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Conserved domains on  [gi|1034664465|ref|XP_016869974|]
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prostaglandin reductase 1 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
B4_12hDH super family cl31253
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
4-254 0e+00

leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase.


The actual alignment was detected with superfamily member TIGR02825:

Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 526.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465   4 TKTWTLKKHFVGYPTNSDFELKTAELPPLKNGEVLLEALFLTVDPYMRVAAKRLKEGDTMMGQQVAKVVESKNVALPKGT 83
Cdd:TIGR02825   1 AKTWTLKKHFVGYPTDSDFELKTVELPPLNNGEVLLEALFLSVDPYMRVAAKRLKEGDTMMGQQVARVVESKNVALPKGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  84 IVLASPGWTTHSISDGKDLEKLLTEWPDTIPLSLALGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAK 163
Cdd:TIGR02825  81 IVLASPGWTSHSISDGKDLEKLLTEWPDTLPLSLALGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 164 LKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAIS 243
Cdd:TIGR02825 161 LKGCKVVGAAGSDEKVAYLKKLGFDVAFNYKTVKSLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAIS 240
                         250
                  ....*....|.
gi 1034664465 244 TYNRTGPLPPG 254
Cdd:TIGR02825 241 TYNRTGPLPPG 251
 
Name Accession Description Interval E-value
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
4-254 0e+00

leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase.


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 526.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465   4 TKTWTLKKHFVGYPTNSDFELKTAELPPLKNGEVLLEALFLTVDPYMRVAAKRLKEGDTMMGQQVAKVVESKNVALPKGT 83
Cdd:TIGR02825   1 AKTWTLKKHFVGYPTDSDFELKTVELPPLNNGEVLLEALFLSVDPYMRVAAKRLKEGDTMMGQQVARVVESKNVALPKGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  84 IVLASPGWTTHSISDGKDLEKLLTEWPDTIPLSLALGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAK 163
Cdd:TIGR02825  81 IVLASPGWTSHSISDGKDLEKLLTEWPDTLPLSLALGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 164 LKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAIS 243
Cdd:TIGR02825 161 LKGCKVVGAAGSDEKVAYLKKLGFDVAFNYKTVKSLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAIS 240
                         250
                  ....*....|.
gi 1034664465 244 TYNRTGPLPPG 254
Cdd:TIGR02825 241 TYNRTGPLPPG 251
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
2-253 5.06e-160

13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 hydroxydehydrogenase activity; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto- 13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176254 [Multi-domain]  Cd Length: 329  Bit Score: 446.71  E-value: 5.06e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465   2 VRTKTWTLKKHFVGYPTNSDFELKTAELPPLKNGEVLLEALFLTVDPYMRVAAKRLKEGDTMMGQQVAKVVESKNVALPK 81
Cdd:cd08294     1 VKAKTWVLKKHFDGKPKESDFELVEEELPPLKDGEVLCEALFLSVDPYMRPYSKRLNEGDTMIGTQVAKVIESKNSKFPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  82 GTIVLASPGWTTHSISDGK---DLEKLLTEWPDTIPLSLALGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVV 158
Cdd:cd08294    81 GTIVVASFGWRTHTVSDGKdqpDLYKLPADLPDDLPPSLALGVLGMPGLTAYFGLLEICKPKAGETVVVNGAAGAVGSLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 159 GQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVeSLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAI 238
Cdd:cd08294   161 GQIAKIKGCKVIGCAGSDDKVAWLKELGFDAVFNYKTV-SLEEALKEAAPDGIDCYFDNVGGEFSSTVLSHMNDFGRVAV 239
                         250
                  ....*....|....*
gi 1034664465 239 CGAISTYNRTGPLPP 253
Cdd:cd08294   240 CGSISTYNDKEPKKG 254
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
1-254 3.52e-119

NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 441733 [Multi-domain]  Cd Length: 333  Bit Score: 343.19  E-value: 3.52e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465   1 MVRTKTWTLKKHFVGYPTNSDFELKTAELPPLKNGEVLLEALFLTVDPYMRVaakRLKE----------GDTMMGQQVAK 70
Cdd:COG2130     2 MTTNRQIVLASRPEGEPTPEDFRLEEVPVPEPGDGEVLVRNLYLSVDPYMRG---RMSDaksyappvelGEVMRGGAVGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  71 VVESKNVALPKGTIVLASPGWTTHSISDGKDLEKLLtewPDTIPLSLALGTVGMPGLTAYFGLLEICGVKGGETVMVNAA 150
Cdd:COG2130    79 VVESRHPDFAVGDLVLGMLGWQDYAVSDGAGLRKVD---PSLAPLSAYLGVLGMPGLTAYFGLLDIGKPKAGETVVVSAA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 151 AGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYL-QKLGFDVVFNYKTvESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQ 229
Cdd:COG2130   156 AGAVGSVVGQIAKLKGCRVVGIAGGAEKCRYLvEELGFDAAIDYKA-GDLAAALAAACPDGIDVYFDNVGGEILDAVLPL 234
                         250       260
                  ....*....|....*....|....*
gi 1034664465 230 MKKFGRIAICGAISTYNRTGPlPPG 254
Cdd:COG2130   235 LNTFARIAVCGAISQYNATEP-PPG 258
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
2-243 1.89e-59

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 191.59  E-value: 1.89e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465   2 VRTKTWTLKKHFVGYPTNSDFELKTAELPPLK----NGEVLLEALFLTVDPYMRvaaKRLKE-----------GDTMMGQ 66
Cdd:PLN03154    7 VENKQVILKNYIDGIPKETDMEVKLGNKIELKapkgSGAFLVKNLYLSCDPYMR---GRMRDfhdsylppfvpGQRIEGF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  67 QVAKVVESKNVALPKGTIVLASPGWTTHSISDGKDLEKLLTEWPDTIPLSLALGTVGMPGLTAYFGLLEICGVKGGETVM 146
Cdd:PLN03154   84 GVSKVVDSDDPNFKPGDLISGITGWEEYSLIRSSDNQLRKIQLQDDIPLSYHLGLLGMAGFTAYAGFYEVCSPKKGDSVF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 147 VNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQ-KLGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGEFSNT 225
Cdd:PLN03154  164 VSAASGAVGQLVGQLAKLHGCYVVGSAGSSQKVDLLKnKLGFDEAFNYKEEPDLDAALKRYFPEGIDIYFDNVGGDMLDA 243
                         250
                  ....*....|....*...
gi 1034664465 226 VIGQMKKFGRIAICGAIS 243
Cdd:PLN03154  244 ALLNMKIHGRIAVCGMVS 261
ADH_N_2 pfam16884
N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin ...
5-105 2.16e-47

N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin reductase and alcohol dehydrogenase.


Pssm-ID: 465297 [Multi-domain]  Cd Length: 108  Bit Score: 152.74  E-value: 2.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465   5 KTWTLKKHFVGYPTNSDFELKTAELPPLKNGEVLLEALFLTVDPYMRVAAKRLKE-------GDTMMGQQVAKVVESKNV 77
Cdd:pfam16884   1 KQWLLAKRPEGVPTPSDFELVEAELPELGDGEVLVRTLYLSVDPYMRGRMNDAKSyvppvelGDVMRGGAVGEVVESNNP 80
                          90       100
                  ....*....|....*....|....*...
gi 1034664465  78 ALPKGTIVLASPGWTTHSISDGKDLEKL 105
Cdd:pfam16884  81 DFPVGDLVLGMLGWQDYAVSDGKGLTKV 108
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
84-206 2.43e-16

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 76.27  E-value: 2.43e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465   84 IVLASPGWTTHSISDgkdlEKLLTEWPDTIPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAK 163
Cdd:smart00829  51 MGLAPGAFATRVVTD----ARLVVPIPDGWSFEEA-ATVPVVFLTAYYALVDLARLRPGESVLIHAAAGGVGQAAIQLAR 125
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034664465  164 LKGCKVVGAVGSDEKVAYLQKLGFDV--VFNYKTVeSLEETLKKA 206
Cdd:smart00829 126 HLGAEVFATAGSPEKRDFLRALGIPDdhIFSSRDL-SFADEILRA 169
 
Name Accession Description Interval E-value
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
4-254 0e+00

leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase.


