----IALPEELVGAYLY- 230


                ....
2QQ5_A      237 LATD 240
Cdd:cd05352 231 LASD 234
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 15-200 1.08e-30

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: 114.06  E-value: 1.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         15 RGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPvvCDSSQESEVRSLFEQVdREQQGRLDVLVNNayAG 94
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEELGAAVLP--CDVTDEEQVEALVAAA-VEKFGRLDILVNN--AG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         95 vqtILNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPagQGLIVVISSPGSLQYMFNV-PYGVGKAACDKLAA 173
Cdd:pfam13561  81 ---FAPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE--GGSIVNLSSIGAERVVPNYnAYGAAKAALEALTR 155

                         170       180
                  ....*....|....*....|....*....
2QQ5_A        174 DCAHELRRHG--VSCVSlwPGIVQTELLK 200
Cdd:pfam13561 156 YLAVELGPRGirVNAIS--PGPIKTLAAS 182
FabG-like PRK07231
SDR family oxidoreductase;
5-204 3.55e-30

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 113.00  E-value: 3.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSlGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:PRK07231   5 GKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILA-GGRAIAVAADVSDEADVEAAVAAA-LERFGSV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNayAGVqtilNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFN-VPYGV 163
Cdd:PRK07231  83 DILVNN--AGT----THRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGlGWYNA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
2QQ5_A       164 GKAACDKLAADCAHELRRHG--VSCVSlwPGIVQTELLKEHMA 204
Cdd:PRK07231 157 SKGAVITLTKALAAELGPDKirVNAVA--PVVVETGLLEAFMG 197
PRK05867 PRK05867
SDR family oxidoreductase;
3-212 6.93e-30

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 112.44  E-value: 6.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQG 82
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 rLDVLVNNayAGVQTIlntrnKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSlQYMFNVPYG 162
Cdd:PRK05867  87 -IDIAVCN--AGIITV-----TPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQGGVIINTASMS-GHIINVPQQ 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
2QQ5_A       163 VG-----KAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLkEHMAKEEVLQDP 212
Cdd:PRK05867 158 VShycasKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELV-EPYTEYQPLWEP 211
PRK12826 PRK12826
SDR family oxidoreductase;
1-201 1.33e-29

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 111.55  E-value: 1.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         1 APMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQ 80
Cdd:PRK12826   2 RDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGV-ED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        81 QGRLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQ--YMFN 158
Cdd:PRK12826  81 FGRLDILVAN--AGI-----FPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRvgYPGL 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
2QQ5_A       159 VPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKE 201
Cdd:PRK12826 154 AHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGN 196
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 3-198 1.07e-28

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 109.29  E-value: 1.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:PRK12939   5 LAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAA-AAALG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNVP-Y 161
Cdd:PRK12939  84 GLDGLVNN--AGI-----TNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGaY 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
2QQ5_A       162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK12939 157 VASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEA 193
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 3-198 1.70e-28

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: 108.65  E-value: 1.70e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVP---VVCDSSQESEVRSLFEQVdRE 79
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSEKKillVVADLTEEEGQDRIISTT-LA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       80 QQGRLDVLVNNAYAGVQtilntrnKAFWETPASMWDDINNVGLRGhyfcSVYGARLMVP---AGQGLIVVISS-PGSLQY 155
Cdd:cd05364  80 KFGRLDILVNNAGILAK-------GGGEDQDIEEYDKVMNLNLRA----VIYLTKLAVPhliKTKGEIVNVSSvAGGRSF 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
2QQ5_A      156 MFNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:cd05364 149 PGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGF 191
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 5-207 2.45e-28

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: 108.35  E-value: 2.45e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTlrvvAQE-AQSLGGQCVPVVCDSSQESEVRSLFEQVDREQqGR 83
Cdd:cd08944   3 GKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGA----AQAvVAQIAGGALALRVDVTDEQQVAALFERAVEEF-GG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       84 LDVLVNNAYAgvqtilNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS----PGSLQYmfnV 159
Cdd:cd08944  78 LDLLVNNAGA------MHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSiagqSGDPGY---G 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
2QQ5_A      160 PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEE 207
Cdd:cd08944 149 AYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFE 196
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 3-215 3.31e-28

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 108.05  E-value: 3.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDReQQG 82
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVE-TFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNayAGVQTILNTRnkafwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQ-YMFNVPY 161
Cdd:PRK12429  81 GVDILVNN--AGIQHVAPIE-----DFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVgSAGKAAY 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
2QQ5_A       162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAK---------EEVLQDPVLK 215
Cdd:PRK12429 154 VSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTPLVRKQIPDlakergiseEEVLEDVLLP 216
PRK06181 PRK06181
SDR family oxidoreductase;
5-200 1.98e-27

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 106.22  E-value: 1.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAA-VARFGGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNayAGVqtilnTRNKAFWETPA-SMWDDINNVglrgHYFCSVYGARLMVP---AGQGLIVVISspgSLQYMFNVP 160
Cdd:PRK06181  80 DILVNN--AGI-----TMWSRFDELTDlSVFERVMRV----NYLGAVYCTHAALPhlkASRGQIVVVS---SLAGLTGVP 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
2QQ5_A       161 YGVGKAA--------CDKLAAdcahELRRHGVSCVSLWPGIVQTELLK 200
Cdd:PRK06181 146 TRSGYAAskhalhgfFDSLRI----ELADDGVAVTVVCPGFVATDIRK 189
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 4-208 3.03e-26

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: 102.74  E-value: 3.03e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        4 NGQVCVVTGASRGIGRGIALQLCKAGATV---YITGRhlDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQ 80
Cdd:cd05362   2 AGKVALVTGASRGIGRAIAKRLARDGASVvvnYASSK--AAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAE-KA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       81 QGRLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQglIVVISSPGSLQYM-FNV 159
Cdd:cd05362  79 FGGVDILVNN--AGV-----MLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDGGR--IINISSSLTAAYTpNYG 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
2QQ5_A      160 PYGVGKAACDKLAADCAHELRRHGVS--CVSlwPGIVQTELLKEHMAKEEV 208
Cdd:cd05362 150 AYAGSKAAVEAFTRVLAKELGGRGITvnAVA--PGPVDTDMFYAGKTEEAV 198
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 5-205 5.00e-26

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: 102.28  E-value: 5.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSL-GGQCVPVVCDSSQESEVRSLFEQVDREqQGR 83
Cdd:cd05369   3 GKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSAtGGRAHPIQCDVRDPEAVEAAVDETLKE-FGK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       84 LDVLVNNAyAGvqtilNtrnkafWETPASM-----WDDINNVGLRGHYFCS-VYGARLMVPAGQGLIVVISSPGSLQYM- 156
Cdd:cd05369  82 IDILINNA-AG-----N------FLAPAESlspngFKTVIDIDLNGTFNTTkAVGKRLIEAKHGGSILNISATYAYTGSp 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
2QQ5_A      157 FNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEllkEHMAK 205
Cdd:cd05369 150 FQVHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTT---EGMER 195
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 9-203 1.55e-25

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: 100.77  E-value: 1.55e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        9 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRvvaQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDVLV 88
Cdd:cd05374   4 LITGCSSGIGLALALALAAQGYRVIATARNPDKLE---SLGELLNDNLEVLELDVTDEESIKAAVKEV-IERFGRIDVLV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       89 NNA---YAGvqtilntrnkAFWETPAsmwDDINNVglrghYFCSVYG--------ARLMVPAGQGLIVVISSPGSLQYM- 156
Cdd:cd05374  80 NNAgygLFG----------PLEETSI---EEVREL-----FEVNVFGplrvtrafLPLMRKQGSGRIVNVSSVAGLVPTp 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
2QQ5_A      157 FNVPYGVGKAACDKLaADC-AHELRRHGVSCVSLWPGIVQTELLKEHM 203
Cdd:cd05374 142 FLGPYCASKAALEAL-SESlRLELAPFGIKVTIIEPGPVRTGFADNAA 188
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-218 2.25e-25

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 100.15  E-value: 2.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:PRK07666   5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQL-KNELG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNayAGVQTILNtrnkaFWETPASMWDDINNVGLRGHYfcsvYGARLMVPA----GQGLIVVISSPGSLQYMFN 158
Cdd:PRK07666  84 SIDILINN--AGISKFGK-----FLELDPAEWEKIIQVNLMGVY----YATRAVLPSmierQSGDIINISSTAGQKGAAV 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       159 V-PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLK---------EHMAKEEVLQDPVLKQFK 218
Cdd:PRK07666 153 TsAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVdlgltdgnpDKVMQPEDLAEFIVAQLK 222
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 5-217 2.40e-25

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: 100.43  E-value: 2.40e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKA-GDAFGRV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       85 DVLVNNAYAGvqtilntRNKAFWETPASMWDDinnvGLRGHYFCSVYGARLMVPA----GQGLIVVISSPGSLQYMFN-V 159
Cdd:cd05344  80 DILVNNAGGP-------PPGPFAELTDEDWLE----AFDLKLLSVIRIVRAVLPGmkerGWGRIVNISSLTVKEPEPNlV 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
2QQ5_A      160 PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTE----LLKEHMAKEEVLQDPVLKQF 217
Cdd:cd05344 149 LSNVARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTErvrrLLEARAEKEGISVEEAEKEV 210
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 5-240 7.15e-25

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 99.25  E-value: 7.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:PRK08213  12 GKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEET-LERFGHV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNAYAGvqtilntrnkafW-----ETPASMWDDINNVGLRGHYFCS-VYGARLMVPAGQGLIVVISSPGSLQ---- 154
Cdd:PRK08213  91 DILVNNAGAT------------WgapaeDHPVEAWDKVMNLNVRGLFLLSqAVAKRSMIPRGYGRIINVASVAGLGgnpp 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       155 -YMFNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTE----LLKEHmaKEEVLQDPVLKQFKSafssaeTTEL 229
Cdd:PRK08213 159 eVMDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKmtrgTLERL--GEDLLAHTPLGRLGD------DEDL 230

                        250
                 ....*....|.
2QQ5_A       230 SGKCVVaLATD 240
Cdd:PRK08213 231 KGAALL-LASD 240
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 3-211 1.19e-24

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: 98.38  E-value: 1.19e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERT-VEALG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       83 RLDVLVNNAYAGVQTILNTRNKAFWETPAsmwdDINNVGLrghyfcsVYGAR----LMVPAGQGLIVVISS-------PG 151
Cdd:cd08934  80 RLDILVNNAGIMLLGPVEDADTTDWTRMI----DTNLLGL-------MYTTHaalpHHLLRNKGTIVNISSvagrvavRN 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
2QQ5_A      152 SlqymfnVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTElLKEHM-------AKEEVLQD 211
Cdd:cd08934 149 S------AVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTE-LRDHIthtitkeAYEERIST 208
PRK06172 PRK06172
SDR family oxidoreductase;
5-220 1.76e-24

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 98.28  E-value: 1.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:PRK06172   7 GKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQT-IAAYGRL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNAYAGVQtilntrNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNVP-YGV 163
Cdd:PRK06172  86 DYAFNNAGIEIE------QGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSiYAA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
2QQ5_A       164 GKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEllkehMAKEEVLQDPVLKQFKSA 220
Cdd:PRK06172 160 SKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTD-----MFRRAYEADPRKAEFAAA 211
PRK08278 PRK08278
SDR family oxidoreductase;
1-191 2.09e-24

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 98.44  E-value: 2.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         1 APMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGR----HLD---TLRVVAQEAQSLGGQCVPVVCDSSQESEVRslf 73
Cdd:PRK08278   2 MSLSGKTLFITGASRGIGLAIALRAARDGANIVIAAKtaepHPKlpgTIHTAAEEIEAAGGQALPLVGDVRDEDQVA--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        74 EQVDR--EQQGRLDVLVNNAYAgvqtiLNTRNKAfwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPG 151
Cdd:PRK08278  79 AAVAKavERFGGIDICVNNASA-----INLTGTE--DTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSPPL 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
2QQ5_A       152 SL-QYMF--NVPYGVGKAACDKLAADCAHELRRHGVSCVSLWP 191
Cdd:PRK08278 152 NLdPKWFapHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 3-241 3.30e-24

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 97.66  E-value: 3.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:PRK13394   5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKV-AERFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNayAGVQTILNTRNKAFwetpaSMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVV--------ISSPGSLQ 154
Cdd:PRK13394  84 SVDILVSN--AGIQIVNPIENYSF-----ADWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIymgsvhshEASPLKSA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       155 YMfnvpygVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHM---AKEE-VLQDPVLKQF---KSAFSSAETT 227
Cdd:PRK13394 157 YV------TAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIpeqAKELgISEEEVVKKVmlgKTVDGVFTTV 230

                        250
                 ....*....|....
2QQ5_A       228 ELSGKCVVALATDP 241
Cdd:PRK13394 231 EDVAQTVLFLSSFP 244
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 5-184 3.64e-24

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: 97.08  E-value: 3.64e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQsLGGQCVPVVCDSSQESEVRSLFEQVDREQQGrL 84
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQ-GGPRALGVQCDVTSEAQVQSAFEQAVLEFGG-L 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       85 DVLVNNayAGVQTilntrNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQG--LIVVISSPGSLQYMFNVPYG 162
Cdd:cd08943  79 DIVVSN--AGIAT-----SSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGgnIVFNASKNAVAPGPNAAAYS 151

                       170       180
                ....*....|....*....|..
2QQ5_A      163 VGKAACDKLAADCAHELRRHGV 184
Cdd:cd08943 152 AAKAAEAHLARCLALEGGEDGI 173
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 3-210 5.03e-24

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: 96.78  E-value: 5.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLgGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:cd08942   4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAY-GECIAIPADLSSEEGIEALVARV-AERSD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       83 RLDVLVNNAYAgvqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQ----------GLIVVISSPGS 152
Cdd:cd08942  82 RLDVLVNNAGA-------TWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaenparviniGSIAGIVVSGL 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
2QQ5_A      153 LQYmfnvPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTE----LLKEHMAKEEVLQ 210
Cdd:cd08942 155 ENY----SYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKmtafLLNDPAALEAEEK 212
PRK07326 PRK07326
SDR family oxidoreductase;
3-197 8.96e-24

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 95.85  E-value: 8.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSlGGQCVPVVCDSSQESEVRSLFEQVDREQqG 82
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNN-KGNVLGLAADVRDEADVQRAVDAIVAAF-G 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNA----YAGVQtilntrnkafwETPASMWDDINNVGLRGHYfcsvYGARLMVPA---GQGLIVVISSPGslqy 155
Cdd:PRK07326  82 GLDVLIANAgvghFAPVE-----------ELTPEEWRLVIDTNLTGAF----YTIKAAVPAlkrGGGYIINISSLA---- 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
2QQ5_A       156 mfnvpygvGKAACDKLAADCAH-------------ELRRHGVSCVSLWPGIVQTE 197
Cdd:PRK07326 143 --------GTNFFAGGAAYNASkfglvgfseaamlDLRQYGIKVSTIMPGSVATH 189
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 9-210 1.25e-23

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: 95.27  E-value: 1.25e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        9 VVTGASRGIGRGIALQLCKAGATVYITGRhlDTLRvVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRLDVLV 88
Cdd:cd08929   4 LVTGASRGIGEATARLLHAEGYRVGICAR--DEAR-LAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEA-FGGLDALV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       89 NNAYAGVQTILNTRnkafweTPASMWDDINNVgLRGHYFCSVYGARLMVPAGQGLIVVISS-PGSLQYMFNVPYGVGKAA 167
Cdd:cd08929  80 NNAGVGVMKPVEEL------TPEEWRLVLDTN-LTGAFYCIHKAAPALLRRGGGTIVNVGSlAGKNAFKGGAAYNASKFG 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
2QQ5_A      168 CDKLAADCAHELRRHGVSCVSLWPGIVQTELLKE------HMAKEEVLQ 210
Cdd:cd08929 153 LLGLSEAAMLDLREANIRVVNVMPGSVDTGFAGSpegqawKLAPEDVAQ 201
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-198 1.67e-23

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 95.41  E-value: 1.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:PRK08217   3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQI-AEDFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNayAGVqtilnTRN---------KAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQ-GLIVVISSPGS 152
Cdd:PRK08217  82 QLNGLINN--AGI-----LRDgllvkakdgKVTSKMSLEQFQSVIDVNLTGVFLCGREAAAKMIESGSkGVIINISSIAR 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
2QQ5_A       153 LQYMFNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK08217 155 AGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEM 200
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 1-197 1.95e-23

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 95.51  E-value: 1.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         1 APMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLrvvAQEAQSLGGQCV-PVVCDSSQESEVRSLFEQVdRE 79
Cdd:PRK12829   7 KPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAAL---AATAARLPGAKVtATVADVADPAQVERVFDTA-VE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        80 QQGRLDVLVNNA-----YAGVQTIlntrnkafweTPASmWDDINNVGLRGHYfcsvYGARLMVPA-----GQGLIVVISS 149
Cdd:PRK12829  83 RFGGLDVLVNNAgiagpTGGIDEI----------TPEQ-WEQTLAVNLNGQF----YFARAAVPLlkasgHGGVIIALSS 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
2QQ5_A       150 -PGSLQYMFNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTE 197
Cdd:PRK12829 148 vAGRLGYPGRTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGP 196
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
2-184 2.57e-23

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 98.76  E-value: 2.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLGGQ--CVPVVCDSSQESEVRSLFEQVDRE 79
Cdd:PRK08324 419 PLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAE---LGGPdrALGVACDVTDEAAVQAAFEEAALA 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        80 QQGrLDVLVNNAYAGVQtilntrnKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQG-LIVVISS-----PGSL 153
Cdd:PRK08324 496 FGG-VDIVVSNAGIAIS-------GPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLGgSIVFIASknavnPGPN 567

                        170       180       190
                 ....*....|....*....|....*....|.
2QQ5_A       154 qymfNVPYGVGKAACDKLAADCAHELRRHGV 184
Cdd:PRK08324 568 ----FGAYGAAKAAELHLVRQLALELGPDGI 594
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 3-191 9.00e-23

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: 93.28  E-value: 9.00e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLD-------TLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQ 75
Cdd:cd09762   1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgTIYTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       76 VdREQQGRLDVLVNNAYAgvqtiLNTRNKAfwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQY 155
Cdd:cd09762  81 A-VEKFGGIDILVNNASA-----ISLTGTL--DTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLNP 152

                       170       180       190
                ....*....|....*....|....*....|....*....
2QQ5_A      156 MF---NVPYGVGKAACDKLAADCAHELRRHGVSCVSLWP 191
Cdd:cd09762 153 KWfknHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 4-198 9.73e-23

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: 93.59  E-value: 9.73e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        4 NGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLD-TLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:cd05366   1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEeAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQA-VEKFG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       83 RLDVLVNNayAGVQTIlntrnKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQG--LIVVISSPGSLQYMFNVP 160
Cdd:cd05366  80 SFDVMVNN--AGIAPI-----TPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHGgkIINASSIAGVQGFPNLGA 152

                       170       180       190
                ....*....|....*....|....*....|....*...
2QQ5_A      161 YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:cd05366 153 YSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEM 190
PRK07774 PRK07774
SDR family oxidoreductase;
5-197 1.01e-22

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 93.27  E-value: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:PRK07774   6 DKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADAT-VSAFGGI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNA--YAGVQ-TILNTrnkafweTPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSlqYMFNVPY 161
Cdd:PRK07774  85 DYLVNNAaiYGGMKlDLLIT-------VPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAA--WLYSNFY 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
2QQ5_A       162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTE 197
Cdd:PRK07774 156 GLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTE 191
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 3-212 1.16e-22

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: 93.28  E-value: 1.16e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQG 82
Cdd:cd05329   4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFGG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       83 RLDVLVNNayAGVqtilNTRNKAFWETPASmWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS-PGSLQYMFNVPY 161
Cdd:cd05329  84 KLNILVNN--AGT----NIRKEAKDYTEED-YSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSvAGVIAVPSGAPY 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
2QQ5_A      162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLkehmakEEVLQDP 212
Cdd:cd05329 157 GATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLV------EPVIQQK 201
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 4-198 2.11e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 92.47  E-value: 2.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         4 NGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAqslggQCVPVVCDSSQESEVRSLFeqvdrEQQGR 83
Cdd:PRK07060   8 SGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGET-----GCEPLRLDVGDDAAIRAAL-----AAAGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        84 LDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQ-GLIVVISSPGSLQ-YMFNVPY 161
Cdd:PRK07060  78 FDGLVNC--AGI-----ASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRgGSIVNVSSQAALVgLPDHLAY 150