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 526.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465   4 TKTWTLKKHFVGYPTNSDFELKTAELPPLKNGEVLLEALFLTVDPYMRVAAKRLKEGDTMMGQQVAKVVESKNVALPKGT 83
Cdd:TIGR02825   1 AKTWTLKKHFVGYPTDSDFELKTVELPPLNNGEVLLEALFLSVDPYMRVAAKRLKEGDTMMGQQVARVVESKNVALPKGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  84 IVLASPGWTTHSISDGKDLEKLLTEWPDTIPLSLALGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAK 163
Cdd:TIGR02825  81 IVLASPGWTSHSISDGKDLEKLLTEWPDTLPLSLALGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 164 LKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAIS 243
Cdd:TIGR02825 161 LKGCKVVGAAGSDEKVAYLKKLGFDVAFNYKTVKSLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAIS 240
                         250
                  ....*....|.
gi 1034664465 244 TYNRTGPLPPG 254
Cdd:TIGR02825 241 TYNRTGPLPPG 251
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
2-253 5.06e-160

13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 hydroxydehydrogenase activity; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto- 13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176254 [Multi-domain]  Cd Length: 329  Bit Score: 446.71  E-value: 5.06e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465   2 VRTKTWTLKKHFVGYPTNSDFELKTAELPPLKNGEVLLEALFLTVDPYMRVAAKRLKEGDTMMGQQVAKVVESKNVALPK 81
Cdd:cd08294     1 VKAKTWVLKKHFDGKPKESDFELVEEELPPLKDGEVLCEALFLSVDPYMRPYSKRLNEGDTMIGTQVAKVIESKNSKFPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  82 GTIVLASPGWTTHSISDGK---DLEKLLTEWPDTIPLSLALGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVV 158
Cdd:cd08294    81 GTIVVASFGWRTHTVSDGKdqpDLYKLPADLPDDLPPSLALGVLGMPGLTAYFGLLEICKPKAGETVVVNGAAGAVGSLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 159 GQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVeSLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAI 238
Cdd:cd08294   161 GQIAKIKGCKVIGCAGSDDKVAWLKELGFDAVFNYKTV-SLEEALKEAAPDGIDCYFDNVGGEFSSTVLSHMNDFGRVAV 239
                         250
                  ....*....|....*
gi 1034664465 239 CGAISTYNRTGPLPP 253
Cdd:cd08294   240 CGSISTYNDKEPKKG 254
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
1-254 3.52e-119

NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 441733 [Multi-domain]  Cd Length: 333  Bit Score: 343.19  E-value: 3.52e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465   1 MVRTKTWTLKKHFVGYPTNSDFELKTAELPPLKNGEVLLEALFLTVDPYMRVaakRLKE----------GDTMMGQQVAK 70
Cdd:COG2130     2 MTTNRQIVLASRPEGEPTPEDFRLEEVPVPEPGDGEVLVRNLYLSVDPYMRG---RMSDaksyappvelGEVMRGGAVGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  71 VVESKNVALPKGTIVLASPGWTTHSISDGKDLEKLLtewPDTIPLSLALGTVGMPGLTAYFGLLEICGVKGGETVMVNAA 150
Cdd:COG2130    79 VVESRHPDFAVGDLVLGMLGWQDYAVSDGAGLRKVD---PSLAPLSAYLGVLGMPGLTAYFGLLDIGKPKAGETVVVSAA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 151 AGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYL-QKLGFDVVFNYKTvESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQ 229
Cdd:COG2130   156 AGAVGSVVGQIAKLKGCRVVGIAGGAEKCRYLvEELGFDAAIDYKA-GDLAAALAAACPDGIDVYFDNVGGEILDAVLPL 234
                         250       260
                  ....*....|....*....|....*
gi 1034664465 230 MKKFGRIAICGAISTYNRTGPlPPG 254
Cdd:COG2130   235 LNTFARIAVCGAISQYNATEP-PPG 258
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
4-253 1.53e-118

Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176190 [Multi-domain]  Cd Length: 329  Bit Score: 341.77  E-value: 1.53e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465   4 TKTWTLKKHFVGYPTNSDFELKTAELPPLKNGEVLLEALFLTVDPYMRV-------AAKRLKEGDTMMGQQVAKVVESKN 76
Cdd:cd05288     2 NRQVVLAKRPEGPPPPDDFELVEVPLPELKDGEVLVRTLYLSVDPYMRGwmsdaksYSPPVQLGEPMRGGGVGEVVESRS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  77 VALPKGTIVLASPGWTTHSISDG-KDLEKLLTEWPdtIPLSLALGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVG 155
Cdd:cd05288    82 PDFKVGDLVSGFLGWQEYAVVDGaSGLRKLDPSLG--LPLSAYLGVLGMTGLTAYFGLTEIGKPKPGETVVVSAAAGAVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 156 SVVGQIAKLKGCKVVGAVGSDEKVAYL-QKLGFDVVFNYKTvESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFG 234
Cdd:cd05288   160 SVVGQIAKLLGARVVGIAGSDEKCRWLvEELGFDAAINYKT-PDLAEALKEAAPDGIDVYFDNVGGEILDAALTLLNKGG 238
                         250
                  ....*....|....*....
gi 1034664465 235 RIAICGAISTYNRTGPLPP 253
Cdd:cd05288   239 RIALCGAISQYNATEPPGP 257
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
2-250 5.78e-82

Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This group includes proteins identified as the Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase. The Arabidopsis enzyme, a member of the medium chain dehydrogenase/reductase family, catalyzes the reduction of 7-8-double bond of phenylpropanal substrates as a plant defense mechanism. Prostaglandins and related eicosanoids (lipid mediators involved in host defense and inflamation) are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. Leukotriene B4 (LTB4) can be metabolized by LTB4 20-hydroxylase in inflamatory cells, and in other cells by bifunctional LTB4 12-HD/PGR. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176255 [Multi-domain]  Cd Length: 338  Bit Score: 248.77  E-value: 5.78e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465   2 VRTKTWTLKKHFVGYPTNSDFELKTAEL----PPLKNGEVLLEALFLTVDPYMRVAAKR---------LKEGDTMMGQQV 68
Cdd:cd08295     1 VRNKQVILKAYVTGFPKESDLELRTTKLtlkvPPGGSGDVLVKNLYLSCDPYMRGRMKGhddslylppFKPGEVITGYGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  69 AKVVESKNVALPKGTIVLASPGWTTHS-ISDGKDLEKLLtewPDTIPLSLALGTVGMPGLTAYFGLLEICGVKGGETVMV 147
Cdd:cd08295    81 AKVVDSGNPDFKVGDLVWGFTGWEEYSlIPRGQDLRKID---HTDVPLSYYLGLLGMPGLTAYAGFYEVCKPKKGETVFV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 148 NAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQ-KLGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGEFSNTV 226
Cdd:cd08295   158 SAASGAVGQLVGQLAKLKGCYVVGSAGSDEKVDLLKnKLGFDDAFNYKEEPDLDAALKRYFPNGIDIYFDNVGGKMLDAV 237
                         250       260
                  ....*....|....*....|....
gi 1034664465 227 IGQMKKFGRIAICGAISTYNRTGP 250
Cdd:cd08295   238 LLNMNLHGRIAACGMISQYNLEWP 261
PTGR2 cd08293
Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the ...
14-253 4.98e-71

Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176253 [Multi-domain]  Cd Length: 345  Bit Score: 221.11  E-value: 4.98e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  14 VGYPTNSDFELKTAELPP-LKNGEVLLEALFLTVDPYMRVaakRLKEG------------DTMMGQQVAKVVESKNVALP 80
Cdd:cd08293    15 NGNPVAENFRVEECTLPDeLNEGQVLVRTLYLSVDPYMRC---RMNEDtgtdylapwqlsQVLDGGGVGVVEESKHQKFA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  81 KGTIVlASPG--WTTHSISDGKDLEKLLTEWPDTIPlSLALGTVGMPGLTAYFGLLEICGVKGG--ETVMVNAAAGAVGS 156
Cdd:cd08293    92 VGDIV-TSFNwpWQTYAVLDGSSLEKVDPQLVDGHL-SYFLGAVGLPGLTALIGIQEKGHITPGanQTMVVSGAAGACGS 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 157 VVGQIAKLKGC-KVVGAVGSDEKVAYLQK-LGFDVVFNYKTvESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFG 234
Cdd:cd08293   170 LAGQIGRLLGCsRVVGICGSDEKCQLLKSeLGFDAAINYKT-DNVAERLRELCPEGVDVYFDNVGGEISDTVISQMNENS 248
                         250
                  ....*....|....*....
gi 1034664465 235 RIAICGAISTYNRTGPLPP 253
Cdd:cd08293   249 HIILCGQISQYNKDVPYPP 267
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
2-243 1.89e-59