                        170       180       190
                 ....*....|....*....|....*....|....*..
2QQ5_A       162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK07060 151 CASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPM 187
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 3-198 2.59e-22

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: 92.26  E-value: 2.59e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVV-CDSSQESEVRSLFEQVdREQQ 81
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVpLDMSDLEDAEQVVEEA-LKLF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       82 GRLDVLVNNAyagvqtILNTRNKaFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISspgSLQYMFNVPY 161
Cdd:cd05332  80 GGLDILINNA------GISMRSL-FHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVS---SIAGKIGVPF 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
2QQ5_A      162 GVGKAAcDKLA----ADC-AHELRRHGVSCVSLWPGIVQTEL 198
Cdd:cd05332 150 RTAYAA-SKHAlqgfFDSlRAELSEPNISVTVVCPGLIDTNI 190
PRK07814 PRK07814
SDR family oxidoreductase;
3-215 3.00e-22

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 92.53  E-value: 3.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQA-VEAFG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNN-AYAGVQTILNTRNKAFWETPASmwddinNVGlRGHYFcSVYGARLMV-PAGQGLIVVISSP-GSLQYMFNV 159
Cdd:PRK07814  87 RLDIVVNNvGGTMPNPLLSTSTKDLADAFTF------NVA-TAHAL-TVAAVPLMLeHSGGGSVINISSTmGRLAGRGFA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       160 PYGVGKAACD---KLAA-DCAHELRRHGVScvslwPGIVQTELLKEHMAKEEvLQDPVLK 215
Cdd:PRK07814 159 AYGTAKAALAhytRLAAlDLCPRIRVNAIA-----PGSILTSALEVVAANDE-LRAPMEK 212
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 3-240 4.37e-22

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: 91.68  E-value: 4.37e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:cd05341   3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAE---LGDAARFFHLDVTDEDGWTAVVDTA-REAFG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       83 RLDVLVNNayAGVQTILNTRnkafwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNVP-Y 161
Cdd:cd05341  79 RLDVLVNN--AGILTGGTVE-----TTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAaY 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      162 GVGKAACDKLAADCAHELRRH--GVSCVSLWPGIVQTELLKEHMAKEEVLQDPVLKQFKSAfssAETTELSGkCVVALAT 239
Cdd:cd05341 152 NASKGAVRGLTKSAALECATQgyGIRVNSVHPGYIYTPMTDELLIAQGEMGNYPNTPMGRA---GEPDEIAY-AVVYLAS 227


                .
2QQ5_A      240 D 240
Cdd:cd05341 228 D 228
PRK08589 PRK08589
SDR family oxidoreductase;
3-240 5.41e-22

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 91.76  E-value: 5.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVyITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYV-LAVDIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEI-KEQFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNAyaGVqtilNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNVPYG 162
Cdd:PRK08589  82 RVDVLFNNA--GV----DNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAADLYRSGYN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       163 VGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEvlqDPVLKQFKSA------FSSAETTELSGKCVVA 236
Cdd:PRK08589 156 AAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTGTSE---DEAGKTFRENqkwmtpLGRLGKPEEVAKLVVF 232


                 ....
2QQ5_A       237 LATD 240
Cdd:PRK08589 233 LASD 236
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 3-240 5.47e-22

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: 91.36  E-value: 5.47e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLGGQCVPVV-CDSSQESEVRSLF-EQVDReq 80
Cdd:cd05326   2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAE---LGDPDISFVhCDVTVEADVRAAVdTAVAR-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       81 QGRLDVLVNNAyaGVqtiLNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNV- 159
Cdd:cd05326  77 FGRLDIMFNNA--GV---LGAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPh 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      160 PYGVGKAACDKLAADCAHELRRHG--VSCVSlwPGIVQTELLKEHMAKEEVLQDPVLKQFKSAFSSAETTELSGKCVVAL 237
Cdd:cd05326 152 AYTASKHAVLGLTRSAATELGEHGirVNCVS--PYGVATPLLTAGFGVEDEAIEEAVRGAANLKGTALRPEDIAAAVLYL 229


                ...
2QQ5_A      238 ATD 240
Cdd:cd05326 230 ASD 232
PRK12743 PRK12743
SDR family oxidoreductase;
6-196 5.77e-22

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 91.63  E-value: 5.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         6 QVCVVTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIGITWHSdEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKL-IQRLGRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNAYAGVqtilntrNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQ-GLIVVISS-------PGSlqym 156
Cdd:PRK12743  82 DVLVNNAGAMT-------KAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQgGRIINITSvhehtplPGA---- 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
2QQ5_A       157 fnVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQT 196
Cdd:PRK12743 151 --SAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIAT 188
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 7-198 6.34e-22

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: 91.37  E-value: 6.34e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        7 VCVVTGASRGIGRGIALQLCKAGATVYIT-GRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLD 85
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAARGFDIAINdLPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQA-WEDFGRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       86 VLVNNayAGVQTilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMV-----PAG-QGLIVVISSPGSlqYMFNV 159
Cdd:cd05337  82 CLVNN--AGIAV---RPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVeqpdrFDGpHRSIIFVTSINA--YLVSP 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
2QQ5_A      160 ---PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:cd05337 155 nrgEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDM 196
PRK12746 PRK12746
SDR family oxidoreductase;
3-239 1.12e-21

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 90.86  E-value: 1.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYI-TGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQ 81
Cdd:PRK12746   4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNELQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        82 GR-----LDVLVNNAYAGVQ-TILNTRNKAFwetpasmwDDINNVGLRGHYFcsVYGARLMVPAGQGLIVVISSPG-SLQ 154
Cdd:PRK12746  84 IRvgtseIDILVNNAGIGTQgTIENTTEEIF--------DEIMAVNIKAPFF--LIQQTLPLLRAEGRVINISSAEvRLG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       155 YMFNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELlkehmaKEEVLQDPVLKQF---KSAFSSAETTELSG 231
Cdd:PRK12746 154 FTGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDI------NAKLLDDPEIRNFatnSSVFGRIGQVEDIA 227


                 ....*...
2QQ5_A       232 KCVVALAT 239
Cdd:PRK12746 228 DAVAFLAS 235
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 5-249 1.24e-21

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: 90.75  E-value: 1.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRVVAQEAQSLGGQCVPVV-CD-SSQESeVRSLFEQVdREQQ 81
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNeEKGEEAAAEIKKETGNAKVEVIqLDlSSLAS-VRQFAEEF-LARF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       82 GRLDVLVNNAYAGVQTILNTRNkafwetpasmwddinnvGLRGH----YFCSVYGARLMVPA----GQGLIVVISSpgSL 153
Cdd:cd05327  79 PRLDILINNAGIMAPPRRLTKD-----------------GFELQfavnYLGHFLLTNLLLPVlkasAPSRIVNVSS--IA 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      154 QYM-----------FNVPYGVGKAACD-KLAadC---AHELRRH----GVSCVSLWPGIVQTELLKEHmaKEEVLQDPVL 214
Cdd:cd05327 140 HRAgpidfndldleNNKEYSPYKAYGQsKLA--NilfTRELARRlegtGVTVNALHPGVVRTELLRRN--GSFFLLYKLL 215

                       250       260       270
                ....*....|....*....|....*....|....*..
2QQ5_A      215 KQF--KSAFSSAETTelsgkcvVALATDPNILSLSGK 249
Cdd:cd05327 216 RPFlkKSPEQGAQTA-------LYAATSPELEGVSGK 245
PRK09242 PRK09242
SDR family oxidoreductase;
3-216 1.34e-21

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 90.58  E-value: 1.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQ 80
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDElaEEFPEREVHGLAADVSDDEDRRAILDWVE-DH 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        81 QGRLDVLVNNayAGVqtilNTRNKAFWETPASmWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFN-V 159
Cdd:PRK09242  86 WDGLHILVNN--AGG----NIRKAAIDYTEDE-WRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSgA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
2QQ5_A       160 PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVLQdPVLKQ 216
Cdd:PRK09242 159 PYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYE-QVIER 214
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 3-200 3.83e-21

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 89.14  E-value: 3.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFeQVDREQQG 82
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALA-DFALSKLG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNAYAGvqtilntRNKAFwETPAS--MWDDINNVglrghyFCSVYGARLMVP----AGQGLIVVISS-PGSLQY 155
Cdd:PRK06113  88 KVDILVNNAGGG-------GPKPF-DMPMAdfRRAYELNV------FSFFHLSQLVAPemekNGGGVILTITSmAAENKN 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
2QQ5_A       156 MFNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLK 200
Cdd:PRK06113 154 INMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALK 198
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 7-249 4.09e-21

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: 88.45  E-value: 4.09e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        7 VCVVTGASRGIGRGIALQLCKAGA-TVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLD 85
Cdd:cd05324   2 VALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFV-EEKYGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       86 VLVNNayAGVQTILNTRNKAFWETpASMWDDINnvglrghyfcsVYGAR--------LMVPAGQGLIVVISS-PGSLQym 156
Cdd:cd05324  81 ILVNN--AGIAFKGFDDSTPTREQ-ARETMKTN-----------FFGTVdvtqallpLLKKSPAGRIVNVSSgLGSLT-- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      157 fnVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEllkehMAKEevlqdpvlKQFKSAFSSAETtelsgkcVVA 236
Cdd:cd05324 145 --SAYGVSKAALNALTRILAKELKETGIKVNACCPGWVKTD-----MGGG--------KAPKTPEEGAET-------PVY 202

                       250
                ....*....|...
2QQ5_A      237 LATDPNILSLSGK 249
Cdd:cd05324 203 LALLPPDGEPTGK 215
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 1-197 4.79e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 88.91  E-value: 4.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         1 APMNGQVCVVTGASRGIGRGIALQLCKAGAT-VYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrE 79
Cdd:PRK06198   2 GRLDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAAD-E 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        80 QQGRLDVLVNNAYagvqtiLNTRNkAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAG-QGLIVVISSPGSL--QyM 156
Cdd:PRK06198  81 AFGRLDALVNAAG------LTDRG-TILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKaEGTIVNIGSMSAHggQ-P 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
2QQ5_A       157 FNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTE 197
Cdd:PRK06198 153 FLAAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATE 193
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 1-198 7.99e-21

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 88.26  E-value: 7.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         1 APMNGQVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdRE 79
Cdd:PRK12937   1 MTLSNKVAIVTGASRGIGAAIARRLAADGFAVAVNyAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAA-ET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        80 QQGRLDVLVNNayAGVQTILNTRnkafwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQglIVVIS-SPGSLQYMFN 158
Cdd:PRK12937  80 AFGRIDVLVNN--AGVMPLGTIA-----DFDLEDFDRTIATNLRGAFVVLREAARHLGQGGR--IINLStSVIALPLPGY 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
2QQ5_A       159 VPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK12937 151 GPYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 4-240 9.00e-21

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: 88.27  E-value: 9.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        4 NGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHlDTLRVVAQEAQSLGGQCVPVV---CDSSQESEVRSLFEQVDReQ 80
Cdd:cd08940   1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGFG-DAAEIEAVRAGLAAKHGVKVLyhgADLSKPAAIEDMVAYAQR-Q 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       81 QGRLDVLVNNayAGVQTIlntrnKAFWETPASMWDDINNVGLRGhyfcSVYGARLMVPA----GQGLIVVISSP-GSLQY 155
Cdd:cd08940  79 FGGVDILVNN--AGIQHV-----APIEDFPTEKWDAIIALNLSA----VFHTTRLALPHmkkqGWGRIINIASVhGLVAS 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      156 MFNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHM-------------AKEEVLQDpvlKQFKSAFS 222
Cdd:cd08940 148 ANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVEKQIsalaqkngvpqeqAARELLLE---KQPSKQFV 224

                       250
                ....*....|....*...
2QQ5_A      223 SAEttELsGKCVVALATD 240
Cdd:cd08940 225 TPE--QL-GDTAVFLASD 239
PRK06138 PRK06138
SDR family oxidoreductase;
3-205 1.02e-20

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 87.90  E-value: 1.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSlGGQCVPVVCDSSQESEVRSLFEQVDREqQG 82
Cdd:PRK06138   3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAA-GGRAFARQGDVGSAEAVEALVDFVAAR-WG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNAYAGVQTILNTrnkafweTPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYM-FNVPY 161
Cdd:PRK06138  81 RLDVLVNNAGFGCGGTVVT-------TDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGrGRAAY 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
2QQ5_A       162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAK 205
Cdd:PRK06138 154 VASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFAR 197
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 2-206 1.16e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 87.79  E-value: 1.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDtlrvVAQEAQSLG-GQCVPVVCDSSQESEVRSLFEQVdREQ 80
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSED----VAEVAAQLLgGNAKGLVCDVSDSQSVEAAVAAV-ISA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        81 QGRLDVLVNNayAGVQTIlntrNKAFwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS-PGSLQYMFNV 159
Cdd:PRK06841  87 FGRIDILVNS--AGVALL----APAE-DVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASqAGVVALERHV 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
2QQ5_A       160 PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKE 206
Cdd:PRK06841 160 AYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGKKAWAGE 206
PRK07454 PRK07454
SDR family oxidoreductase;
10-198 1.22e-20

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 87.71  E-value: 1.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        10 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDVLVN 89
Cdd:PRK07454  11 ITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAEL-LEQFGCPDVLIN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        90 NAYAGvqtilntRNKAFWETPASMWDDINNVGLRGHYFCsvygARLMVPA----GQGLIVVISSPGSlqymFNV-----P 160
Cdd:PRK07454  90 NAGMA-------YTGPLLEMPLSDWQWVIQLNLTSVFQC----CSAVLPGmrarGGGLIINVSSIAA----RNAfpqwgA 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
2QQ5_A       161 YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK07454 155 YCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPL 192
PRK06124 PRK06124
SDR family oxidoreductase;
5-208 1.69e-20

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 87.46  E-value: 1.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRL 84
Cdd:PRK06124  11 GQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAE-HGRL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNAYAgvqtilntRN-KAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS-PGSLQYMFNVPYG 162
Cdd:PRK06124  90 DILVNNVGA--------RDrRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSiAGQVARAGDAVYP 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
2QQ5_A       163 VGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEV 208
Cdd:PRK06124 162 AAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATETNAAMAADPAV 207
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 7-216 2.65e-20

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: 86.85  E-value: 2.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        7 VCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDV 86
Cdd:cd05365   1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKAT-VSQFGGITI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       87 LVNNAYAGvqtilntrnKAFWETPASMWDDINNV---GLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNV-PYG 162
Cdd:cd05365  80 LVNNAGGG---------GPKPFDMPMTEEDFEWAfklNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIaAYG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
2QQ5_A      163 VGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKE---HMAKEEVLQDPVLKQ 216
Cdd:cd05365 151 SSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALASvltPEIERAMLKHTPLGR 207
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 7-203 3.43e-20

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: 85.88  E-value: 3.43e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        7 VCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRvvaqeAQSLGGQCV-PVVCDSSQESEVRSLFEQVdREQQGRLD 85
Cdd:cd08932   2 VALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLA-----ALSASGGDVeAVPYDARDPEDARALVDAL-RDRFGRID 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       86 VLVNNAYAGVQTILNTRNKAFWEtpaSMWdDINnvglrghyfcsVYGARLMV--------PAGQGLIVVISS-PGSLQYM 156
Cdd:cd08932  76 VLVHNAGIGRPTTLREGSDAELE---AHF-SIN-----------VIAPAELTrallpalrEAGSGRVVFLNSlSGKRVLA 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
2QQ5_A      157 FNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHM 203
Cdd:cd08932 141 GNAGYSASKFALRALAHALRQEGWDHGVRVSAVCPGFVDTPMAQGLT 187
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 3-232 4.56e-20

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 86.60  E-value: 4.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYItgrhLDtLRVVAQEAQSLggqcVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVN----AD-IHGGDGQHENY----QFVPTDVSSAEEVNHTVAEI-IEKFG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNAYAGVQTIL--NTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS----PGSL-QY 155
Cdd:PRK06171  77 RIDGLVNNAGINIPRLLvdEKDPAGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSeaglEGSEgQS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       156 MfnvpYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEhMAKEEVL---QDPVLKQFKSAFSSAETTEL--S 230
Cdd:PRK06171 157 C----YAATKAALNSFTRSWAKELGKHNIRVVGVAPGILEATGLRT-PEYEEALaytRGITVEQLRAGYTKTSTIPLgrS 231


                 ..
2QQ5_A       231 GK 232
Cdd:PRK06171 232 GK 233
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 9-201 5.13e-20

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: 85.81  E-value: 5.13e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        9 VVTGASRGIGRGIALQLCKAG-ATVYITGRHLDTlrvvAQEAQSLGGQCVPVVC---DSSqeSEVRSLFEQV-DREQQGR 83
Cdd:cd05325   2 LITGASRGIGLELVRQLLARGnNTVIATCRDPSA----ATELAALGASHSRLHIlelDVT--DEIAESAEAVaERLGDAG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       84 LDVLVNNAyaGVQTILNTRNkafwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSP-GSLQYMF---NV 159
Cdd:cd05325  76 LDVLINNA--GILHSYGPAS----EVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRvGSIGDNTsggWY 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
2QQ5_A      160 PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKE 201
Cdd:cd05325 150 SYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGP 191
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 7-184 8.40e-20

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: 85.13  E-value: 8.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        7 VCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVA-QEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRLD 85
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLvDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEE-IGPLE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       86 VLVNNAYAGVQ-TILntrnkafwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFN-VPYGV 163
Cdd:cd05373  80 VLVYNAGANVWfPIL--------ETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGfAAFAG 151

                       170       180
                ....*....|....*....|.
2QQ5_A      164 GKAACDKLAADCAHELRRHGV 184
Cdd:cd05373 152 AKFALRALAQSMARELGPKGI 172
PRK05855 PRK05855
SDR family oxidoreductase;
2-196 1.03e-19

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 88.11  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQ 81
Cdd:PRK05855 312 PFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWV-RAEH 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        82 GRLDVLVNNA---YAGvqtilntrnkAFWETPASMWDDINNVGLRGhyfcSVYGARL----MVPAGQ-GLIVVISSPGSL 153
Cdd:PRK05855 391 GVPDIVVNNAgigMAG----------GFLDTSAEDWDRVLDVNLWG----VIHGCRLfgrqMVERGTgGHIVNVASAAAY 456

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
2QQ5_A       154 QYMFNVP-YGVGKAACDKLaADCAH-ELRRHGVSCVSLWPGIVQT 196
Cdd:PRK05855 457 APSRSLPaYATSKAAVLML-SECLRaELAAAGIGVTAICPGFVDT 500
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 5-192 1.06e-19

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 85.38  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHlDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:PRK12823   8 GKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRS-ELVHEVAAELRAAGGEALALTADLETYAGAQAAMAAA-VEAFGRI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNAyAGvqTIlntRNKAFWE-TPASMWDDInnvglRGHYFCSVYGAR----LMVPAGQGLIVVISSPGSlQYMFNV 159
Cdd:PRK12823  86 DVLINNV-GG--TI---WAKPFEEyEEEQIEAEI-----RRSLFPTLWCCRavlpHMLAQGGGAIVNVSSIAT-RGINRV 153

                        170       180       190
                 ....*....|....*....|....*....|...
2QQ5_A       160 PYGVGKAACDKLAADCAHELRRHGVSCVSLWPG 192
Cdd:PRK12823 154 PYSAAKGGVNALTASLAFEYAEHGIRVNAVAPG 186
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 1-210 1.23e-19

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 85.16  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         1 APMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRH----LDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEqV 76
Cdd:PRK12827   2 ASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHpmrgRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALD-A 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        77 DREQQGRLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHY-FCSVYGARLMVPAGQGLIVVISS-PGSLQ 154
Cdd:PRK12827  81 GVEEFGRLDILVNN--AGI-----ATDAAFAELSIEEWDDVIDVNLDGFFnVTQAALPPMIRARRGGRIVNIASvAGVRG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
2QQ5_A       155 YMFNVPYGVGKAACDKLAADCAHELRRHG--VSCVSlwPGIVQTELLKEHMAKEEVLQ 210
Cdd:PRK12827 154 NRGQVNYAASKAGLIGLTKTLANELAPRGitVNAVA--PGAINTPMADNAAPTEHLLN 209
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 7-251 1.49e-19

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: 84.65  E-value: 1.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        7 VCVVTGASRGIGRGIALQLCKAGAT--VYITGRHLDTLRVVAQEAQSlGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPsvVVLLARSEEPLQELKEELRP-GLRVTTVKADLSDAAGVEQLLEAI-RKLDGER 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       85 DVLVNNayAGVqtiLNTRNKAFwetPASMwDDINNvglrgHYFCSVYGARLMVPA---------GQGLIVVISSPGSLQY 155
Cdd:cd05367  79 DLLINN--AGS---LGPVSKIE---FIDL-DELQK-----YFDLNLTSPVCLTSTllrafkkrgLKKTVVNVSSGAAVNP 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      156 MFN-VPYGVGKAACDKLAADCAHELRrhGVSCVSLWPGIVQTELLKEhmAKEEVLQDPVLKQFKSAFSSAE--TTELSGK 232
Cdd:cd05367 145 FKGwGLYCSSKAARDMFFRVLAAEEP--DVRVLSYAPGVVDTDMQRE--IRETSADPETRSRFRSLKEKGEllDPEQSAE 220

                       250
                ....*....|....*....
2QQ5_A      233 CVVALAtdPNILSLSGKVL 251
Cdd:cd05367 221 KLANLL--EKDKFESGAHV 237
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-198 1.61e-19

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 85.01  E-value: 1.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         6 QVCVVTGASRGIGRGIALQLCKAGATVYITG-RHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDrPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAA-QAAWGRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNayAGVQTIlnTRNKAFWETPASmWDDINNVGLRGHYFCSVYGARLMV------PAGQGLIVVISSPGSLQYMFN 158
Cdd:PRK12745  82 DCLVNN--AGVGVK--VRGDLLDLTPES-FDRVLAINLRGPFFLTQAVAKRMLaqpepeELPHRSIVFVSSVNAIMVSPN 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
2QQ5_A       159 -VPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK12745 157 rGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDM 197
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 7-255 1.65e-19

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


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 84.66  E-value: 1.65e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        7 VCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDV 86
Cdd:cd05323   2 VAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKA-IEKFGRVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       87 LVNNAyagvqTILNTRNKAFWETPASMWDDINNVGLRGhyfcSVYGARLMVPA-------GQGLIVVISSPGSLQYMFNV 159
Cdd:cd05323  81 LINNA-----GILDEKSYLFAGKLPPPWEKTIDVNLTG----VINTTYLALHYmdknkggKGGVIVNIGSVAGLYPAPQF 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      160 P-YGVGKAACDKLAADCAHEL-RRHGVSCVSLWPGIVQTELLKEHMAKEEVLQDPVLKQfksafssaeTTELSGKCVVAL 237
Cdd:cd05323 152 PvYSASKHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLLPDLVAKEAEMLPSAPTQ---------SPEVVAKAIVYL 222

                       250
                ....*....|....*...
2QQ5_A      238 ATDPnilSLSGKVLPSCD 255
Cdd:cd05323 223 IEDD---EKNGAIWIVDG 237
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 5-203 1.76e-19

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 84.70  E-value: 1.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQG 82
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEinAEYGEGMAYGFGADATSEQSVLALSRGVD-EIFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAG-QGLIVVISS-PGSLQYMFNVP 160
Cdd:PRK12384  81 RVDLLVYN--AGI-----AKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINSkSGKVGSKHNSG 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
2QQ5_A       161 YGVGKAACDKLAADCAHELRRHGVSCVSLWPGivqtELLKEHM 203
Cdd:PRK12384 154 YSAAKFGGVGLTQSLALDLAEYGITVHSLMLG----NLLKSPM 192
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 5-228 2.02e-19

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: 84.23  E-value: 2.02e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQE----AQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQ 80
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEieaeANASGQKVSYISADLSDYEEVEQAFAQAV-EK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       81 QGRLDVLVNNAYAGVQtilntrnKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFN-V 159
Cdd:cd08939  80 GGPPDLVVNCAGISIP-------GLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGyS 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2QQ5_A      160 PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEllkehMAKEEVLQDPVLKQFKSAFSSAETTE 228
Cdd:cd08939 153 AYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTP-----GFEEENKTKPEETKAIEGSSGPITPE 216
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-184 2.52e-19

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 85.22  E-value: 2.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVyITGRHLDTLRV--VAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDre 79
Cdd:PRK07792   9 DLSGKVAVVTGAAAGLGRAEALGLARLGATV-VVNDVASALDAsdVLDEIRAAGAKAVAVAGDISQRATADELVATAV-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        80 QQGRLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHY----FCSVY-GARLMVPAGQ--GLIVVISSPGS 152
Cdd:PRK07792  86 GLGGLDIVVNN--AGI-----TRDRMLFNMSDEEWDAVIAVHLRGHFlltrNAAAYwRAKAKAAGGPvyGRIVNTSSEAG 158

                        170       180       190
                 ....*....|....*....|....*....|...
2QQ5_A       153 LQYMFNVP-YGVGKAACDKLAADCAHELRRHGV 184
Cdd:PRK07792 159 LVGPVGQAnYGAAKAGITALTLSAARALGRYGV 191
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 9-200 3.04e-19

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 84.04  E-value: 3.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         9 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRLDVLV 88
Cdd:PRK08085  13 LITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKD-IGPIDVLI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        89 NNayAGVQtilntRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVIsspGSLQYMFN----VPYGVG 164
Cdd:PRK08085  92 NN--AGIQ-----RRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINI---CSMQSELGrdtiTPYAAS 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
2QQ5_A       165 KAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLK 200
Cdd:PRK08085 162 KGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTK 197
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-197 4.46e-19

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 83.63  E-value: 4.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITgRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIIT-THGTNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEA-LEEFG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNAyagvQTIlnTRNKAFwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQ-YMFNVPY 161
Cdd:PRK06935  91 KIDILVNNA----GTI--RRAPLL-EYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQgGKFVPAY 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
2QQ5_A       162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTE 197
Cdd:PRK06935 164 TASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTA 199
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 5-218 4.76e-19

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: 83.33  E-value: 4.76e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCV-PVVCDSSQESEVRSLFEQVdREQQGR 83
Cdd:cd05343   6 GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLfPYQCDLSNEEQILSMFSAI-RTQHQG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       84 LDVLVNNAYAGvqtilntRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLM--VPAGQGLIVVISS-------PGSLQ 154
Cdd:cd05343  85 VDVCINNAGLA-------RPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMkeRNVDDGHIININSmsghrvpPVSVF 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
2QQ5_A      155 YMFNVPYGVGKAACDKLAADCaHELRRH-GVSCVSlwPGIVQTELLKEHMAKEEVLQDPVLKQFK 218
Cdd:cd05343 158 HFYAATKHAVTALTEGLRQEL-REAKTHiRATSIS--PGLVETEFAFKLHDNDPEKAAATYESIP 219
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 3-96 5.14e-19

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: 83.29  E-value: 5.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGqcvpVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:COG3967   3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPGLHT----IVLDVADPASIAALAEQV-TAEFP 77

                        90
                ....*....|....
2QQ5_A       83 RLDVLVNNayAGVQ 96
Cdd:COG3967  78 DLNVLINN--AGIM 89
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 6-196 9.35e-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: 82.43  E-value: 9.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        6 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLfEQVDREQQGRLD 85
Cdd:cd05360   1 QVVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERA-ADTAVERFGRID 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       86 VLVNNayAGVQTIlntrnKAFWETPASMWDDINNVGLRGHyfcsVYGARLMVP----AGQGLIVVISSPGSLQYM-FNVP 160
Cdd:cd05360  80 TWVNN--AGVAVF-----GRFEDVTPEEFRRVFDVNYLGH----VYGTLAALPhlrrRGGGALINVGSLLGYRSApLQAA 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
2QQ5_A      161 YGVGKAAC----DKLAADCAHELRrhGVSCVSLWPGIVQT 196
Cdd:cd05360 149 YSASKHAVrgftESLRAELAHDGA--PISVTLVQPTAMNT 186
PRK07201 PRK07201
SDR family oxidoreductase;
2-91 1.58e-18

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 84.62  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQ 81
Cdd:PRK07201 368 PLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAE-H 446

                         90
                 ....*....|
2QQ5_A        82 GRLDVLVNNA 91
Cdd:PRK07201 447 GHVDYLVNNA 456
PRK06484 PRK06484
short chain dehydrogenase; Validated
 5-201 1.64e-18

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 84.52  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRvvaQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDReQQGRL 84
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERAR---ERADSLGPDHHALAMDVSDEAQIREGFEQLHR-EFGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNAyagvqTILNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQG--LIVVISSPGSLQYMFNVPYG 162
Cdd:PRK06484  81 DVLVNNA-----GVTDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGaaIVNVASGAGLVALPKRTAYS 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
2QQ5_A       163 VGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKE 201
Cdd:PRK06484 156 ASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAE 194
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 2-198 2.02e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 82.30  E-value: 2.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAqslgGQCVPVVCDSSQESEVRSLFEQVDReQQ 81
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAEL----GLVVGGPLDVTDPASFAAFLDAVEA-DL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        82 GRLDVLVNNayAGVQTIlntrnKAFWETPASMWDDINNVGLRGhyfcSVYGARL----MVPAGQGLIVVISSPGSlqyMF 157
Cdd:PRK07825  77 GPIDVLVNN--AGVMPV-----GPFLDEPDAVTRRILDVNVYG----VILGSKLaaprMVPRGRGHVVNVASLAG---KI 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
2QQ5_A       158 NVP----YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK07825 143 PVPgmatYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTEL 187
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 2-216 2.09e-18

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: 81.81  E-value: 2.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHlDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQ 81
Cdd:cd08937   1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRS-ELVHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAA-VERF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       82 GRLDVLVNNAYAGVQTilntrnKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPgSLQYMFNVPY 161
Cdd:cd08937  79 GRVDVLINNVGGTIWA------KPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSI-ATRGIYRIPY 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
2QQ5_A      162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLK-EHMAKEEVLQDPVLKQ 216
Cdd:cd08937 152 SAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKiPRNAAPMSEQEKVWYQ 207
PRK09730 PRK09730
SDR family oxidoreductase;
7-198 2.13e-18

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 81.82  E-value: 2.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         7 VCVVTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDReQQGRLD 85
Cdd:PRK09730   3 IALVTGGSRGIGRATALLLAQEGYTVAVNYQQnLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQ-HDEPLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        86 VLVNNAyagvqTILNTRNKAFWETPASmwddINNV---GLRGHYFCSVYGARLMV--PAGQ-GLIVVISS-------PGs 152
Cdd:PRK09730  82 ALVNNA-----GILFTQCTVENLTAER----INRVlstNVTGYFLCCREAVKRMAlkHGGSgGAIVNVSSaasrlgaPG- 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
2QQ5_A       153 lQYmfnVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK09730 152 -EY---VDYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEM 193
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 5-206 2.66e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 81.70  E-value: 2.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLGGQCVPVvcDSSQESEVRSLFEQVDrEQQGRL 84
Cdd:PRK06057   7 GRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADE---VGGLFVPT--DVTDEDAVNALFDTAA-ETYGSV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNayAGVQ-----TILNTRNKAfwetpasmWDDINNVGLRGHYFCSVYGARLMVPAGQGLIV-------VISSPGS 152
Cdd:PRK06057  81 DIAFNN--AGISppeddSILNTGLDA--------WQRVQDVNLTSVYLCCKAALPHMVRQGKGSIIntasfvaVMGSATS 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
2QQ5_A       153 lqymfNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKE 206
Cdd:PRK06057 151 -----QISYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELFAKD 199
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 10-198 3.24e-18

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: 80.84  E-value: 3.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       10 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRLDVLVN 89
Cdd:cd05350   3 ITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAE-LGGLDLVII 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       90 NayAGVQTILNTRNKAFWETPASMwdDINNVGlrghyfcSVYGARLMVPA----GQGLIVVISSPGSLQYMFNVP-YGVG 164
Cdd:cd05350  82 N--AGVGKGTSLGDLSFKAFRETI--DTNLLG-------AAAILEAALPQfrakGRGHLVLISSVAALRGLPGAAaYSAS 150

                       170       180       190
                ....*....|....*....|....*....|....
2QQ5_A      165 KAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:cd05350 151 KAALSSLAESLRYDVKKRGIRVTVINPGFIDTPL 184
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 5-240 3.27e-18

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: 80.98  E-value: 3.27e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLrvvaQEAQSLGGqCVPVVCDSSQESEVRSLFEQVDreqqgRL 84
Cdd:cd05368   2 GKVALITAAAQGIGRAIALAFAREGANVIATDINEEKL----KELERGPG-ITTRVLDVTDKEQVAALAKEEG-----RI 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       85 DVLVNNA-YAGVQTILNTRNKAfwetpasmWDDINNVGLRGHYFcsVYGARL--MVPAGQGLIVVISSPGSlqYMFNVP- 160
Cdd:cd05368  72 DVLFNCAgFVHHGSILDCEDDD--------WDFAMNLNVRSMYL--MIKAVLpkMLARKDGSIINMSSVAS--SIKGVPn 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      161 ---YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAK----EEVLQDPVLKQFKSAFSSAEttELSGKC 233
Cdd:cd05368 140 rfvYSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERIQAqpdpEEALKAFAARQPLGRLATPE--EVAALA 217


                ....*..
2QQ5_A      234 VVaLATD 240
Cdd:cd05368 218 VY-LASD 223
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 4-192 3.36e-18

(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: 81.21  E-value: 3.36e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        4 NGQVCVVTGASRGIGRGIALQLCKAGATVYI---------TGRHLDTLRVVAQEAQSLGGQCVPvvcDSSQESEVRSLFE 74
Cdd:cd05353   4 DGRVVLVTGAGGGLGRAYALAFAERGAKVVVndlggdrkgSGKSSSAADKVVDEIKAAGGKAVA---NYDSVEDGEKIVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       75 QVdREQQGRLDVLVNNAyagvqTILntRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQ 154
Cdd:cd05353  81 TA-IDAFGRVDILVNNA-----GIL--RDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLY 152

                       170       180       190
                ....*....|....*....|....*....|....*....
2QQ5_A      155 YMF-NVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPG 192
Cdd:cd05353 153 GNFgQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
PRK07832 PRK07832
SDR family oxidoreductase;
8-200 3.99e-18

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 81.24  E-value: 3.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         8 CVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQcVP--VVCDSSQESEVRSLFEQVDREqQGRLD 85
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGT-VPehRALDISDYDAVAAFAADIHAA-HGSMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        86 VLVNNayAGVqtilntrnkAFWETPASM----WDDINNVGLRGhyfcSVYGARLMVP----AGQG--LIVVISSPGSLQY 155
Cdd:PRK07832  81 VVMNI--AGI---------SAWGTVDRLtheqWRRMVDVNLMG----PIHVIETFVPpmvaAGRGghLVNVSSAAGLVAL 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
2QQ5_A       156 MFNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLK 200
Cdd:PRK07832 146 PWHAAYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVN 190
PRK06484 PRK06484
short chain dehydrogenase; Validated
 5-196 4.74e-18

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 82.97  E-value: 4.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVaqeAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:PRK06484 269 PRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKL---AEALGDEHLSVQADITDEAAVESAFAQI-QARWGRL 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNAYAGVQTILNTRnkafwETPASMwDDINNVGLRGHYFCSVYGARLMvpAGQGLIVVISS-PGSLQYMFNVPYGV 163
Cdd:PRK06484 345 DVLVNNAGIAEVFKPSLE-----QSAEDF-TRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSiASLLALPPRNAYCA 416

                        170       180       190
                 ....*....|....*....|....*....|...
2QQ5_A       164 GKAACDKLAADCAHELRRHGVSCVSLWPGIVQT 196
Cdd:PRK06484 417 SKAAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449
PRK06123 PRK06123
SDR family oxidoreductase;
6-198 5.07e-18

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 80.59  E-value: 5.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         6 QVCVVTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRL 84
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERGYAVCLNYLRnRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRE-LGRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNAyagvqTILNTRNKaFWETPASMWDDINNVGLRGHYFCSVYGARLMVP--AGQ-GLIVVISS-------PGslQ 154
Cdd:PRK06123  82 DALVNNA-----GILEAQMR-LEQMDAARLTRIFATNVVGSFLCAREAVKRMSTrhGGRgGAIVNVSSmaarlgsPG--E 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
2QQ5_A       155 YmfnVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK06123 154 Y---IDYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEI 194
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 3-203 7.04e-18

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 80.23  E-value: 7.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLD----TLRVVAQEAQSLGGqcvpvvCDSSQESEVRSLFEQVDR 78
Cdd:PRK12828   5 LQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAplsqTLPGVPADALRIGG------IDLVDPQAARRAVDEVNR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        79 eQQGRLDVLVNNAYAGV-QTIlntrnkafWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS-PGSLQYM 156
Cdd:PRK12828  79 -QFGRLDALVNIAGAFVwGTI--------ADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAgAALKAGP 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
2QQ5_A       157 FNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHM 203
Cdd:PRK12828 150 GMGAYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNRADM 196
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 3-242 7.36e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 80.72  E-value: 7.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLdtlrvvaQEAQSLGGqcVP-VVCDSSQESEVRSLFEQVdREQQ 81
Cdd:PRK06179   2 SNSKVALVTGASSGIGRATAEKLARAGYRVFGTSRNP-------ARAAPIPG--VElLELDVTDDASVQAAVDEV-IARA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        82 GRLDVLVNNAYAGV------------QTILNTrnkafwetpasmwddinNVglrghyFCSVYGARLMVP----AGQGLIV 145
Cdd:PRK06179  72 GRIDVLVNNAGVGLagaaeessiaqaQALFDT-----------------NV------FGILRMTRAVLPhmraQGSGRII 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       146 VISSP-GSLQYMFNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL----------LKEHMAKEEVLQDPVL 214
Cdd:PRK06179 129 NISSVlGFLPAPYMALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNFdanapepdspLAEYDRERAVVSKAVA 208

                        250       260
                 ....*....|....*....|....*...
2QQ5_A       215 KQFKsafsSAETTELSGKCVVALATDPN 242
Cdd:PRK06179 209 KAVK----KADAPEVVADTVVKAALGPW 232
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 5-256 9.95e-18

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: 80.20  E-value: 9.95e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQg 82
Cdd:cd09807   1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEirRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEED- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       83 RLDVLVNNayAGVQTILNTRNKAFWETPASmwddINNVglrGHYFCSVYGARLMVPAGQGLIVVISS----PGSLQY--- 155
Cdd:cd09807  80 RLDVLINN--AGVMRCPYSKTEDGFEMQFG----VNHL---GHFLLTNLLLDLLKKSAPSRIVNVSSlahkAGKINFddl 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      156 MFNVPYGVGKAAC-DKLA-----ADCAHELRRHGVSCVSLWPGIVQTELLKeHMAKEEVLQDPVLKQ-----FKSAFSSA 224
Cdd:cd09807 151 NSEKSYNTGFAYCqSKLAnvlftRELARRLQGTGVTVNALHPGVVRTELGR-HTGIHHLFLSTLLNPlfwpfVKTPREGA 229

                       250       260       270
                ....*....|....*....|....*....|..
2QQ5_A      225 ETTelsgkcvVALATDPNILSLSGKVLPSCDL 256
Cdd:cd09807 230 QTS-------IYLALAEELEGVSGKYFSDCKL 254
PRK06949 PRK06949
SDR family oxidoreductase;
3-207 1.08e-17