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 191.59  E-value: 1.89e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465   2 VRTKTWTLKKHFVGYPTNSDFELKTAELPPLK----NGEVLLEALFLTVDPYMRvaaKRLKE-----------GDTMMGQ 66
Cdd:PLN03154    7 VENKQVILKNYIDGIPKETDMEVKLGNKIELKapkgSGAFLVKNLYLSCDPYMR---GRMRDfhdsylppfvpGQRIEGF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  67 QVAKVVESKNVALPKGTIVLASPGWTTHSISDGKDLEKLLTEWPDTIPLSLALGTVGMPGLTAYFGLLEICGVKGGETVM 146
Cdd:PLN03154   84 GVSKVVDSDDPNFKPGDLISGITGWEEYSLIRSSDNQLRKIQLQDDIPLSYHLGLLGMAGFTAYAGFYEVCSPKKGDSVF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 147 VNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQ-KLGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGEFSNT 225
Cdd:PLN03154  164 VSAASGAVGQLVGQLAKLHGCYVVGSAGSSQKVDLLKnKLGFDEAFNYKEEPDLDAALKRYFPEGIDIYFDNVGGDMLDA 243
                         250
                  ....*....|....*...
gi 1034664465 226 VIGQMKKFGRIAICGAIS 243
Cdd:PLN03154  244 ALLNMKIHGRIAVCGMVS 261
ADH_N_2 pfam16884
N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin ...
5-105 2.16e-47

N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin reductase and alcohol dehydrogenase.


Pssm-ID: 465297 [Multi-domain]  Cd Length: 108  Bit Score: 152.74  E-value: 2.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465   5 KTWTLKKHFVGYPTNSDFELKTAELPPLKNGEVLLEALFLTVDPYMRVAAKRLKE-------GDTMMGQQVAKVVESKNV 77
Cdd:pfam16884   1 KQWLLAKRPEGVPTPSDFELVEAELPELGDGEVLVRTLYLSVDPYMRGRMNDAKSyvppvelGDVMRGGAVGEVVESNNP 80
                          90       100
                  ....*....|....*....|....*...
gi 1034664465  78 ALPKGTIVLASPGWTTHSISDGKDLEKL 105
Cdd:pfam16884  81 DFPVGDLVLGMLGWQDYAVSDGKGLTKV 108
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
22-253 8.33e-35

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: 126.80  E-value: 8.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  22 FELKTAELPPLKNGEVLLEALFLTVDP---YMRVAAKRLKEGDTM-MGQQVAKVVES--KNVALPK-GTIVLASP---GW 91
Cdd:COG0604    15 LELEEVPVPEPGPGEVLVRVKAAGVNPadlLIRRGLYPLPPGLPFiPGSDAAGVVVAvgEGVTGFKvGDRVAGLGrggGY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  92 TTHSISDGKDLEKLltewPDTIPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVG 171
Cdd:COG0604    95 AEYVVVPADQLVPL----PDGLSFEEA-AALPLAGLTAWQALFDRGRLKPGETVLVHGAAGGVGSAAVQLAKALGARVIA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 172 AVGSDEKVAYLQKLGFDVVFNYKTvESLEETLKKAS-PDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAISTYNRTGP 250
Cdd:COG0604   170 TASSPEKAELLRALGADHVIDYRE-EDFAERVRALTgGRGVDVVLDTVGGDTLARSLRALAPGGRLVSIGAASGAPPPLD 248

                  ...
gi 1034664465 251 LPP 253
Cdd:COG0604   249 LAP 251
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
126-254 9.48e-33

Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of undetermined function. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176212 [Multi-domain]  Cd Length: 329  Bit Score: 121.60  E-value: 9.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 126 GLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTvESLEETLKK 205
Cdd:cd08250   124 GLTASIALEEVGEMKSGETVLVTAAAGGTGQFAVQLAKLAGCHVIGTCSSDEKAEFLKSLGCDRPINYKT-EDLGEVLKK 202
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034664465 206 ASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAISTY-NRTGPLPPG 254
Cdd:cd08250   203 EYPKGVDVVYESVGGEMFDTCVDNLALKGRLIVIGFISGYqSGTGPSPVK 252
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
90-246 2.64e-26

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 103.17  E-value: 2.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  90 GWTTHSISDGKDLEKLltewPDTIPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAaGAVGSVVGQIAKLKGCKV 169
Cdd:cd05188    88 GFAEYVVVPADNLVPL----PDGLSLEEA-ALLPEPLATAYHALRRAGVLKPGDTVLVLGA-GGVGLLAAQLAKAAGARV 161
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034664465 170 VGAVGSDEKVAYLQKLGFDVVFNYKTvESLEETLKKASPDGYDCYFDNVGGEFS-NTVIGQMKKFGRIAICGAISTYN 246
Cdd:cd05188   162 IVTDRSDEKLELAKELGADHVIDYKE-EDLEEELRLTGGGGADVVIDAVGGPETlAQALRLLRPGGRIVVVGGTSGGP 238
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
65-236 8.05e-25

Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176203 [Multi-domain]  Cd Length: 323  Bit Score: 100.27  E-value: 8.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  65 GQQVAKVVES---KNVALPKGTIVLASPGW---TTHSISDGKDLEKLltewPDTIPLSLALGtVGMPGLTAYFGLLEICG 138
Cdd:cd08241    62 GSEVAGVVEAvgeGVTGFKVGDRVVALTGQggfAEEVVVPAAAVFPL----PDGLSFEEAAA-LPVTYGTAYHALVRRAR 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 139 VKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKKASPDGYDCYFDNV 218
Cdd:cd08241   137 LQPGETVLVLGAAGGVGLAAVQLAKALGARVIAAASSEEKLALARALGADHVIDYRDPDLRERVKALTGGRGVDVVYDPV 216
                         170
                  ....*....|....*...
gi 1034664465 219 GGEFSNTVIGQMKKFGRI 236
Cdd:cd08241   217 GGDVFEASLRSLAWGGRL 234
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
115-252 1.33e-23

Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye lens protein with NADP-dependent quinone reductase activity (QOR). It has been cited as a structural component in mammalian eyes, but also has homology to quinone reductases in unrelated species. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176215 [Multi-domain]  Cd Length: 325  Bit Score: 96.88  E-value: 1.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 115 LSLALG-TVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNY 193
Cdd:cd08253   117 VSFEQGaALGIPALTAYRALFHRAGAKAGETVLVHGGSGAVGHAAVQLARWAGARVIATASSAEGAELVRQAGADAVFNY 196
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034664465 194 KTVESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAIcgaISTYNRTGPLP 252
Cdd:cd08253   197 RAEDLADRILAATAGQGVDVIIEVLANVNLAKDLDVLAPGGRIVV---YGSGGLRGTIP 252
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
127-253 1.65e-22

Alcohol dehydrogenases of the MDR family; This group contains proteins related to the zinc-dependent alcohol dehydrogenases. However, while the group has structural zinc site characteristic of these enzymes, it lacks the consensus site for a catalytic zinc. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 94.25  E-value: 1.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 127 LTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKKA 206
Cdd:cd08266   152 LTAWHMLVTRARLRPGETVLVHGAGSGVGSAAIQIAKLFGATVIATAGSEDKLERAKELGADYVIDYRKEDFVREVRELT 231
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034664465 207 SPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAIstynrTGPLPP 253
Cdd:cd08266   232 GKRGVDVVVEHVGAATWEKSLKSLARGGRLVTCGAT-----TGYEAP 273
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
22-253 3.31e-22

Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. 2-haloacrylate reductase, a member of this subgroup, catalyzes the NADPH-dependent reduction of a carbon-carbon double bond in organohalogen compounds. Although similar to QOR, Burkholderia 2-haloacrylate reductase does not act on the quinones 1,4-benzoquinone and 1,4-naphthoquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176189 [Multi-domain]  Cd Length: 320  Bit Score: 93.27  E-value: 3.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  22 FELKTAELPPLKNGEVLLEALFLTV---DPYMR--VAAKRLKEGdtmMGQQVAKVVE---SKNVALPKGT-IVLASPGWT 92
Cdd:cd05286    14 LEYEDVPVPEPGPGEVLVRNTAIGVnfiDTYFRsgLYPLPLPFV---LGVEGAGVVEavgPGVTGFKVGDrVAYAGPPGA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  93 --THSISDGKDLEKLltewPDTIPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVV 170
Cdd:cd05286    91 yaEYRVVPASRLVKL----PDGISDETA-AALLLQGLTAHYLLRETYPVKPGDTVLVHAAAGGVGLLLTQWAKALGATVI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 171 GAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAIStynrtGP 250
Cdd:cd05286   166 GTVSSEEKAELARAAGADHVINYRDEDFVERVREITGGRGVDVVYDGVGKDTFEGSLDSLRPRGTLVSFGNAS-----GP 240

                  ...
gi 1034664465 251 LPP 253
Cdd:cd05286   241 VPP 243
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
110-237 4.13e-22

alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176191 [Multi-domain]  Cd Length: 309  Bit Score: 92.62  E-value: 4.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 110 PDTIPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVgAVGSDEKVAYLQKLGFDV 189
Cdd:cd05289   114 PANLSFEEA-AALPLAGLTAWQALFELGGLKAGQTVLIHGAAGGVGSFAVQLAKARGARVI-ATASAANADFLRSLGADE 191
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1034664465 190 VFNYKTveslEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIA 237
Cdd:cd05289   192 VIDYTK----GDFERAAAPGGVDAVLDTVGGETLARSLALVKPGGRLV 235
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
127-240 1.99e-21

PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176180 [Multi-domain]  Cd Length: 323  Bit Score: 90.96  E-value: 1.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 127 LTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKKA 206
Cdd:cd05276   125 FTAWQNLFQLGGLKAGETVLIHGGASGVGTAAIQLAKALGARVIATAGSEEKLEACRALGADVAINYRTEDFAEEVKEAT 204
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034664465 207 SPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICG 240
Cdd:cd05276   205 GGRGVDVILDMVGGDYLARNLRALAPDGRLVLIG 238
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
153-244 7.77e-21

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 84.97  E-value: 7.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 153 AVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVG-GEFSNTVIGQMK 231
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSEEKLELAKELGADHVINPKETDLVEEIKELTGGKGVDVVFDCVGsPATLEQALKLLR 80
                          90
                  ....*....|...
gi 1034664465 232 KFGRIAICGAIST 244
Cdd:pfam00107  81 PGGRVVVVGLPGG 93
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
106-252 2.01e-20

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 88.42  E-value: 2.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 106 LTEWPDTIPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKL 185
Cdd:cd08268   110 VVKLPDGLSFVEA-AALWMQYLTAYGALVELAGLRPGDSVLITAASSSVGLAAIQIANAAGATVIATTRTSEKRDALLAL 188
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034664465 186 GFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAISTynRTGPLP 252
Cdd:cd08268   189 GAAHVIVTDEEDLVAEVLRITGGKGVDVVFDPVGGPQFAKLADALAPGGTLVVYGALSG--EPTPFP 253
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
103-221 2.66e-20

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 88.04  E-value: 2.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 103 EKLLTEWPDTIPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGaVGSDEKVAYL 182
Cdd:cd08267   106 ESGLAKKPEGVSFEEA-AALPVAGLTALQALRDAGKVKPGQRVLINGASGGVGTFAVQIAKALGAHVTG-VCSTRNAELV 183
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034664465 183 QKLGFDVVFNYKTVESLEETLKKASpdgYDCYFDNVGGE 221
Cdd:cd08267   184 RSLGADEVIDYTTEDFVALTAGGEK---YDVIFDAVGNS 219
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
126-241 4.18e-20