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 79.81  E-value: 1.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQG 82
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETE-AG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNayAGVqtilNTRNKAFWETPASmWDDINNVGLRGHYFCSVYGARLMV--------PAGQGLIVVISSPGSLQ 154
Cdd:PRK06949  86 TIDILVNN--SGV----STTQKLVDVTPAD-FDFVFDTNTRGAFFVAQEVAKRMIarakgagnTKPGGRIINIASVAGLR 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
2QQ5_A       155 YMFNV-PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEE 207
Cdd:PRK06949 159 VLPQIgLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWETEQ 212
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 3-240 1.14e-17

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 79.66  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQ 81
Cdd:PRK12935   4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVINyNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEA-VNHF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        82 GRLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS-PGSLQYMFNVP 160
Cdd:PRK12935  83 GKVDILVNN--AGI-----TRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSiIGQAGGFGQTN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       161 YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEhmAKEEVLQDPVLKQFKSAFSSAETTelsGKCVVALATD 240
Cdd:PRK12935 156 YSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAE--VPEEVRQKIVAKIPKKRFGQADEI---AKGVVYLCRD 230
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 5-200 1.25e-17

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: 79.18  E-value: 1.25e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQE-AQSLGGQCVPVVCDSSQESEVrslFEQVDREQQGr 83
Cdd:cd05356   1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEiEEKYGVETKTIAADFSAGDDI---YERIEKELEG- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       84 LDV--LVNNayAGvqtILNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS-PGSLQYMFNVP 160
Cdd:cd05356  77 LDIgiLVNN--VG---ISHSIPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSfAGLIPTPLLAT 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
2QQ5_A      161 YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLK 200
Cdd:cd05356 152 YSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSK 191
PRK06947 PRK06947
SDR family oxidoreductase;
6-198 1.29e-17

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 79.46  E-value: 1.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         6 QVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQqGRL 84
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVGINyARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAF-GRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNAyaGVqtILNTRNKAfwETPASMWDDINNVGLRGHYFCSVYGARLMVPA---GQGLIVVISSPGSL-----QYm 156
Cdd:PRK06947  82 DALVNNA--GI--VAPSMPLA--DMDAARLRRMFDTNVLGAYLCAREAARRLSTDrggRGGAIVNVSSIASRlgspnEY- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
2QQ5_A       157 fnVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK06947 155 --VDYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 7-215 1.71e-17

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 79.21  E-value: 1.71e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        7 VCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDV 86
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKI-KKEVGDVTI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       87 LVNNayAGVQTilntrNKAFWETPASMWDDINNVGLRGHYFcsVYGARL--MVPAGQGLIVVISSPGSLQY-MFNVPYGV 163
Cdd:cd05339  80 LINN--AGVVS-----GKKLLELPDEEIEKTFEVNTLAHFW--TTKAFLpdMLERNHGHIVTIASVAGLISpAGLADYCA 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
2QQ5_A      164 GKAACDKLAADCAHELRRHG-----VSCVSlwPGIVQTELLkEHMAKEEVLQDPVLK 215
Cdd:cd05339 151 SKAAAVGFHESLRLELKAYGkpgikTTLVC--PYFINTGMF-QGVKTPRPLLAPILE 204
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 3-223 1.83e-17

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 79.35  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYI-TGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQ 81
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIhYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNELQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        82 GR-----LDVLVNNAYAGVQTILNtrnkafwETPASMWDDINNVGLRGHYFcsVYGARLMVPAGQGLIVVISSPGSLQYM 156
Cdd:PRK12747  82 NRtgstkFDILINNAGIGPGAFIE-------ETTEQFFDRMVSVNAKAPFF--IIQQALSRLRDNSRIINISSAATRISL 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
2QQ5_A       157 FN-VPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELlkehmaKEEVLQDPVLKQFKSAFSS 223
Cdd:PRK12747 153 PDfIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDM------NAELLSDPMMKQYATTISA 214
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 5-201 1.99e-17

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: 79.12  E-value: 1.99e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLG-GQCVPVVCDSSQESEVRSLFEqVDREQQGR 83
Cdd:cd08933   9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGpGSCKFVPCDVTKEEDIKTLIS-VTVERFGR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       84 LDVLVNNA--YAGVQTILntrnkafwETPASMWDDINNVGLRGHYFCSVYgARLMVPAGQGLIVVISS-PGSLQYMFNVP 160
Cdd:cd08933  88 IDCLVNNAgwHPPHQTTD--------ETSAQEFRDLLNLNLISYFLASKY-ALPHLRKSQGNIINLSSlVGSIGQKQAAP 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
2QQ5_A      161 YGVGKAACDKLAADCAHELRRHG--VSCVSlwPGIVQTELLKE 201
Cdd:cd08933 159 YVATKGAITAMTKALAVDESRYGvrVNCIS--PGNIWTPLWEE 199
PRK06398 PRK06398
aldose dehydrogenase; Validated
 3-212 2.52e-17

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 78.72  E-value: 2.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQeaqslggqcvpVVCDSSQESEVRSLFEQVDReQQG 82
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYNDVDY-----------FKVDVSNKEQVIKGIDYVIS-KYG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNAyaGVQTIlntrnKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNV-PY 161
Cdd:PRK06398  72 RIDILVNNA--GIESY-----GAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAaAY 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
2QQ5_A       162 GVGKAA----CDKLAADCAHELRrhgvsCVSLWPGIVQTELLkEHMAKEEVLQDP 212
Cdd:PRK06398 145 VTSKHAvlglTRSIAVDYAPTIR-----CVAVCPGSIRTPLL-EWAAELEVGKDP 193
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 4-197 2.75e-17

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 79.17  E-value: 2.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         4 NGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGR 83
Cdd:PRK08277   9 KGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQI-LEDFGP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        84 LDVLVNNA--------YAGVQTILNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQY 155
Cdd:PRK08277  88 CDILINGAggnhpkatTDNEFHELIEPTKTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAFTP 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
2QQ5_A       156 MFNVP-YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTE 197
Cdd:PRK08277 168 LTKVPaYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE 210
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 3-207 2.78e-17

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: 78.12  E-value: 2.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLrvvaQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQg 82
Cdd:cd05370   3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERL----AEAKKELPNIHTIVLDVGDAESVEALAEALLSEYP- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       83 RLDVLVNNayAGVQTILNTRNKAfwETPASMWDDInNVGLRGhyfcSVYGARLMVP----AGQGLIVVISSPGSLQYMFN 158
Cdd:cd05370  78 NLDILINN--AGIQRPIDLRDPA--SDLDKADTEI-DTNLIG----PIRLIKAFLPhlkkQPEATIVNVSSGLAFVPMAA 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
2QQ5_A      159 VP-YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEE 207
Cdd:cd05370 149 NPvYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDG 198
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 3-223 2.80e-17

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: 78.22  E-value: 2.80e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGAT-VYITGRHLDTLRVVAQEAQSlggQCVPVVCDSSQESEVRSLFEQVDreqq 81
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAKkVYAAVRDPGSAAHLVAKYGD---KVVPLRLDVTDPESIKAAAAQAK---- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       82 gRLDVLVNNayAGVQTILNTRNKAFWETpASMWDDINNVGLRGhyFCSVYgARLMVPAGQGLIVVISSPGSLQymfNVP- 160
Cdd:cd05354  74 -DVDVVINN--AGVLKPATLLEEGALEA-LKQEMDVNVFGLLR--LAQAF-APVLKANGGGAIVNLNSVASLK---NFPa 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      161 ---YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLK---------EHMAK----------EEVLQDPVLKQFK 218
Cdd:cd05354 144 mgtYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAgaggpkespETVAEavlkalkageFHVFPDEMAKQVK 223


                ....*
2QQ5_A      219 SAFSS 223
Cdd:cd05354 224 EAYQS 228
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
6-210 3.02e-17

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 78.27  E-value: 3.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         6 QVCVVTGASRGIGRGIALQLCKAGATVYITGRhldTLRVVAQEAQSLGG----QCVPVVCDSSQESEVRSLFEQVDrEQQ 81
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYF---SGNDCAKDWFEEYGftedQVRLKELDVTDTEECAEALAEIE-EEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        82 GRLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLrghyfCSVYG-ARLMVPA----GQGLIVVISSPGSLQYM 156
Cdd:PRK12824  79 GPVDILVNN--AGI-----TRDSVFKRMSHQEWNDVINTNL-----NSVFNvTQPLFAAmceqGYGRIINISSVNGLKGQ 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
2QQ5_A       157 FNVP-YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEhmAKEEVLQ 210
Cdd:PRK12824 147 FGQTnYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVEQ--MGPEVLQ 199
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
3-212 3.39e-17

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 78.69  E-value: 3.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRvVAQEAQSLGGQCVPVVCDSSQESEVRSLFEqVDREQQG 82
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANLILLDISPEIEK-LADELCGRGHRCTAVVADVRDPASVAAAIK-RAKEKEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS--------PGSlq 154
Cdd:PRK08226  82 RIDILVNN--AGV-----CRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSvtgdmvadPGE-- 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
2QQ5_A       155 ymfnVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLkEHMAKEEVLQDP 212
Cdd:PRK08226 153 ----TAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMA-ESIARQSNPEDP 205
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 3-210 3.59e-17

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


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 78.35  E-value: 3.59e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:cd08945   1 QDSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAA-VARYG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       83 RLDVLVNNAYagvqtilNTRNKAFWETPASMWDDINNVGLRGHYFCS--VYGARLMVPAGQGLIVVISSPGSLQ-YMFNV 159
Cdd:cd08945  80 PIDVLVNNAG-------RSGGGATAELADELWLDVVETNLTGVFRVTkeVLKAGGMLERGTGRIINIASTGGKQgVVHAA 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      160 PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL---LKEHMA------KEEVLQ 210
Cdd:cd08945 153 PYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMaasVREHYAdiwevsTEEAFD 212
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 9-211 3.69e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 78.69  E-value: 3.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         9 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDV 86
Cdd:PRK05875  11 LVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEieALKGAGAVRYEPADVTDEDQVARAVDAA-TAWHGRLHG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        87 LVNNAyAGVQTIlntrnKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS-PGSLQYMFNVPYGVGK 165
Cdd:PRK05875  90 VVHCA-GGSETI-----GPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSiAASNTHRWFGAYGVTK 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
2QQ5_A       166 AACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVLQD 211
Cdd:PRK05875 164 SAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITESPELSAD 209
PRK07063 PRK07063
SDR family oxidoreductase;
5-198 7.06e-17

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 77.78  E-value: 7.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQG 82
Cdd:PRK07063   7 GKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAiaRDVAGARVLAVPADVTDAASVAAAVAAAEEA-FG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNAYAGVqtilntrnkafWETPASM----WDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS-------PG 151
Cdd:PRK07063  86 PLDVLVNNAGINV-----------FADPLAMtdedWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASthafkiiPG 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
2QQ5_A       152 SLqymfnvPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK07063 155 CF------PYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQL 195
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-197 8.95e-17

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 77.25  E-value: 8.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATvyITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGAD--IVGVGVAEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQA-VEVMG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNayAGV---QTILNTRNKAfwetpasmWDDINNVGLRGHYFCSVYGARLMVPAGQ-GLIVVISSPGSLQYMFN 158
Cdd:PRK12481  83 HIDILINN--AGIirrQDLLEFGNKD--------WDDVININQKTVFFLSQAVAKQFVKQGNgGKIINIASMLSFQGGIR 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
2QQ5_A       159 VP-YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTE 197
Cdd:PRK12481 153 VPsYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATD 192
PLN02253 PLN02253
xanthoxin dehydrogenase
 5-225 9.05e-17

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 77.56  E-value: 9.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYItgrhLDTLRVVAQE-AQSLGGQ--CVPVVCDSSQESEVRslfEQVD--RE 79
Cdd:PLN02253  18 GKVALVTGGATGIGESIVRLFHKHGAKVCI----VDLQDDLGQNvCDSLGGEpnVCFFHCDVTVEDDVS---RAVDftVD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        80 QQGRLDVLVNNAYAGVQTILNTRNKAFwetpaSMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSlqymfnV 159
Cdd:PLN02253  91 KFGTLDIMVNNAGLTGPPCPDIRNVEL-----SEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVAS------A 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2QQ5_A       160 PYGVG-------KAACDKLAADCAHELRRHG--VSCVSlwPGIVQTELLKEHMAKEEVLQDpVLKQFKsAFSSAE 225
Cdd:PLN02253 160 IGGLGphaytgsKHAVLGLTRSVAAELGKHGirVNCVS--PYAVPTALALAHLPEDERTED-ALAGFR-AFAGKN 230
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 9-197 1.10e-16

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: 76.94  E-value: 1.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        9 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQE-AQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQgRLDVL 87
Cdd:cd05346   4 LITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADElGAKFPVKVLPLQLDVSDRESIEAALENLPEEFR-DIDIL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       88 VNNA--YAGVQTIlntrnkafWETPASMWD---DINNVGLrghyfcsVYGARLMVPA----GQGLIVVISS-------PG 151
Cdd:cd05346  83 VNNAglALGLDPA--------QEADLEDWEtmiDTNVKGL-------LNVTRLILPImiarNQGHIINLGSiagrypyAG 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
2QQ5_A      152 SlqymfNVpYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTE 197
Cdd:cd05346 148 G-----NV-YCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETE 187
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 5-207 2.22e-16

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 76.25  E-value: 2.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRL 84
Cdd:PRK07097  10 GKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKE-VGVI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNV-PYGV 163
Cdd:PRK07097  89 DILVNN--AGI-----IKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVsAYAA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
2QQ5_A       164 GKAACDKLAADCAHELRRHGVSCVSLWPGIV---QTELLKEHMAKEE 207
Cdd:PRK07097 162 AKGGLKMLTKNIASEYGEANIQCNGIGPGYIatpQTAPLRELQADGS 208
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
4-201 2.27e-16

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 76.30  E-value: 2.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         4 NGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGR 83
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQV-VDTFGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        84 LDVLVNNAYAGVQTILNTRnkafweTPaSMWDDINNVGLRGhyfcSVYGARLMVPA----GQG--LIVVISSPGSLQYMF 157
Cdd:PRK08643  80 LNVVVNNAGVAPTTPIETI------TE-EQFDKVYNINVGG----VIWGIQAAQEAfkklGHGgkIINATSQAGVVGNPE 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
2QQ5_A       158 NVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKE 201
Cdd:PRK08643 149 LAVYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPMMFD 192
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 2-149 2.27e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 77.27  E-value: 2.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQ 81
Cdd:PRK07109   5 PIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEE-L 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2QQ5_A        82 GRLDVLVNNA----YAGVQTIlntrnkafweTPASM--WDDINnvglrghYFCSVYGA----RLMVPAGQGLIVVISS 149
Cdd:PRK07109  84 GPIDTWVNNAmvtvFGPFEDV----------TPEEFrrVTEVT-------YLGVVHGTlaalRHMRPRDRGAIIQVGS 144
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 3-199 2.94e-16

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 75.69  E-value: 2.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVyiTGrhLDTlrvvaQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQG 82
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKV--IG--FDQ-----AFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAE-TG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSlqymfNVP-- 160
Cdd:PRK08220  76 PLDVLVNA--AGI-----LRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAA-----HVPri 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
2QQ5_A       161 ----YGVGKAACDKLAADCAHELRRHGVSC--VSlwPGIVQTELL 199
Cdd:PRK08220 144 gmaaYGASKAALTSLAKCVGLELAPYGVRCnvVS--PGSTDTDMQ 186
PRK07074 PRK07074
SDR family oxidoreductase;
6-197 4.03e-16

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 75.58  E-value: 4.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         6 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLG-GQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADA---LGdARFVPVACDLTDAASLAAALANA-AAERGPV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNAYAGVQTILNTrnkafweTPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNVPYGVG 164
Cdd:PRK07074  79 DVLVANAGAARAASLHD-------TTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMAALGHPAYSAA 151

                        170       180       190
                 ....*....|....*....|....*....|...
2QQ5_A       165 KAACDKLAADCAHELRRHGVSCVSLWPGIVQTE 197
Cdd:PRK07074 152 KAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQ 184
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 4-192 4.73e-16

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: 75.06  E-value: 4.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        4 NGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGG-QCVPVVCDSSQESEVRSLFEQVDrEQQG 82
Cdd:cd08930   1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKnRVIALELDITSKESIKELIESYL-EKFG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       83 RLDVLVNNAYAGVQtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS------PGSLQY- 155
Cdd:cd08930  80 RIDILINNAYPSPK----VWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASiygviaPDFRIYe 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
2QQ5_A      156 ---MFN-VPYGVGKAACDKLAADCAHELRRHGVSCVSLWPG 192
Cdd:cd08930 156 ntqMYSpVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG 196
PRK08264 PRK08264
SDR family oxidoreductase;
3-224 5.27e-16

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 74.93  E-value: 5.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGAT-VYITGRHLDTlrvvaqeAQSLGGQCVPVVCDSSQESEVRSLFEQVdreqq 81
Cdd:PRK08264   4 IKGKVVLVTGANRGIGRAFVEQLLARGAAkVYAAARDPES-------VTDLGPRVVPLQLDVTDPASVAAAAEAA----- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        82 GRLDVLVNNayAGVQTilntrnkafweTPASMWDDiNNVGLRGHYFCSVYG----ARLMVPA----GQGLIVVISSPGSL 153
Cdd:PRK08264  72 SDVTILVNN--AGIFR-----------TGSLLLEG-DEDALRAEMETNYFGplamARAFAPVlaanGGGAIVNVLSVLSW 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       154 qymFNVP----YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLK---------EHMAK----------EEVLQ 210
Cdd:PRK08264 138 ---VNFPnlgtYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAgldapkaspADVARqildaleagdEEVLP 214

                        250
                 ....*....|....
2QQ5_A       211 DPVLKQFKSAFSSA 224
Cdd:PRK08264 215 DEMARQVKAALSAD 228
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 5-183 9.67e-16

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 76.49  E-value: 9.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQG 82
Cdd:COG3347 425 GRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAElgGGYGADAVDATDVDVTAEAAVAAAFGFAGLDIGG 504

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       83 RLDVLVNNAYAGVqtilntrnKAFWETPASMWDDINNVGLRGHYFCSVYGARLMvpAGQGL---IVVISSPGSLQYmfnv 159
Cdd:COG3347 505 SDIGVANAGIASS--------SPEEETRLSFWLNNFAHLSTGQFLVARAAFQGT--GGQGLggsSVFAVSKNAAAA---- 570

                       170       180
                ....*....|....*....|....
2QQ5_A      160 PYGVGKAACDKLAAdcAHELRRHG 183
Cdd:COG3347 571 AYGAAAAATAKAAA--QHLLRALA 592
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 3-198 1.05e-15

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 74.42  E-value: 1.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSlfeQVDR--EQ 80
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRA---AIDAfeAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        81 QGRLDVLVNNAYAGVQTILNtrnkafwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS-------PGSl 153
Cdd:PRK07523  85 IGPIDILVNNAGMQFRTPLE-------DFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASvqsalarPGI- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
2QQ5_A       154 qymfnVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK07523 157 -----APYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPL 196
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 5-207 1.80e-15

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 73.84  E-value: 1.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:PRK07890   5 GKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALA-LERFGRV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNAYAgVQTIlntrnKAFWETPASMWDDINNVglrghyfcSVYGA----RLMVPA---GQGLIVVISS---PGSlQ 154
Cdd:PRK07890  84 DALVNNAFR-VPSM-----KPLADADFAHWRAVIEL--------NVLGTlrltQAFTPAlaeSGGSIVMINSmvlRHS-Q 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
2QQ5_A       155 YMFNvPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLK---EHMAKEE 207
Cdd:PRK07890 149 PKYG-AYKMAKGALLAASQSLATELGPQGIRVNSVAPGYIWGDPLKgyfRHQAGKY 203
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 5-198 1.83e-15

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: 73.66  E-value: 1.83e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLggqcVPVVCDSSQESEVRSLFEQVdreqqGRL 84
Cdd:cd05351   7 GKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPGI----EPVCVDLSDWDATEEALGSV-----GPV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       85 DVLVNNayAGVQTIlntrnKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAG-QGLIVVISSPGSLQYMFN-VPYG 162
Cdd:cd05351  78 DLLVNN--AAVAIL-----QPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNhTVYC 150

                       170       180       190
                ....*....|....*....|....*....|....*.
2QQ5_A      163 VGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:cd05351 151 STKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDM 186
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 3-191 2.20e-15

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 73.94  E-value: 2.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYI---------TGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLF 73
Cdd:PRK07791   4 LDGRVVIVTGAGGGIGRAHALAFAAEGARVVVndigvgldgSASGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAANLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        74 EQVdREQQGRLDVLVNNAyagvqTILntRNKAFWETPASMWDDINNVGLRGHyFCSVYGA----RLMVPAGQGL---IVV 146
Cdd:PRK07791  84 DAA-VETFGGLDVLVNNA-----GIL--RDRMIANMSEEEWDAVIAVHLKGH-FATLRHAaaywRAESKAGRAVdarIIN 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
2QQ5_A       147 ISSPGSLQYmfNV---PYGVGKAACDKLAADCAHELRRHGVSCVSLWP 191
Cdd:PRK07791 155 TSSGAGLQG--SVgqgNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP 200
PRK05650 PRK05650
SDR family oxidoreductase;
9-199 2.54e-15

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 73.54  E-value: 2.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         9 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSlFEQVDREQQGRLDVLV 88
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTA-LAQACEEKWGGIDVIV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        89 NNayAGVQTilntrNKAFWETPASMWD---DINNVGLrghyfcsVYGARLMVPA----GQGLIVVISSPGSLQ---YMFN 158
Cdd:PRK05650  83 NN--AGVAS-----GGFFEELSLEDWDwqiAINLMGV-------VKGCKAFLPLfkrqKSGRIVNIASMAGLMqgpAMSS 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
2QQ5_A       159 vpYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELL 199
Cdd:PRK05650 149 --YNVAKAGVVALSETLLVELADDEIGVHVVCPSFFQTNLL 187
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-198 2.58e-15

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 73.22  E-value: 2.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHL-----DTLRVVaqeaQSLGGQCVPVVCDSSQESEVRSLFeQVD 77
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRaeemnETLKMV----KENGGEGIGVLADVSTREGCETLA-KAT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        78 REQQGRLDVLVNNAYAGVQTIlntrnkaFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQglIVVISSPGSLQYMF 157
Cdd:PRK06077  79 IDRYGVADILVNNAGLGLFSP-------FLNVDDKLIDKHISTDFKSVIYCSQELAKEMREGGA--IVNIASVAGIRPAY 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
2QQ5_A       158 NVP-YGVGKAACDKLAADCAHELR-RHGVSCVSlwPGIVQTEL 198
Cdd:PRK06077 150 GLSiYGAMKAAVINLTKYLALELApKIRVNAIA--PGFVKTKL 190
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 5-94 2.73e-15

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 73.17  E-value: 2.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQGRL 84
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQID-EKFGRI 79

                         90
                 ....*....|
2QQ5_A        85 DVLVNNAyAG 94
Cdd:PRK07677  80 DALINNA-AG 88
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 3-198 2.91e-15

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: 73.26  E-value: 2.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQG 82
Cdd:cd08935   3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIV-AQFG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       83 RLDVLVN-------NAYAGVQTILNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQY 155
Cdd:cd08935  82 TVDILINgaggnhpDATTDPEHYEPETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSP 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
2QQ5_A      156 MFNVP-YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:cd08935 162 LTKVPaYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQ 205
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 6-197 3.26e-15

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: 72.88  E-value: 3.26e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        6 QVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHLDTLRVVAQEAqslGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARVVVNyYRSTESAEAVAAEA---GERAIAIQADVRDRDQVQAMIEEA-KNHFGPV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       85 DVLVNNAYAGVQTILNTRNKAFWETpasmWDDINN---VGLRGHYFCSVYGARLMVPAGQGLIVVISSpgSLQYMFNVPY 161
Cdd:cd05349  77 DTIVNNALIDFPFDPDQRKTFDTID----WEDYQQqleGAVKGALNLLQAVLPDFKERGSGRVINIGT--NLFQNPVVPY 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
2QQ5_A      162 G---VGKAACDKLAADCAHELRRHG--VSCVSlwPGIVQTE 197
Cdd:cd05349 151 HdytTAKAALLGFTRNMAKELGPYGitVNMVS--GGLLKVT 189
PRK09072 PRK09072
SDR family oxidoreductase;
4-91 3.64e-15

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 73.05  E-value: 3.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         4 NGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaQSLGGQCVPVVCDSSQESEVRSLFEQVdrEQQGR 83
Cdd:PRK09072   4 KDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAAR-LPYPGRHRWVVADLTSEAGREAVLARA--REMGG 80


                 ....*...
2QQ5_A        84 LDVLVNNA 91
Cdd:PRK09072  81 INVLINNA 88
PRK07856 PRK07856
SDR family oxidoreductase;
4-207 5.55e-15

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 72.27  E-value: 5.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         4 NGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHldtlrvVAQEAQSLGGQCVPvvCDSSQESEVRSLFEQVdREQQGR 83
Cdd:PRK07856   5 TGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRR------APETVDGRPAEFHA--ADVRDPDQVAALVDAI-VERHGR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        84 LDVLVNNAYAGVQTILNTRNKAFWETpasmwddINNVGLRGHYFCSVYGARLMVP-AGQGLIVVISS-------PGSlqy 155
Cdd:PRK07856  76 LDVLVNNAGGSPYALAAEASPRFHEK-------IVELNLLAPLLVAQAANAVMQQqPGGGSIVNIGSvsgrrpsPGT--- 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
2QQ5_A       156 mfnVPYGVGKAACDKLAADCAHE----LRrhgVSCVSlwPGIVQTELLKEHMAKEE 207
Cdd:PRK07856 146 ---AAYGAAKAGLLNLTRSLAVEwapkVR---VNAVV--VGLVRTEQSELHYGDAE 193
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 10-218 6.14e-15

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: 72.12  E-value: 6.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       10 VTGASRGIGRGIALQLCKAGATVyiTGRHLDtlrvvAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRLDVLVN 89
Cdd:cd05331   3 VTGAAQGIGRAVARHLLQAGATV--IALDLP-----FVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAE-HGPIDALVN 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       90 naYAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSlqymfNVP------YGV 163
Cdd:cd05331  75 --CAGV-----LRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAA-----HVPrismaaYGA 142

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      164 GKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLK-----EHMAKEEVLQDPvlKQFK 218
Cdd:cd05331 143 SKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAMQRtlwhdEDGAAQVIAGVP--EQFR 200
PRK06182 PRK06182
short chain dehydrogenase; Validated
 3-197 6.40e-15

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 72.30  E-value: 6.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLrvvaQEAQSLGGQCVPVvcDSSQESEVRSLFEQVdREQQG 82
Cdd:PRK06182   1 MQKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKM----EDLASLGVHPLSL--DVTDEASIKAAVDTI-IAEEG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNAYAGVqtilntrnkafwetpasmWDDINNVGL---RGHYFCSVYG-ARL-------MVPAGQGLIVVISSPG 151
Cdd:PRK06182  74 RIDVLVNNAGYGS------------------YGAIEDVPIdeaRRQFEVNLFGaARLtqlvlphMRAQRSGRIINISSMG 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
2QQ5_A       152 SLQY-MFNVPYGVGKAACDKLaADCAH-ELRRHGVSCVSLWPGIVQTE 197
Cdd:PRK06182 136 GKIYtPLGAWYHATKFALEGF-SDALRlEVAPFGIDVVVIEPGGIKTE 182
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-207 1.18e-14

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 71.44  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATvyITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQG 82
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCD--IVGINIVEPTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAE-FG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNAYagvqtiLNTRNKAFwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQ-GLIVVISSPGSLQYMFNVP- 160
Cdd:PRK08993  85 HIDILVNNAG------LIRREDAI-EFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNgGKIINIASMLSFQGGIRVPs 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
2QQ5_A       161 YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEE 207
Cdd:PRK08993 158 YTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQ 204
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 4-200 1.57e-14

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 71.17  E-value: 1.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        4 NGQVCVVTGASRGIGRGIALQLCKAGATVYItgrhLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGR 83
Cdd:cd05371   1 KGLVAVVTGGASGLGLATVERLLAQGAKVVI----LDLPNSPGETVAKLGDNCRFVPVDVTSEKDVKAALALA-KAKFGR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       84 LDVLVNNAYAGV-QTILNTRNKAfwETPASMWDDINNVGLRGHYFCSVYGARLMV-----PAGQ-GLIVVISSPGSLQ-Y 155
Cdd:cd05371  76 LDIVVNCAGIAVaAKTYNKKGQQ--PHSLELFQRVINVNLIGTFNVIRLAAGAMGknepdQGGErGVIINTASVAAFEgQ 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
2QQ5_A      156 MFNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLK 200
Cdd:cd05371 154 IGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLA 198
PRK06500 PRK06500
SDR family oxidoreductase;
10-240 2.29e-14

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 70.37  E-value: 2.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        10 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLrvvaQEAQS-LGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDVLV 88
Cdd:PRK06500  11 ITGGTSGIGLETARQFLAEGARVAITGRDPASL----EAARAeLGESALVIRADAGDVAAQKALAQAL-AEAFGRLDAVF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        89 NNayAGVQTIlntrnKAFWETPASMWDDINNVGLRGHYFcsvygarLMvpagQGLIVVISSP------GSLQYMFNVP-- 160
Cdd:PRK06500  86 IN--AGVAKF-----APLEDWDEAMFDRSFNTNVKGPYF-------LI----QALLPLLANPasivlnGSINAHIGMPns 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       161 --YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELL---------KEHMAKEEVLQDPvLKQFksafssAETTEL 229
Cdd:PRK06500 148 svYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPLYgklglpeatLDAVAAQIQALVP-LGRF------GTPEEI 220

                        250
                 ....*....|.
2QQ5_A       230 SgKCVVALATD 240
Cdd:PRK06500 221 A-KAVLYLASD 230
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 3-211 2.71e-14

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 70.53  E-value: 2.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGR-HLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQ 81
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKE-F 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        82 GRLDVLVNNayAGVQTILNTRnkafwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQ-GLIVVISS-----PGSLqy 155
Cdd:PRK08936  84 GTLDVMINN--AGIENAVPSH-----EMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDIkGNIINMSSvheqiPWPL-- 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
2QQ5_A       156 mFnVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVLQD 211
Cdd:PRK08936 155 -F-VHYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKFADPKQRAD 208
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 3-196 3.29e-14

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: 69.91  E-value: 3.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGG---QCVPVVCDSSQESEVRSLFEQVDRE 79
Cdd:cd05340   2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGrqpQWFILDLLTCTSENCQQLAQRIAVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       80 qQGRLD-VLVNNAYAGVQTILNtrnkafwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFN 158
Cdd:cd05340  82 -YPRLDgVLHNAGLLGDVCPLS-------EQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRAN 153

                       170       180       190
                ....*....|....*....|....*....|....*....
2QQ5_A      159 V-PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQT 196
Cdd:cd05340 154 WgAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRT 192
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 5-201 5.07e-14

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


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 69.66  E-value: 5.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A          5 GQVCVVTGASRGIGRGIALQLCKAGATVYIT---------GRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQ 75
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVdlcaddpavGYPLATRAELDAVAAACPDQVLPVIADVRDPAALAAAVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         76 VdREQQGRLDVLVnnAYAGVqtILNTRnkAFWETPASMWDDINNVGLRGhyfcsVYG-ARLMVPA-------GQGLIVVI 147
Cdd:TIGR04504  81 A-VERWGRLDAAV--AAAGV--IAGGR--PLWETTDAELDLLLDVNLRG-----VWNlARAAVPAmlarpdpRGGRFVAV 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
2QQ5_A        148 SSPGSLQYMFNVP-YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKE 201
Cdd:TIGR04504 149 ASAAATRGLPHLAaYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLAA 203
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 5-201 9.61e-14

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: 68.76  E-value: 9.61e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITgrHLDTLRvVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFA--DIDEER-GADFAEAEGPNLFFVHGDVADETLVKFVVYAM-LEKLGRI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       85 DVLVNNAYAGVQTILNTRnkafwetPASMWDDINNVGLRGHYFCSVYGARLMVpAGQGLIVVISSPGSLQYMFNV-PYGV 163
Cdd:cd09761  77 DVLVNNAARGSKGILSSL-------LLEEWDRILSVNLTGPYELSRYCRDELI-KNKGRIINIASTRAFQSEPDSeAYAA 148

                       170       180       190
                ....*....|....*....|....*....|....*...
2QQ5_A      164 GKAACDKLAADCAHELRRHgVSCVSLWPGIVQTELLKE 201
Cdd:cd09761 149 SKGGLVALTHALAMSLGPD-IRVNCISPGWINTTEQQE 185
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-240 9.67e-14

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 69.04  E-value: 9.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTlrvVAQEAQSLGGQCVPvvCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:PRK06463   7 GKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAEN---EAKELREKGVFTIK--CDVGNRDQVKKSKEVV-EKEFGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNayAGVQTILNTRNkaFWETPASMWDDINnvgLRGHYFCSVYGARLMVPAGQGLIVVISSPGSL-----QYMFnv 159
Cdd:PRK06463  81 DVLVNN--AGIMYLMPFEE--FDEEKYNKMIKIN---LNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgtaaeGTTF-- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       160 pYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVlqdpvlKQFKSAFSSAETTELSGK------C 233
Cdd:PRK06463 152 -YAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQEEA------EKLRELFRNKTVLKTTGKpedianI 224


                 ....*..
2QQ5_A       234 VVALATD 240
Cdd:PRK06463 225 VLFLASD 231
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
3-210 2.15e-13

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 67.74  E-value: 2.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLGGQCVPVVCDSSQESEVRSLFEQVDrEQQG 82
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALE---IGPAAIAVSLDVTRQDSIDRIVAAAV-ERFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNAYA-GVQTILntrnkafwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQG--LIVVISSPGSLQYMFNV 159
Cdd:PRK07067  80 GIDILFNNAALfDMAPIL--------DISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGRGgkIINMASQAGRRGEALVS 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
2QQ5_A       160 PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL---LKEHMAKEEVLQ 210
Cdd:PRK07067 152 HYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMwdqVDALFARYENRP 205
PRK06114 PRK06114
SDR family oxidoreductase;
3-196 3.54e-13

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 67.11  E-value: 3.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDT-LRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQ 81
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDgLAETAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAE-L 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        82 GRLDVLVNNAyagvqTILNTrNKAFwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIV-------VISSPGSLQ 154
Cdd:PRK06114  85 GALTLAVNAA-----GIANA-NPAE-EMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVniasmsgIIVNRGLLQ 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
2QQ5_A       155 YMFNvpygVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQT 196
Cdd:PRK06114 158 AHYN----ASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTAT 195
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 3-197 3.87e-13

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 67.26  E-value: 3.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLGGQCVPVVCDSSQESEV-RSLFEQVDReqQ 81
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAE---IGPAACAISLDVTDQASIdRCVAALVDR--W 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       82 GRLDVLVNNAYA-GVQTILNTRnkafWETpasmWDDINNVGLRGHYFCSVYGARLMVPAGQG--LIVVISSPGSLQYMFN 158
Cdd:cd05363  76 GSIDILVNNAALfDLAPIVDIT----RES----YDRLFAINVSGTLFMMQAVARAMIAQGRGgkIINMASQAGRRGEALV 147

                       170       180       190
                ....*....|....*....|....*....|....*....
2QQ5_A      159 VPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTE 197
Cdd:cd05363 148 GVYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGE 186
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 5-203 4.36e-13

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: 67.10  E-value: 4.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQS-LGGQCVPVVCDSSQESEVRSLFEQVDrEQQGR 83
Cdd:cd05322   2 NQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAeYGEKAYGFGADATNEQSVIALSKGVD-EIFKR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       84 LDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAG-QGLIVVISS-PGSLQYMFNVPY 161
Cdd:cd05322  81 VDLLVYS--AGI-----AKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGiQGRIIQINSkSGKVGSKHNSGY 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
2QQ5_A      162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGivqtELLKEHM 203
Cdd:cd05322 154 SAAKFGGVGLTQSLALDLAEHGITVNSLMLG----NLLKSPM 191
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 2-210 5.08e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 67.30  E-value: 5.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLGGQC--VPVVCDSSQESEVRSLFEQVdRE 79
Cdd:PRK05872   6 SLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAE---LGGDDrvLTVVADVTDLAAMQAAAEEA-VE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        80 QQGRLDVLVNNA----YAGVQTIlntrnkafweTPASmWD---DINNVGlrghyfcSVYGARLMVPA---GQGLIVVISS 149
Cdd:PRK05872  82 RFGGIDVVVANAgiasGGSVAQV----------DPDA-FRrviDVNLLG-------VFHTVRATLPAlieRRGYVLQVSS 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
2QQ5_A       150 PGSLqymFNVP----YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVLQ 210
Cdd:PRK05872 144 LAAF---AAAPgmaaYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVRDADADLPAFR 205
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 1-192 5.68e-13

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 66.96  E-value: 5.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         1 APMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVaqeAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQ 80
Cdd:PRK08265   2 IGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAV---AASLGERARFIATDITDDAAIERAVATV-VAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        81 QGRLDVLVNNA--Y--AGVQTilntrNKAFWEtpASMwdDINNVGlrghyfcSVYGARLMVP---AGQGLIVVISSPGS- 152
Cdd:PRK08265  78 FGRVDILVNLActYldDGLAS-----SRADWL--AAL--DVNLVS-------AAMLAQAAHPhlaRGGGAIVNFTSISAk 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
2QQ5_A       153 -------LqymfnvpYGVGKAACDKLAADCAHELRRHGVSCVSLWPG 192
Cdd:PRK08265 142 faqtgrwL-------YPASKAAIRQLTRSMAMDLAPDGIRVNSVSPG 181
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-185 1.47e-12

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 65.50  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTlrvVAQE-AQSLGGQCVPVVCDSSQESEVRSLFEQVdREQ 80
Cdd:PRK08642   2 QISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSED---AAEAlADELGDRAIALQADVTDREQVQAMFATA-TEH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        81 QGR-LDVLVNNAYAGVQTILNTRNKAfwetPASMWDDINNvGLRGhyfcSVYGARL--------MVPAGQGLIVVISSPg 151
Cdd:PRK08642  78 FGKpITTVVNNALADFSFDGDARKKA----DDITWEDFQQ-QLEG----SVKGALNtiqaalpgMREQGFGRIINIGTN- 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
2QQ5_A       152 slqyMFNVP------YGVGKAACDKLAADCAHELRRHGVS 185
Cdd:PRK08642 148 ----LFQNPvvpyhdYTTAKAALLGLTRNLAAELGPYGIT 183
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 5-204 1.57e-12

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: 65.49  E-value: 1.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:cd05345   5 GKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAAD---IGEAAIAIQADVTKRADVEAMVEAA-LSKFGRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       85 DVLVNNayAGVqtilNTRNKAFWETPASMWDDINNVGLRGHYfcsvYGARLMVP----AGQGLIVVISSPGSLQYMFN-V 159
Cdd:cd05345  81 DILVNN--AGI----THRNKPMLEVDEEEFDRVFAVNVKSIY----LSAQALVPhmeeQGGGVIINIASTAGLRPRPGlT 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
2QQ5_A      160 PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMA 204
Cdd:cd05345 151 WYNASKGWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFMG 195
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 3-209 2.46e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 64.95  E-value: 2.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:PRK07478   4 LNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALA-VERFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNayAGVqtilNTRNKAFWETPASMWDDINNVGLRGhyfcSVYGARLMVPA----GQGLIVVISS--------P 150
Cdd:PRK07478  83 GLDIAFNN--AGT----LGEMGPVAEMSLEGWRETLATNLTS----AFLGAKHQIPAmlarGGGSLIFTSTfvghtagfP 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
2QQ5_A       151 GslqymfNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVL 209
Cdd:PRK07478 153 G------MAAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMGDTPEAL 205
PRK07831 PRK07831
SDR family oxidoreductase;
3-146 2.49e-12

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 65.06  E-value: 2.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGAS-RGIGRGIALQLCKAGATVYITGRHLDTLRVVAQE-AQSLGGQCVP-VVCDSSQESEVRSLFEQVDrE 79
Cdd:PRK07831  15 LAGKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADElAAELGLGRVEaVVCDVTSEAQVDALIDAAV-E 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2QQ5_A        80 QQGRLDVLVNNAYAGVQTILntrnkafwetpASM----WDDINNVGLRGHYFCSVYGARLMVPAGQGLIVV 146
Cdd:PRK07831  94 RLGRLDVLVNNAGLGGQTPV-----------VDMtddeWSRVLDVTLTGTFRATRAALRYMRARGHGGVIV 153
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 10-198 2.53e-12

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 64.08  E-value: 2.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       10 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGgqcvpVVCDSSQESEVRSLFEQVdreqqGRLDVLVN 89
Cdd:cd11730   3 ILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALA-----RPADVAAELEVWALAQEL-----GPLDLLVY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       90 NAYAGVQtilntrnKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVvisspGSLQYMFNVP----YGVGK 165
Cdd:cd11730  73 AAGAILG-------KPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFL-----GAYPELVMLPglsaYAAAK 140

                       170       180       190
                ....*....|....*....|....*....|...
2QQ5_A      166 AACDKLAADCAHELRrhGVSCVSLWPGIVQTEL 198
Cdd:cd11730 141 AALEAYVEVARKEVR--GLRLTLVRPPAVDTGL 171
PRK09134 PRK09134
SDR family oxidoreductase;
10-91 2.57e-12

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 64.95  E-value: 2.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        10 VTGASRGIGRGIALQLCKAGATVYI-TGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDVLV 88
Cdd:PRK09134  14 VTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALAAEIRALGRRAVALQADLADEAEVRALVARA-SAALGPITLLV 92


                 ...
2QQ5_A        89 NNA 91
Cdd:PRK09134  93 NNA 95
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-210 2.74e-12

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 64.81  E-value: 2.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASR--GIGRGIALQLCKAGATVYIT-----------GRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEV 69
Cdd:PRK12859   4 LKNKVAVVTGVSRldGIGAAICKELAEAGADIFFTywtaydkempwGVDQDEQIQLQEELLKNGVKVSSMELDLTQNDAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        70 RSLFEQVdREQQGRLDVLVNNAYAGVqtilntrNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS 149
Cdd:PRK12859  84 KELLNKV-TEQLGYPHILVNNAAYST-------NNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTS 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
2QQ5_A       150 PGSLQYM-FNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMaKEEVLQ 210
Cdd:PRK12859 156 GQFQGPMvGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGWMTEEI-KQGLLP 216
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 5-91 3.34e-12

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: 64.62  E-value: 3.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYIT--GRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:cd05355  26 GKKALITGGDSGIGRAVAIAFAREGADVAINylPEEEDDAEETKKLIEEEGRKCLLIPGDLGDESFCRDLVKEV-VKEFG 104


                ....*....
2QQ5_A       83 RLDVLVNNA 91
Cdd:cd05355 105 KLDILVNNA 113
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-204 3.56e-12

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 64.33  E-value: 3.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASR--GIGRGIALQLCKAGATVYIT-----------GRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESE 68
Cdd:PRK12748   2 PLMKKIALVTGASRlnGIGAAVCRRLAAKGIDIFFTywspydktmpwGMHDKEPVLLKEEIESYGVRCEHMEIDLSQPYA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        69 VRSLFEQVdREQQGRLDVLVNNAYAGVQTILNTRNkafwetpASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVIS 148
Cdd:PRK12748  82 PNRVFYAV-SERLGDPSILINNAAYSTHTRLEELT-------AEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLT 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
2QQ5_A       149 SPGSLQYMFN-VPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQT----ELLKEHMA 204
Cdd:PRK12748 154 SGQSLGPMPDeLAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTgwitEELKHHLV 214
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 3-203 4.92e-12

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 64.08  E-value: 4.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLG--GQCVPVVCDSSQESEVRSlFEQVDREQ 80
Cdd:cd05330   1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIApdAEVLLIKADVSDEAQVEA-YVDATVEQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       81 QGRLDVLVNNayAGVQtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFN-V 159
Cdd:cd05330  80 FGRIDGFFNN--AGIE----GKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNqS 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
2QQ5_A      160 PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHM 203
Cdd:cd05330 154 GYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSL 197
PRK06139 PRK06139
SDR family oxidoreductase;
1-165 6.35e-12

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 64.36  E-value: 6.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         1 APMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQ 80
Cdd:PRK06139   3 GPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQA-ASF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        81 QGRLDVLVNNayAGVQTILNtrnkaFWETPASMWDDINNVGLRGHyfcsVYGARLMVP----AGQG-LIVVISSPGSLQY 155
Cdd:PRK06139  82 GGRIDVWVNN--VGVGAVGR-----FEETPIEAHEQVIQTNLIGY----MRDAHAALPifkkQGHGiFINMISLGGFAAQ 150

                        170
                 ....*....|
2QQ5_A       156 MFNVPYGVGK 165
Cdd:PRK06139 151 PYAAAYSASK 160
PRK06196 PRK06196
oxidoreductase; Provisional
 3-258 7.48e-12

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 63.93  E-value: 7.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDtlrvVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPD----VAREALAGIDGVEVVMLDLADLESVRAFAERF-LDSGR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNayAGVQTILNTRNKAFWETPASmwddINNVglrGHYFCSVYGARLMVPAGQGLIVVISSPG---------SL 153
Cdd:PRK06196  99 RIDILINN--AGVMACPETRVGDGWEAQFA----TNHL---GHFALVNLLWPALAAGAGARVVALSSAGhrrspirwdDP 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       154 QymFNVP------YGVGKAA-------CDKLAADcahelrrHGVSCVSLWPGIVQTElLKEHMAKEEVLQ--------DP 212
Cdd:PRK06196 170 H--FTRGydkwlaYGQSKTAnalfavhLDKLGKD-------QGVRAFSVHPGGILTP-LQRHLPREEQVAlgwvdehgNP 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
2QQ5_A       213 VLKQFKSAFSSAETTelsgkcvVALATDPNILSLSGKVLPSCDLAR 258
Cdd:PRK06196 240 IDPGFKTPAQGAATQ-------VWAATSPQLAGMGGLYCEDCDIAE 278
PRK07062 PRK07062
SDR family oxidoreductase;
2-196 1.11e-11

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 63.14  E-value: 1.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQVDRe 79
Cdd:PRK07062   5 QLEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARlrEKFPGARLLAARCDVLDEADVAAFAAAVEA- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        80 QQGRLDVLVNNAYAGvqtilntRNKAFWETPASMWDDinnvGLRGHYFCSVYGARLMVPA----GQGLIVVISSPGSLQ- 154
Cdd:PRK07062  84 RFGGVDMLVNNAGQG-------RVSTFADTTDDAWRD----ELELKYFSVINPTRAFLPLlrasAAASIVCVNSLLALQp 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
2QQ5_A       155 --YMfnVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQT 196
Cdd:PRK07062 153 epHM--VATSAARAGLLNLVKSLATELAPKGVRVNSILLGLVES 194
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 3-120 1.36e-11

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 62.58  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGG-QCVPVVCD--SSQESEVRSLFEQVDrE 79
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGpQPAIIPLDllTATPQNYQQLADTIE-E 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
2QQ5_A        80 QQGRLDVLVNNAyagvqTILNTRNkAFWETPASMWDDINNV 120
Cdd:PRK08945  89 QFGRLDGVLHNA-----GLLGELG-PMEQQDPEVWQDVMQV 123
PRK05866 PRK05866
SDR family oxidoreductase;
1-196 1.73e-11

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 62.84  E-value: 1.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         1 APMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQ 80
Cdd:PRK05866  36 VDLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVE-KR 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        81 QGRLDVLVNNAYAGVQTILntrnkafwETPASMWDDINNVgLRGHYFCSVygaRL-------MVPAGQGLIVVISSPGSL 153
Cdd:PRK05866 115 IGGVDILINNAGRSIRRPL--------AESLDRWHDVERT-MVLNYYAPL---RLirglapgMLERGDGHIINVATWGVL 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
2QQ5_A       154 QY---MFNVpYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQT 196
Cdd:PRK05866 183 SEaspLFSV-YNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVAT 227
PRK07806 PRK07806
SDR family oxidoreductase;
4-97 1.83e-11

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 62.43  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         4 NGQVCVVTGASRGIGRGIALQLCKAGATVYITGR-HLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:PRK07806   5 PGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRqKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTA-REEFG 83

                         90
                 ....*....|....*
2QQ5_A        83 RLDVLVNNAYAGVQT 97
Cdd:PRK07806  84 GLDALVLNASGGMES 98
PRK05693 PRK05693
SDR family oxidoreductase;
7-209 2.30e-11

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 62.50  E-value: 2.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         7 VCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqslGGQCVPVvcDSSQESEVRSLFEQVDrEQQGRLDV 86
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAAA----GFTAVQL--DVNDGAALARLAEELE-AEHGGLDV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        87 LVNNA-YAGVQTILNTRNKAF---WETpasmwddinNVglrghyFCSVYGARLMVPA---GQGLIVVISS-PGSLQYMFN 158
Cdd:PRK05693  76 LINNAgYGAMGPLLDGGVEAMrrqFET---------NV------FAVVGVTRALFPLlrrSRGLVVNIGSvSGVLVTPFA 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
2QQ5_A       159 VPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVL 209
Cdd:PRK05693 141 GAYCASKAAVHALSDALRLELAPFGVQVMEVQPGAIASQFASNASREAEQL 191
PRK08219 PRK08219
SDR family oxidoreductase;
7-206 2.75e-11

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 61.49  E-value: 2.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         7 VCVVTGASRGIGRGIALQLCKAgATVYITGRHLDTLRVVAQEAQSLggqcVPVVCDSSQESEVRSLFEQVDreqqgRLDV 86
Cdd:PRK08219   5 TALITGASRGIGAAIARELAPT-HTLLLGGRPAERLDELAAELPGA----TPFPVDLTDPEAIAAAVEQLG-----RLDV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        87 LVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLrghyFCSVYGARLMVP---AGQGLIVVISS-------PGslqym 156
Cdd:PRK08219  75 LVHN--AGV-----ADLGPVAESTVDEWRATLEVNV----VAPAELTRLLLPalrAAHGHVVFINSgaglranPG----- 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
2QQ5_A       157 fNVPYGVGK----AACDKLAADCAHELRrhgVSCVSlwPGIVQTELLKEHMAKE 206
Cdd:PRK08219 139 -WGSYAASKfalrALADALREEEPGNVR---VTSVH--PGRTDTDMQRGLVAQE 186
PRK08416 PRK08416
enoyl-ACP reductase;
3-233 4.92e-11

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 61.33  E-value: 4.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHLDTLRVVAQE-AQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQ 80
Cdd:PRK08416   6 MKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTyNSNVEEANKIAEDlEQKYGIKAKAYPLNILEPETYKELFKKID-ED 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        81 QGRLDVLVNNAYAGVQTILNTRNKAFWETPASmwddINNVglrghYFCSVY--------GARLMVPAGQGLIVVISSPGS 152
Cdd:PRK08416  85 FDRVDFFISNAIISGRAVVGGYTKFMRLKPKG----LNNI-----YTATVNafvvgaqeAAKRMEKVGGGSIISLSSTGN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       153 LQYMFNVP-YGVGKAACDKLAADCAHELRRHG--VSCVSLWPgiVQTELLKEHMAKEEVlQDPVLKQfkSAFSS-AETTE 228
Cdd:PRK08416 156 LVYIENYAgHGTSKAAVETMVKYAATELGEKNirVNAVSGGP--IDTDALKAFTNYEEV-KAKTEEL--SPLNRmGQPED 230


                 ....*
2QQ5_A       229 LSGKC 233
Cdd:PRK08416 231 LAGAC 235
PRK08703 PRK08703
SDR family oxidoreductase;
2-91 5.33e-11

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 61.10  E-value: 5.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQ---CVPVVCDSSQESEVRSLFEQVDR 78
Cdd:PRK08703   3 TLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPepfAIRFDLMSAEEKEFEQFAATIAE 82

                         90
                 ....*....|...
2QQ5_A        79 EQQGRLDVLVNNA 91
Cdd:PRK08703  83 ATQGKLDGIVHCA 95
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-123 7.81e-11

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 61.39  E-value: 7.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYI-----TGRHLDTLrvvaqeAQSLGGqcVPVVCDSSQESEVRSLFEQV 76
Cdd:PRK08261 207 PLAGKVALVTGAARGIGAAIAEVLARDGAHVVCldvpaAGEALAAV------ANRVGG--TALALDITAPDAPARIAEHL 278

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
2QQ5_A        77 dREQQGRLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLR 123
Cdd:PRK08261 279 -AERHGGLDIVVHN--AGI-----TRDKTLANMDEARWDSVLAVNLL 317
PRK08628 PRK08628
SDR family oxidoreductase;
3-198 8.23e-11

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 60.74  E-value: 8.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRvVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQG 82
Cdd:PRK08628   5 LKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDE-FAEELRALQPRAEFVQVDLTDDAQCRDAVEQTV-AKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNAYAGVQTILNTRNKAFwetPASMwdDINNVglrgHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFNVP-Y 161
Cdd:PRK08628  83 RIDGLVNNAGVNDGVGLEAGREAF---VASL--ERNLI----HYYVMAHYCLPHLKASRGAIVNISSKTALTGQGGTSgY 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
2QQ5_A       162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK08628 154 AAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMTPL 190
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 9-207 8.50e-11

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: 60.37  E-value: 8.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        9 VVTGASRGIGRGIALQLCKAGATVYITGR--HLDTLRvVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDReQQGRLDV 86
Cdd:cd05357   4 LVTGAAKRIGRAIAEALAAEGYRVVVHYNrsEAEAQR-LKDELNALRNSAVLVQADLSDFAACADLVAAAFR-AFGRCDV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       87 LVNNAYAGVQTILNtrnkafwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMFN-VPYGVGK 165
Cdd:cd05357  82 LVNNASAFYPTPLG-------QGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGyFAYCMSK 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
2QQ5_A      166 AACDKL----AADCAHELRRHGVScvslwPGIVqteLLKEHMAKEE 207
Cdd:cd05357 155 AALEGLtrsaALELAPNIRVNGIA-----PGLI---LLPEDMDAEY 192
PRK06194 PRK06194
hypothetical protein; Provisional
 5-196 8.60e-11

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 60.80  E-value: 8.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRL 84
Cdd:PRK06194   6 GKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAA-LERFGAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNAYAGVQTILntrnkafWETPASMWDDINNVGLRGhyfcSVYGARLMVP----------AGQGLIVVISSPGSLq 154
Cdd:PRK06194  85 HLLFNNAGVGAGGLV-------WENSLADWEWVLGVNLWG----VIHGVRAFTPlmlaaaekdpAYEGHIVNTASMAGL- 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
2QQ5_A       155 ymFNVP----YGVGKAACDKLAADCAHELRRHG--VSCVSLWPGIVQT 196
Cdd:PRK06194 153 --LAPPamgiYNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPT 198
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 10-200 1.20e-10

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: 59.77  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       10 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLGGQCVPV-VCDSSQESEVRSLFEQVDREQQGRLDVLV 88
Cdd:cd08931   5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAE---LGAENVVAgALDVTDRAAWAAALADFAAATGGRLDALF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       89 NNAYAGvqtilntRNKAFWETPASMWDDINNVGLRGhyfcSVYGARLMVP-----AGQGLIVVISSPGslqyMFNVP--- 160
Cdd:cd08931  82 NNAGVG-------RGGPFEDVPLAAHDRMVDINVKG----VLNGAYAALPylkatPGARVINTASSSA----IYGQPdla 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
2QQ5_A      161 -YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLK 200
Cdd:cd08931 147 vYSATKFAVRGLTEALDVEWARHGIRVADVWPWFVDTPILT 187
PRK07069 PRK07069
short chain dehydrogenase; Validated
 10-210 1.38e-10

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 59.72  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        10 VTGASRGIGRGIALQLCKAGATVYITgrHLDTLRVVAQEAQSLGGQCVPVVC-----DSSQESEVRSLFEQVDrEQQGRL 84
Cdd:PRK07069   4 ITGAAGGLGRAIARRMAEQGAKVFLT--DINDAAGLDAFAAEINAAHGEGVAfaavqDVTDEAQWQALLAQAA-DAMGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNayAGVQTILNTRNKAFWETPASMWDDINNVglrghyfcsVYGAR----LMVPAGQGLIVVISSPGSLQYMFNVP 160
Cdd:PRK07069  81 SVLVNN--AGVGSFGAIEQIELDEWRRVMAINVESI---------FLGCKhalpYLRASQPASIVNISSVAAFKAEPDYT 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
2QQ5_A       161 -YGVGKAACDKL----AADCAHelRRHGVSCVSLWPGIVQT---ELLKEHMAKEEVLQ 210
Cdd:PRK07069 150 aYNASKAAVASLtksiALDCAR--RGLDVRCNSIHPTFIRTgivDPIFQRLGEEEATR 205
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 7-212 1.57e-10

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 59.78  E-value: 1.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        7 VCVVTGASRGIGRGIALQLCKAGAT---VYITGRHLDTLRVVAQEAQSLGGQCVPV----VCDSsqesevRSLFEQVDRE 79
Cdd:cd09806   2 VVLITGCSSGIGLHLAVRLASDPSKrfkVYATMRDLKKKGRLWEAAGALAGGTLETlqldVCDS------KSVAAAVERV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       80 QQGRLDVLVNNAYAGVQTILNTRNKAfwETPASMwdDINNVGLrghyfcsvygARL-------MVPAGQGLIVVISSPGS 152
Cdd:cd09806  76 TERHVDVLVCNAGVGLLGPLEALSED--AMASVF--DVNVFGT----------VRMlqaflpdMKRRGSGRILVTSSVGG 141

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
2QQ5_A      153 LQ-YMFNVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLKEHMAKEEVLQDP 212
Cdd:cd09806 142 LQgLPFNDVYCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEEVLDR 202
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 5-91 1.58e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 60.05  E-value: 1.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITgrHLD-------TLRVVAQEaqslGGQCVPVVCDSSQESEVRSLFEQVD 77
Cdd:PRK06701  46 GKVALITGGDSGIGRAVAVLFAKEGADIAIV--YLDehedaneTKQRVEKE----GVKCLLIPGDVSDEAFCKDAVEETV 119

                         90
                 ....*....|....
2QQ5_A        78 REqQGRLDVLVNNA 91
Cdd:PRK06701 120 RE-LGRLDILVNNA 132
PRK09291 PRK09291
SDR family oxidoreductase;
10-196 1.76e-10

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 59.63  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        10 VTGASRGIGRGIALQLCKAG----ATVYITGRhLDTLRvvaQEAQSLGGqcvpvvcdsSQESEVRSLFEQVDREQQGRL- 84
Cdd:PRK09291   7 ITGAGSGFGREVALRLARKGhnviAGVQIAPQ-VTALR---AEAARRGL---------ALRVEKLDLTDAIDRAQAAEWd 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 -DVLVNNAYAGvqtilntRNKAFWETPASMwddinnvgLRGHYFCSVYG--------ARLMVPAGQGLIVVISSPGSLqy 155
Cdd:PRK09291  74 vDVLLNNAGIG-------EAGAVVDIPVEL--------VRELFETNVFGpleltqgfVRKMVARGKGKVVFTSSMAGL-- 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
2QQ5_A       156 mFNVP----YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQT 196
Cdd:PRK09291 137 -ITGPftgaYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLT 180
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
3-200 1.79e-10

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 59.64  E-value: 1.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVyITGRHLDTLRVVA--QEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREq 80
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKV-VAGCGPNSPRRVKwlEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAE- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        81 QGRLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYMF-NV 159
Cdd:PRK12938  79 VGEIDVLVNN--AGI-----TRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFgQT 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
2QQ5_A       160 PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELLK 200
Cdd:PRK12938 152 NYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVK 192
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 2-207 2.04e-10

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: 59.48  E-value: 2.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQeSEVRSLFEQVDREQQ 81
Cdd:cd08936   7 PLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGK-AEDRERLVATAVNLH 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       82 GRLDVLVNNAyagvqtilntRNKAFW----ETPASMWDDINNVGLRGhyfcSVYGARLMVPA----GQGLIVVISSPGSL 153
Cdd:cd08936  86 GGVDILVSNA----------AVNPFFgnilDSTEEVWDKILDVNVKA----TALMTKAVVPEmekrGGGSVVIVSSVAAF 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
2QQ5_A      154 QYMFNV-PYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQT---ELLKEHMAKEE 207
Cdd:cd08936 152 HPFPGLgPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTsfsSALWMDKAVEE 209
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 3-198 2.74e-10

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 58.77  E-value: 2.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLGGQCVPVVCDSSQESEVRSLFEQVDREQQG 82
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAE---LGERVKIFPANLSDRDEVKALGQKAEADLEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 rLDVLVNNayAGVqtilnTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISS-------PGSLQY 155
Cdd:PRK12936  81 -VDILVNN--AGI-----TKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSvvgvtgnPGQANY 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
2QQ5_A       156 MfnvpygVGKAACDKLAADCAHEL--RRHGVSCVSlwPGIVQTEL 198
Cdd:PRK12936 153 C------ASKAGMIGFSKSLAQEIatRNVTVNCVA--PGFIESAM 189
PRK09135 PRK09135
pteridine reductase; Provisional
 2-191 3.38e-10

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 58.79  E-value: 3.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         2 PMNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRH-LDTLRVVAQEAQSLGGQCVPVVC-DSSQESEVRSLFEQVDRe 79
Cdd:PRK09135   3 TDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADALAAELNALRPGSAAALQaDLLDPDALPELVAACVA- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        80 QQGRLDVLVNNAyagvqtilntrnKAFWETP-----ASMWDDINNVGLRGHYFCSVYGARLMVPAgQGLIVVISSPGSLQ 154
Cdd:PRK09135  82 AFGRLDALVNNA------------SSFYPTPlgsitEAQWDDLFASNLKAPFFLSQAAAPQLRKQ-RGAIVNITDIHAER 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
2QQ5_A       155 YMFNVP-YGVGKAACDKLAADCAHEL----RRHGVS-CVSLWP 191
Cdd:PRK09135 149 PLKGYPvYCAAKAALEMLTRSLALELapevRVNAVApGAILWP 191
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 3-198 1.17e-09

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 57.36  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLrvvAQEAQSLGGQCVPVVCDSSQESEVRSLFEQ-VDReqQ 81
Cdd:PRK08263   1 MMEKVWFITGASRGFGRAWTEAALERGDRVVATARDTATL---ADLAEKYGDRLLPLALDVTDRAAVFAAVETaVEH--F 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        82 GRLDVLVNNAYAGVqtilntrnkafwetpASMWDDINNVGLRGHYFCSVYGARLMVPA--------GQGLIVVISSPGSL 153
Cdd:PRK08263  76 GRLDIVVNNAGYGL---------------FGMIEEVTESEARAQIDTNFFGALWVTQAvlpylreqRSGHIIQISSIGGI 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
2QQ5_A       154 QYMFNVP-YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK08263 141 SAFPMSGiYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDW 186
PRK12742 PRK12742
SDR family oxidoreductase;
1-208 1.76e-09

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 56.69  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         1 APMNGQVCVVTGASRGIGRGIALQLCKAGATVYIT-GRHLDTLRVVAQEAqslGGQCVPVvcDSSQESEVRSLFeqvdrE 79
Cdd:PRK12742   2 GAFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTyAGSKDAAERLAQET---GATAVQT--DSADRDAVIDVV-----R 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        80 QQGRLDVLVNNA---YAGVQTILNTrnkafwetpasmwDDIN---NVGLRGHYFCSVYGARLMVPAGQglIVVISSPGSL 153
Cdd:PRK12742  72 KSGALDILVVNAgiaVFGDALELDA-------------DDIDrlfKINIHAPYHASVEAARQMPEGGR--IIIIGSVNGD 136

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2QQ5_A       154 QYMFN--VPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL----------------LKEHMAKEEV 208
Cdd:PRK12742 137 RMPVAgmAAYAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDAnpangpmkdmmhsfmaIKRHGRPEEV 209
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 5-213 2.98e-09

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site 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: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 56.05  E-value: 2.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGAS--RGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:cd05372   1 GKRILITGIAndRSIAWGIAKALHEAGAELAFTYQPEALRKRVEKLAERLGESALVLPCDVSNDEEIKELFAEV-KKDWG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       83 RLDVLVNN-AYAgvQTILNTRNkaFWETPASMWDDINNVglrghyfcSVYG-------ARLMVPAGqGLIVVISSPGSLQ 154
Cdd:cd05372  80 KLDGLVHSiAFA--PKVQLKGP--FLDTSRKGFLKALDI--------SAYSlvslakaALPIMNPG-GSIVTLSYLGSER 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2QQ5_A      155 YM--FNVpYGVGKAAcdkLAADC---AHELRRHG--VSCVSLWP-------GIVQTELLKEH---MA--KEEVLQDPV 213
Cdd:cd05372 147 VVpgYNV-MGVAKAA---LESSVrylAYELGRKGirVNAISAGPiktlaasGITGFDKMLEYseqRAplGRNVTAEEV 220
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 9-248 4.31e-09

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 55.99  E-value: 4.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        9 VVTGASRGIGRGIALQLCKAGA-TVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGRLDVL 87
Cdd:cd09810   5 VITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVGMPKDSYSVLHCDLASLDSVRQFVDNF-RRTGRPLDAL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       88 VNNAYAGVQTILNTRNKA--FWETPAS-----------MWDDINN----------VGLRGHYFCSVYGarlMVPAGQGLI 144
Cdd:cd09810  84 VCNAAVYLPTAKEPRFTAdgFELTVGVnhlghflltnlLLEDLQRsenaspriviVGSITHNPNTLAG---NVPPRATLG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      145 VVISSPGSLQyMFNVPYGVGKAACDKLAAD---C----AHELRRH-----GVSCVSLWPG-IVQTELLKEHMAKEEVLQD 211
Cdd:cd09810 161 DLEGLAGGLK-GFNSMIDGGEFEGAKAYKDskvCnmltTYELHRRlheetGITFNSLYPGcIAETGLFREHYPLFRTLFP 239

                       250       260       270
                ....*....|....*....|....*....|....*..
2QQ5_A      212 PVlkqFKSAFSSAETTELSGKCVVALATDPNiLSLSG 248
Cdd:cd09810 240 PF---QKYITKGYVSEEEAGERLAAVIADPS-LGVSG 272
PRK05717 PRK05717
SDR family oxidoreductase;
1-154 4.33e-09

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 55.67  E-value: 4.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         1 APMNGQVCVVTGASRGIGRGIALQLCKAGATVYITgrHLDTLRvVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDReQ 80
Cdd:PRK05717   6 PGHNGRVALVTGAARGIGLGIAAWLIAEGWQVVLA--DLDRER-GSKVAKALGENAWFIAMDVADEAQVAAGVAEVLG-Q 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2QQ5_A        81 QGRLDVLVNNAyagvqTILNTRNKAFWETPASMWDDINNVGLRGHYF----CSVYgarlmVPAGQGLIVVISSPGSLQ 154
Cdd:PRK05717  82 FGRLDALVCNA-----AIADPHNTTLESLSLAHWNRVLAVNLTGPMLlakhCAPY-----LRAHNGAIVNLASTRARQ 149
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 3-192 5.43e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 55.31  E-value: 5.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAqslGGQCVPVVCDSSQesevrslFEQVDR---- 78
Cdd:PRK06180   2 SSMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALH---PDRALARLLDVTD-------FDAIDAvvad 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        79 --EQQGRLDVLVNNAYAGVQTILNtrnkafwETPAS----MWdDINnvglrghyfcsVYGARLMVPA--------GQGLI 144
Cdd:PRK06180  72 aeATFGPIDVLVNNAGYGHEGAIE-------ESPLAemrrQF-EVN-----------VFGAVAMTKAvlpgmrarRRGHI 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
2QQ5_A       145 VVISSPGSLQYMFNVPYGVG-KAACDKLAADCAHELRRHGVSCVSLWPG 192
Cdd:PRK06180 133 VNITSMGGLITMPGIGYYCGsKFALEGISESLAKEVAPFGIHVTAVEPG 181
PRK08267 PRK08267
SDR family oxidoreductase;
10-200 6.00e-09

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 55.33  E-value: 6.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        10 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLG-GQCVPVVCDSSQESEVRSLFEQVDREQQGRLDVLV 88
Cdd:PRK08267   6 ITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAE---LGaGNAWTGALDVTDRAAWDAALADFAAATGGRLDVLF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        89 NNayAGVqtilnTRNKAFWETPASMWD---DINNVGLrghyfcsVYGARLMVPAGQGlivvisSPGSLqyMFNVP----- 160
Cdd:PRK08267  83 NN--AGI-----LRGGPFEDIPLEAHDrviDINVKGV-------LNGAHAALPYLKA------TPGAR--VINTSsasai 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
2QQ5_A       161 YGVGkaacdKLAADCAH-------------ELRRHGVSCVSLWPGIVQTELLK 200
Cdd:PRK08267 141 YGQP-----GLAVYSATkfavrgltealdlEWRRHGIRVADVMPLFVDTAMLD 188
PRK07024 PRK07024
SDR family oxidoreductase;
9-196 6.37e-09

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 54.94  E-value: 6.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         9 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGG-QCVPV-VCDSSQESEVRSLFEQvdreQQGRLDV 86
Cdd:PRK07024   6 FITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAARvSVYAAdVRDADALAAAAADFIA----AHGLPDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        87 LVNNAYAGVQTILNTRN--KAFWETpasMwdDINNVGLrGHYFCSVYGArlMVPAGQGLIVVISS-------PGSlqymf 157
Cdd:PRK07024  82 VIANAGISVGTLTEEREdlAVFREV---M--DTNYFGM-VATFQPFIAP--MRAARRGTLVGIASvagvrglPGA----- 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
2QQ5_A       158 nVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQT 196
Cdd:PRK07024 149 -GAYSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRT 186
PRK06914 PRK06914
SDR family oxidoreductase;
3-93 7.54e-09

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 55.03  E-value: 7.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLD---TLRVVAQEAqslggqcvpvvcDSSQESEVRSL----FEQ 75
Cdd:PRK06914   1 MNKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEkqeNLLSQATQL------------NLQQNIKVQQLdvtdQNS 68

                         90       100
                 ....*....|....*....|....
2QQ5_A        76 VDREQQ-----GRLDVLVNNA-YA 93
Cdd:PRK06914  69 IHNFQLvlkeiGRIDLLVNNAgYA 92
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 3-197 8.97e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 54.66  E-value: 8.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPV-VCDSSQESEVRSLFEQVdreqq 81
Cdd:PRK06125   5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVDVAVhALDLSSPEAREQLAAEA----- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        82 GRLDVLVNNAYAgvqtilntrnkafweTPASMWDDINNVGLRGHYFCSVYG----ARLMVPA----GQGLIV-VISSPGS 152
Cdd:PRK06125  80 GDIDILVNNAGA---------------IPGGGLDDVDDAAWRAGWELKVFGyidlTRLAYPRmkarGSGVIVnVIGAAGE 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
2QQ5_A       153 lQYMFNvpYGVGKAACDKLAA-DCA--HELRRHGVSCVSLWPGIVQTE 197
Cdd:PRK06125 145 -NPDAD--YICGSAGNAALMAfTRAlgGKSLDDGVRVVGVNPGPVATD 189
PRK08862 PRK08862
SDR family oxidoreductase;
10-90 9.08e-09

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 54.34  E-value: 9.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        10 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPV-VCDSSQESeVRSLFEQVDREQQGRLDVLV 88
Cdd:PRK08862  10 ITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCSALTDNVYSFqLKDFSQES-IRHLFDAIEQQFNRAPDVLV 88


                 ..
2QQ5_A        89 NN 90
Cdd:PRK08862  89 NN 90
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
9-201 1.21e-08

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 54.30  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         9 VVTGASRGIGRGIALQLCKAGATVYITGRhlDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDREQQgrldvlv 88
Cdd:PRK06924   5 IITGTSQGLGEAIANQLLEKGTHVISISR--TENKELTKLAEQYNSNLTFHSLDLQDVHELETNFNEILSSIQ------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        89 NNAYAGVQTIlntrNKAFWETPASMWDDINNVGLRGHY---------FCSVYGARLMVPAGQGLIVVISSpGSLQYMFN- 158
Cdd:PRK06924  76 EDNVSSIHLI----NNAGMVAPIKPIEKAESEELITNVhlnllapmiLTSTFMKHTKDWKVDKRVINISS-GAAKNPYFg 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
2QQ5_A       159 -VPYGVGKAACDkLAADCAH---ELRRHGVSCVSLWPGIVQTELLKE 201
Cdd:PRK06924 151 wSAYCSSKAGLD-MFTQTVAteqEEEEYPVKIVAFSPGVMDTNMQAQ 196
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 4-94 2.04e-08

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 53.81  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         4 NGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGR 83
Cdd:PRK07576   8 AGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQI-ADEFGP 86

                         90
                 ....*....|.
2QQ5_A        84 LDVLVNNAyAG 94
Cdd:PRK07576  87 IDVLVSGA-AG 96
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 4-206 5.03e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 52.60  E-value: 5.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         4 NGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLdtlrvvaqeAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQGR 83
Cdd:PRK06523   8 AGKRALVTGGTKGIGAATVARLLEAGARVVTTARSR---------PDDLPEGVEFVAADLTTAEGCAAVARAV-LERLGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        84 LDVLVNNAYA------GVQTIlntrnkafwetPASMWDDINNVGLrghyFCSVYGARLMVPA----GQGLIVVISS---- 149
Cdd:PRK06523  78 VDILVHVLGGssapagGFAAL-----------TDEEWQDELNLNL----LAAVRLDRALLPGmiarGSGVIIHVTSiqrr 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
2QQ5_A       150 ---PGSLqymfnVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTE---LLKEHMAKE 206
Cdd:PRK06523 143 lplPEST-----TAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEaavALAERLAEA 200
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 10-194 7.68e-08

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 51.68  E-value: 7.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        10 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLGGQCVPVVCDSSQESEVRSLFEQVDREQQgRLDVLVN 89
Cdd:PRK10538   5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDE---LGDNLYIAQLDVRNRAAIEEMLASLPAEWR-NIDVLVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        90 NayAGVQTILNTRNKAF---WETPAsmwdDINNVGLrghyfcsVYGARL----MVPAGQGLIVVI-SSPGSLQYMFNVPY 161
Cdd:PRK10538  81 N--AGLALGLEPAHKASvedWETMI----DTNNKGL-------VYMTRAvlpgMVERNHGHIINIgSTAGSWPYAGGNVY 147

                        170       180       190
                 ....*....|....*....|....*....|...
2QQ5_A       162 GVGKAACDKLAADCAHELRRHGVSCVSLWPGIV 194
Cdd:PRK10538 148 GATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLV 180
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 5-199 1.48e-07

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 51.11  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDReQQGRL 84
Cdd:PRK05876   6 GRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFR-LLGHV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        85 DVLVNNAYAGVQTILN--TRNKAFWETPASMWDDINNVglrghyfcSVYGARLMVPAGQGLIVVISSPGSLqymfnVP-- 160
Cdd:PRK05876  85 DVVFSNAGIVVGGPIVemTHDDWRWVIDVDLWGSIHTV--------EAFLPRLLEQGTGGHVVFTASFAGL-----VPna 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
2QQ5_A       161 ----YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELL 199
Cdd:PRK05876 152 glgaYGVAKYGVVGLAETLAREVTADGIGVSVLCPMVVETNLV 194
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 3-88 1.56e-07

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 50.79  E-value: 1.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGA--SRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGgqCVPVV-CDSSQESEVRSLFEQVdRE 79
Cdd:COG0623   3 LKGKRGLITGVanDRSIAWGIAKALHEEGAELAFTYQGEALKKRVEPLAEELG--SALVLpCDVTDDEQIDALFDEI-KE 79


                ....*....
2QQ5_A       80 QQGRLDVLV 88
Cdd:COG0623  80 KWGKLDFLV 88
PRK07041 PRK07041
SDR family oxidoreductase;
9-91 1.89e-07

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 50.42  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         9 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSlGGQCVPVVCDSSQESEVRSLFEQVdreqqGRLDVLV 88
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGG-GAPVRTAALDITDEAAVDAFFAEA-----GPFDHVV 74


                 ...
2QQ5_A        89 NNA 91
Cdd:PRK07041  75 ITA 77
PRK06720 PRK06720
hypothetical protein; Provisional
 3-91 3.70e-07

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 48.81  E-value: 3.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEqVDREQQG 82
Cdd:PRK06720  14 LAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEITNLGGEALFVSYDMEKQGDWQRVIS-ITLNAFS 92


                 ....*....
2QQ5_A        83 RLDVLVNNA 91
Cdd:PRK06720  93 RIDMLFQNA 101
PRK09186 PRK09186
flagellin modification protein A; Provisional
 3-149 5.80e-07

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 49.22  E-value: 5.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQ---CVpVVCDSSQESEVRSLFEQVdRE 79
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSkklSL-VELDITDQESLEEFLSKS-AE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2QQ5_A        80 QQGRLDVLVNNAYAgvqtilntRNKA----FWEtpASMwDDIN---NVGLRGHYFCSVYGARLMVPAGQGLIVVISS 149
Cdd:PRK09186  80 KYGKIDGAVNCAYP--------RNKDygkkFFD--VSL-DDFNenlSLHLGSSFLFSQQFAKYFKKQGGGNLVNISS 145
PRK08340 PRK08340
SDR family oxidoreductase;
9-91 6.24e-07

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 49.42  E-value: 6.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         9 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGqCVPVVCDSSQESEVRSLFEQVdREQQGRLDVLV 88
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYGE-VYAVKADLSDKDDLKNLVKEA-WELLGGIDALV 81


                 ...
2QQ5_A        89 NNA 91
Cdd:PRK08340  82 WNA 84
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-192 1.32e-06

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 48.22  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVpVVCDSSQESEVRSLFEQVDREQQG 82
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYGNIHY-VVGDVSSTESARNVIEKAAKVLNA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        83 RLDVLVNNAYAGVQTIlntrnkafwETPASMWDDINNvGLRGHYFCSVYGARLMVPAGQglIVVISSPGSL--QYMFNVP 160
Cdd:PRK05786  82 IDGLVVTVGGYVEDTV---------EEFSGLEEMLTN-HIKIPLYAVNASLRFLKEGSS--IVLVSSMSGIykASPDQLS 149

                        170       180       190
                 ....*....|....*....|....*....|..
2QQ5_A       161 YGVGKAACDKLAADCAHELRRHGVSCVSLWPG 192
Cdd:PRK05786 150 YAVAKAGLAKAVEILASELLGRGIRVNGIAPT 181
PRK06128 PRK06128
SDR family oxidoreductase;
3-97 1.47e-06

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 48.32  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATV---YITGRHLDTLRVVaQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdRE 79
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFAREGADIalnYLPEEEQDAAEVV-QLIQAEGRKAVALPGDLKDEAFCRQLVERA-VK 130

                         90
                 ....*....|....*...
2QQ5_A        80 QQGRLDVLVNNayAGVQT 97
Cdd:PRK06128 131 ELGGLDILVNI--AGKQT 146
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 5-91 1.86e-06

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 48.52  E-value: 1.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCK-AGATVYITGRH-----LDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdR 78
Cdd:cd08953 205 GGVYLVTGGAGGIGRALARALARrYGARLVLLGRSplppeEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKV-R 283

                        90
                ....*....|...
2QQ5_A       79 EQQGRLDVLVNNA 91
Cdd:cd08953 284 ERYGAIDGVIHAA 296
PRK07102 PRK07102
SDR family oxidoreductase;
10-196 1.92e-06

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 47.61  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        10 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPV-VCDSSQESEVRSLFEQVdreqQGRLD-VL 87
Cdd:PRK07102   6 IIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAVAVSThELDILDTASHAAFLDSL----PALPDiVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        88 VNNAYAGVQtilnTRNKAFWETpASMWDDINNVG---LRGHYfcsvygARLMVPAGQGLIVVISSP------GSlqymfN 158
Cdd:PRK07102  82 IAVGTLGDQ----AACEADPAL-ALREFRTNFEGpiaLLTLL------ANRFEARGSGTIVGISSVagdrgrAS-----N 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
2QQ5_A       159 VPYGVGKAAcdkLAADCA---HELRRHGVSCVSLWPGIVQT 196
Cdd:PRK07102 146 YVYGSAKAA---LTAFLSglrNRLFKSGVHVLTVKPGFVRT 183
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 3-198 2.01e-06

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 47.64  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAqslgGQCVPVVcdssqESEVRSLFEQ---VDR- 78
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRF----GDHVLVV-----EGDVTSYADNqraVDQt 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        79 -EQQGRLDVLVNNayAGVQTILNTRNKAFWETPASMWDDINNVGLRGHyfcsVYGARLMVPA----GQGLIVVISSPGSL 153
Cdd:PRK06200  75 vDAFGKLDCFVGN--AGIWDYNTSLVDIPAETLDTAFDEIFNVNVKGY----LLGAKAALPAlkasGGSMIFTLSNSSFY 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
2QQ5_A       154 QYMFNVPYGVGKAACDKLAADCAHEL----RRHGVScvslwPGIVQTEL 198
Cdd:PRK06200 149 PGGGGPLYTASKHAVVGLVRQLAYELapkiRVNGVA-----PGGTVTDL 192
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
9-194 4.41e-06

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 46.90  E-value: 4.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        9 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAqslggQCVPVVCDSSQESEVRSLFEQVdreqqgrlDVLV 88
Cdd:COG0451   3 LVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALP-----GVEFVRGDLRDPEALAAALAGV--------DAVV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       89 NNA-YAGVQTilntrnkafwETPASMWdDINNVGLRghyfcSVygARLMVPAGQGLIVVISS------------------ 149
Cdd:COG0451  70 HLAaPAGVGE----------EDPDETL-EVNVEGTL-----NL--LEAARAAGVKRFVYASSssvygdgegpidedtplr 131

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
2QQ5_A      150 PGSlqymfnvPYGVGKAACDKLAADCAhelRRHGVSCVSLWPGIV 194
Cdd:COG0451 132 PVS-------PYGASKLAAELLARAYA---RRYGLPVTILRPGNV 166
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-153 6.10e-06

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 46.11  E-value: 6.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYitgrHLDTlrvvaQEAQSLGGQCVPVVCDSSQESEvrSLFEQVdreqqGRL 84
Cdd:PRK06550   5 TKTVLITGAASGIGLAQARAFLAQGAQVY----GVDK-----QDKPDLSGNFHFLQLDLSDDLE--PLFDWV-----PSV 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2QQ5_A        85 DVLVNNayAGV----QTILntrnkafwETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSL 153
Cdd:PRK06550  69 DILCNT--AGIlddyKPLL--------DTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASF 131
PRK07775 PRK07775
SDR family oxidoreductase;
9-196 6.34e-06

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 46.29  E-value: 6.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         9 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDrEQQGRLDVLV 88
Cdd:PRK07775  14 LVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAE-EALGEIEVLV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        89 nnAYAGvqtilNTRNKAFWETPASMWDDINNVGLRGHY--FCSVYGArlMVPAGQGLIVVISSPGSL-QYMFNVPYGVGK 165
Cdd:PRK07775  93 --SGAG-----DTYFGKLHEISTEQFESQVQIHLVGANrlATAVLPG--MIERRRGDLIFVGSDVALrQRPHMGAYGAAK 163

                        170       180       190
                 ....*....|....*....|....*....|.
2QQ5_A       166 AACDKLAADCAHELRRHGVSCVSLWPGIVQT 196
Cdd:PRK07775 164 AGLEAMVTNLQMELEGTGVRASIVHPGPTLT 194
PRK05854 PRK05854
SDR family oxidoreductase;
5-97 1.22e-05

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 45.44  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHldtlRVVAQEAQSLGGQCVPVV------CDSSQESEVRSLFEQVDR 78
Cdd:PRK05854  14 GKRAVVTGASDGLGLGLARRLAAAGAEVILPVRN----RAKGEAAVAAIRTAVPDAklslraLDLSSLASVAALGEQLRA 89

                         90       100
                 ....*....|....*....|
2QQ5_A        79 EqqGR-LDVLVNNayAGVQT 97
Cdd:PRK05854  90 E--GRpIHLLINN--AGVMT 105
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 3-251 1.33e-05

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic 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, 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: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 45.42  E-value: 1.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLGGQCVPVVCDssqeseVRSLFEQ---VDR- 78
Cdd:cd05348   2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRAD---FGDAVVGVEGD------VRSLADNeraVARc 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       79 -EQQGRLDVLVNNayAGVQTILNTRNKAFWETPASMWDDINNVGLRGhYFCSVYGARLMVPAGQG-LIVVISSPGSLQYM 156
Cdd:cd05348  73 vERFGKLDCFIGN--AGIWDYSTSLVDIPEEKLDEAFDELFHINVKG-YILGAKAALPALYATEGsVIFTVSNAGFYPGG 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A      157 FNVPYGVGKAACDKLAADCAHEL----RRHGVScvslwPGIVQTELL------KEHMAKEEVLQDPVLKQFKSAFSSAET 226
Cdd:cd05348 150 GGPLYTASKHAVVGLVKQLAYELaphiRVNGVA-----PGGMVTDLRgpaslgQGETSISTPPLDDMLKSILPLGFAPEP 224

                       250       260
                ....*....|....*....|....*
2QQ5_A      227 TELSGKCVVaLATDPNILSLSGKVL 251
Cdd:cd05348 225 EDYTGAYVF-LASRGDNRPATGTVI 248
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 5-91 1.40e-05

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 45.28  E-value: 1.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTlrvvAQEAQS-----LGGQCVPV-VCDSSQESEVRSLFEQVDR 78
Cdd:cd09808   1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTR----AEEARKeieteSGNQNIFLhIVDMSDPKQVWEFVEEFKE 76

                        90
                ....*....|...
2QQ5_A       79 EQQgRLDVLVNNA 91
Cdd:cd09808  77 EGK-KLHVLINNA 88
PRK07985 PRK07985
SDR family oxidoreductase;
3-198 2.10e-05

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 44.99  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGASRGIGRGIALQLCKAGATVYITgrHLDTLRVVAQEAQSL----GGQCVPVVCDSSQESEVRSLFEQVdR 78
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAIS--YLPVEEEDAQDVKKIieecGRKAVLLPGDLSDEKFARSLVHEA-H 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        79 EQQGRLDV--LVNNAYAGVQTILNTRNKAFWETPAsmwddINNVGLrghyFCSVYGARLMVPAGQGLIVVIS------SP 150
Cdd:PRK07985 124 KALGGLDImaLVAGKQVAIPDIADLTSEQFQKTFA-----INVFAL----FWLTQEAIPLLPKGASIITTSSiqayqpSP 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
2QQ5_A       151 GSLQymfnvpYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK07985 195 HLLD------YAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAL 236
PRK05993 PRK05993
SDR family oxidoreductase;
9-197 2.56e-05

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 44.63  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         9 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTlrVVAQEAQSLggQCVPVvcDSSQESEVRSLFEQVDREQQGRLDVLV 88
Cdd:PRK05993   8 LITGCSSGIGAYCARALQSDGWRVFATCRKEED--VAALEAEGL--EAFQL--DYAEPESIAALVAQVLELSGGRLDALF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        89 NN-AYAgvqtilntrnkafwetPASMWDDINNVGLRGHYFCSVYG----ARLMVPA----GQGLIVVISSP-GSLQYMFN 158
Cdd:PRK05993  82 NNgAYG----------------QPGAVEDLPTEALRAQFEANFFGwhdlTRRVIPVmrkqGQGRIVQCSSIlGLVPMKYR 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
2QQ5_A       159 VPYGVGKAACDKLAADCAHELRRHGVScVSLW-PGIVQTE 197
Cdd:PRK05993 146 GAYNASKFAIEGLSLTLRMELQGSGIH-VSLIePGPIETR 184
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 5-95 3.49e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 44.25  E-value: 3.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDT-LRVVAQEAQSLGGQCVPVV-CDSSQESEVRSLFEQVdREQQG 82
Cdd:PRK06197  16 GRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKgKAAAARITAATPGADVTLQeLDLTSLASVRAAADAL-RAAYP 94

                         90
                 ....*....|...
2QQ5_A        83 RLDVLVNNayAGV 95
Cdd:PRK06197  95 RIDLLINN--AGV 105
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 7-217 4.84e-05

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: 43.75  E-value: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A          7 VCVVTGASRGIGRGIALQLCKA----GATVYITGRHLDTLRVVAQE--AQSLGGQCVPVVCDSSQESEV----RSLFEQV 76
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEigAERSGLRVVRVSLDLGAEAGLeqllKALRELP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         77 DREQQGRLdVLVNNayAGVQTILNTRNKAFWETPASMWDDINNVGLRGHYFCSVYGARLMVPAGQGLIVVISSPGSLQYM 156
Cdd:TIGR01500  82 RPKGLQRL-LLINN--AGTLGDVSKGFVDLSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPGLNRTVVNISSLCAIQPF 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
2QQ5_A        157 FNVP-YGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTELlkEHMAKEEVlQDPVLKQF 217
Cdd:TIGR01500 159 KGWAlYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDM--QQQVREES-VDPDMRKG 217
PRK06482 PRK06482
SDR family oxidoreductase;
10-91 5.57e-05

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 43.57  E-value: 5.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        10 VTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEaqsLGGQCVPVVCDSSQESEVRSLFEQVDREqQGRLDVLVN 89
Cdd:PRK06482   7 ITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKAR---YGDRLWVLQLDVTDSAAVRAVVDRAFAA-LGRIDVVVS 82


                 ..
2QQ5_A        90 NA 91
Cdd:PRK06482  83 NA 84
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 7-121 5.91e-05

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 43.38  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A          7 VCVVTGASRGIGRGIALQLCKAGATVYITGRHL--DTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVDR---EQQ 81
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSaaAASTLAAELNARRPNSAVTCQADLSNSATLFSRCEAIIDacfRAF 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
2QQ5_A         82 GRLDVLVNNAyagvqtilntrnKAFWETPASMWDDINNVG 121
Cdd:TIGR02685  83 GRCDVLVNNA------------SAFYPTPLLRGDAGEGVG 110
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 5-196 1.22e-04

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 41.93  E-value: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRhldtlrvvaQEAQSLGGQCVPVVCDSSQESEvRSLFEQVDReQQGRL 84
Cdd:cd05334   1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDL---------AENEEADASIIVLDSDSFTEQA-KQVVASVAR-LSGKV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       85 DVLVNNA--YAGVqtilNTRNKAFWETPASMWDdinnVGLRGHYFCSVYGARLMVPAgqGLIVVISSPGSLQ-YMFNVPY 161
Cdd:cd05334  70 DALICVAggWAGG----SAKSKSFVKNWDLMWK----QNLWTSFIASHLATKHLLSG--GLLVLTGAKAALEpTPGMIGY 139

                       170       180       190
                ....*....|....*....|....*....|....*..
2QQ5_A      162 GVGKAACDKLAADCAHELR--RHGVSCVSLWPGIVQT 196
Cdd:cd05334 140 GAAKAAVHQLTQSLAAENSglPAGSTANAILPVTLDT 176
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 10-211 1.37e-04

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: 42.26  E-value: 1.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       10 VTGASRGIGRGIALQLCKAGATVYITgrhldTLRVVAQEAQSLGGQCVP----VVCDSSQESEVRSLFEQVDREQQGR-L 84
Cdd:cd09805   5 ITGCDSGFGNLLAKKLDSLGFTVLAG-----CLTKNGPGAKELRRVCSDrlrtLQLDVTKPEQIKRAAQWVKEHVGEKgL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       85 DVLVNNayAGVQTILNTrnkaFWETPASMWDDINNVGLRGhyfcSVYGARLMVP---AGQGLIVVISSP-GSLQYMFNVP 160
Cdd:cd09805  80 WGLVNN--AGILGFGGD----EELLPMDDYRKCMEVNLFG----TVEVTKAFLPllrRAKGRVVNVSSMgGRVPFPAGGA 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
2QQ5_A      161 YGVGKAACDKLAADCAHELRRHG--VSCV---SLWPGIVQTELLKEHMAKE-------EVLQD 211
Cdd:cd09805 150 YCASKAAVEAFSDSLRRELQPWGvkVSIIepgNFKTGITGNSELWEKQAKKlwerlppEVKKD 212
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 10-91 1.45e-04

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 42.09  E-value: 1.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       10 VTGASRGIGRGIALQLCKAGATVYITGRhlDTLRVVAQEAQSLGGQCVpVVCDSSQESEVRSLFEQVDreQQGRLDVLVN 89
Cdd:cd08951  12 ITGSSDGLGLAAARTLLHQGHEVVLHAR--SQKRAADAKAACPGAAGV-LIGDLSSLAETRKLADQVN--AIGRFDAVIH 86


                ..
2QQ5_A       90 NA 91
Cdd:cd08951  87 NA 88
PRK08251 PRK08251
SDR family oxidoreductase;
6-198 1.52e-04

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 41.84  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         6 QVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQE--AQSLGGQCVPVVCDSSQESEVRSLFEQVDREqQGR 83
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAEllARYPGIKVAVAALDVNDHDQVFEVFAEFRDE-LGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        84 LDVLVNNAYAGVQTILNT----RNKAFWETpasmwddiNNVGLRGHyfCSVyGARLMVPAGQGLIVVISS-------PGS 152
Cdd:PRK08251  82 LDRVIVNAGIGKGARLGTgkfwANKATAET--------NFVAALAQ--CEA-AMEIFREQGSGHLVLISSvsavrglPGV 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
2QQ5_A       153 LqymfnVPYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQTEL 198
Cdd:PRK08251 151 K-----AAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEM 191
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 9-91 1.63e-04

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 41.41  E-value: 1.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        9 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVvaqeaqslggqcvpvvcDSSQESEVRSLFEQVdreqqGRLDVLV 88
Cdd:cd11731   2 IVIGATGTIGLAVAQLLSAHGHEVITAGRSSGDYQV-----------------DITDEASIKALFEKV-----GHFDAIV 59


                ...
2QQ5_A       89 NNA 91
Cdd:cd11731  60 STA 62
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 8-80 1.77e-04

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 42.37  E-value: 1.77e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2QQ5_A        8 CVVTGASRGIGRGIALQLCKAGAT-VYITGRHLDTLRVVAQEAQSLGGQCVPVV--CDSSQESEVRSLFEQVDREQ 80
Cdd:cd05274 153 YLITGGLGGLGLLVARWLAARGARhLVLLSRRGPAPRAAARAALLRAGGARVSVvrCDVTDPAALAALLAELAAGG 228
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
3-94 2.50e-04

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 41.24  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGAS--RGIGRGIALQLCKAGATVYIT------GRHLDTLR-VVAQEAQSLggqCVPvvCDSSQESEVRSLF 73
Cdd:PRK07370   4 LTGKKALVTGIAnnRSIAWGIAQQLHAAGAELGITylpdekGRFEKKVReLTEPLNPSL---FLP--CDVQDDAQIEETF 78

                         90       100
                 ....*....|....*....|..
2QQ5_A        74 EQVdREQQGRLDVLVNN-AYAG 94
Cdd:PRK07370  79 ETI-KQKWGKLDILVHClAFAG 99
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 5-91 2.66e-04

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 41.39  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         5 GQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGG--QCVPVVCDSSQESE--VRSLFEQVDREQ 80
Cdd:PLN02780  53 GSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSktQIKTVVVDFSGDIDegVKRIKETIEGLD 132

                         90
                 ....*....|.
2QQ5_A        81 QGrldVLVNNA 91
Cdd:PLN02780 133 VG---VLINNV 140
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 9-201 3.09e-04

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 40.94  E-value: 3.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        9 VVTGASRGIGRGIALQLCKAGATVyitgrhldtLRVVAQEAQslggqcvpVVCDSSQESEVRSLFEQVDREQQGRLDVLV 88
Cdd:cd05328   3 VITGAASGIGAATAELLEDAGHTV---------IGIDLREAD--------VIADLSTPEGRAAAIADVLARCSGVLDGLV 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A       89 NNAYAGVQtilntrnkafweTPASMWDDINNVGLRgHYFCSVygARLMVPAGQGLIVVISSPGSLQYMFNVP-------- 160
Cdd:cd05328  66 NCAGVGGT------------TVAGLVLKVNYFGLR-ALMEAL--LPRLRKGHGPAAVVVSSIAGAGWAQDKLelakalaa 130

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
2QQ5_A      161 --------------------YGVGKAACDKLAADCAHE-LRRHGVSCVSLWPGIVQTELLKE 201
Cdd:cd05328 131 gtearavalaehagqpgylaYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPILQA 192
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 9-79 3.51e-04

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 40.24  E-value: 3.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2QQ5_A          9 VVTGASRGIGRGIALQLCKAGA-TVYITGRHLDTLRVVAQ---EAQSLGGQCVPVVCDSSQESEVRSLFEQVDRE 79
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGArHLVLLSRSAAPRPDAQAliaELEARGVEVVVVACDVSDPDAVAALLAEIKAE 78
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 7-91 1.06e-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: 39.00  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A           7 VCVVTGASRGIGRGIALQLCKAGA-TVYITGRH---LDTLRVVAQEAQSLGGQCVPVVCDSSQESEVRSLFEQVdREQQG 82
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGArRLVLLSRSgpdAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAI-PAVEG 80


                   ....*....
2QQ5_A          83 RLDVLVNNA 91
Cdd:smart00822  81 PLTGVIHAA 89
PRK05884 PRK05884
SDR family oxidoreductase;
9-89 1.19e-03

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 39.02  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         9 VVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGgqcvpVVCDSSQES---EVRSLFEQvdreqqgRLD 85
Cdd:PRK05884   4 LVTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVAAKELDVDA-----IVCDNTDPAsleEARGLFPH-------HLD 71


                 ....
2QQ5_A        86 VLVN 89
Cdd:PRK05884  72 TIVN 75
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
3-196 6.49e-03

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 37.03  E-value: 6.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A         3 MNGQVCVVTGAS--RGIGRGIALQLCKAGATVYITGRHLDTLRVVAQEAQSLGGQCVpVVCDSSQESEVRSLFEQVDREQ 80
Cdd:PRK08415   3 MKGKKGLIVGVAnnKSIAYGIAKACFEQGAELAFTYLNEALKKRVEPIAQELGSDYV-YELDVSKPEHFKSLAESLKKDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QQ5_A        81 qGRLDVLVNN-AYAGVQTILNtrnkAFWETPASMWDDINNVglrghyfcSVYG----ARLMVP--AGQGLIVVISSPGSL 153
Cdd:PRK08415  82 -GKIDFIVHSvAFAPKEALEG----SFLETSKEAFNIAMEI--------SVYSlielTRALLPllNDGASVLTLSYLGGV 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
2QQ5_A       154 QYM--FNVpYGVGKAACDKLAADCAHELRRHGVSCVSLWPGIVQT 196
Cdd:PRK08415 149 KYVphYNV-MGVAKAALESSVRYLAVDLGKKGIRVNAISAGPIKT 192
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 5-63 6.69e-03

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 37.43  E-value: 6.69e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2QQ5_A        5 GQVCVVTGASRGIGrGIALQLCKA-GATVYITGR---HLDTLR--------------VVAQEAQSLGGQCVPVVCDS 63
Cdd:COG0604 140 GETVLVHGAAGGVG-SAAVQLAKAlGARVIATASspeKAELLRalgadhvidyreedFAERVRALTGGRGVDVVLDT 215
 
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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