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 87.64  E-value: 4.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 126 GLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKgcKVVGAVG--SDEKVAYLQKLGFDVVFNYKTVESLEEtL 203
Cdd:cd08275   123 YLTAYYALFELGNLRPGQSVLVHSAAGGVGLAAGQLCKTV--PNVTVVGtaSASKHEALKENGVTHVIDYRTQDYVEE-V 199
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034664465 204 KKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGA 241
Cdd:cd08275   200 KKISPEGVDIVLDALGGEDTRKSYDLLKPMGRLVVYGA 237
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
15-244 1.52e-17

2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176645 [Multi-domain]  Cd Length: 323  Bit Score: 80.40  E-value: 1.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  15 GYPTNSDFELKTAELPPLKNGEVLLEALFLTVDP----YMRVAAKRLKEGDTMMGQQ-VAKVVE--SKNVALPKGTIVLA 87
Cdd:cd05282     7 GEPLPLVLELVSLPIPPPGPGEVLVRMLAAPINPsdliTISGAYGSRPPLPAVPGNEgVGVVVEvgSGVSGLLVGQRVLP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  88 SPG---WTTHSISDgkdlEKLLTEWPDTIPLSLALGTVGMPgLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKL 164
Cdd:cd05282    87 LGGegtWQEYVVAP----ADDLIPVPDSISDEQAAMLYINP-LTAWLMLTEYLKLPPGDWVIQNAANSAVGRMLIQLAKL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 165 KGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTvESLEETLKKAS-PDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAIS 243
Cdd:cd05282   162 LGFKTINVVRRDEQVEELKALGADEVIDSSP-EDLAQRVKEATgGAGARLALDAVGGESATRLARSLRPGGTLVNYGLLS 240

                  .
gi 1034664465 244 T 244
Cdd:cd05282   241 G 241
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
126-246 1.53e-17

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 80.30  E-value: 1.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 126 GLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVgAVGSDEKVAYLQKLGFDVVFNYKTvESLEETLKK 205
Cdd:cd08272   129 GITAWEGLVDRAAVQAGQTVLIHGGAGGVGHVAVQLAKAAGARVY-ATASSEKAAFARSLGADPIIYYRE-TVVEYVAEH 206
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1034664465 206 ASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAISTYN 246
Cdd:cd08272   207 TGGRGFDVVFDTVGGETLDASFEAVALYGRVVSILGGATHD 247
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
84-236 2.23e-17

enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176179 [Multi-domain]  Cd Length: 293  Bit Score: 79.54  E-value: 2.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  84 IVLASPGWTTHSISDGKDLEKLltewPDTIPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAK 163
Cdd:cd05195    56 MGLAPGAFATHVRVDARLVVKI----PDSLSFEEA-ATLPVAYLTAYYALVDLARLQKGESVLIHAAAGGVGQAAIQLAQ 130
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034664465 164 LKGCKVVGAVGSDEKVAYLQKLGFDV--VFNYKTVESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRI 236
Cdd:cd05195   131 HLGAEVFATVGSEEKREFLRELGGPVdhIFSSRDLSFADGILRATGGRGVDVVLNSLSGELLRASWRCLAPFGRF 205
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
110-242 2.45e-17

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 80.03  E-value: 2.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 110 PDTIPLS-LALGTVGMPGLTAYfGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVgAVGSDEKVAYLQKLGFD 188
Cdd:cd08274   146 PVNSPLSdVELATFPCSYSTAE-NMLERAGVGAGETVLVTGASGGVGSALVQLAKRRGAIVI-AVAGAAKEEAVRALGAD 223
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034664465 189 VVfnYKTVESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAI 242
Cdd:cd08274   224 TV--ILRDAPLLADAKALGGEPVDVVADVVGGPLFPDLLRLLRPGGRYVTAGAI 275
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
23-223 7.29e-17

2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 78.42  E-value: 7.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  23 ELKTAELPPLK-NGEVLLEALFLTVDP---------YMRVAAKRLK-------EGdtmmgqqVAKVVES-KNV-ALPKGT 83
Cdd:cd08290    17 QLESYEIPPPGpPNEVLVKMLAAPINPadinqiqgvYPIKPPTTPEppavggnEG-------VGEVVKVgSGVkSLKPGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  84 IVL-ASPG---WTTHSISDGKDLEKLltewPDTIPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVG 159
Cdd:cd08290    90 WVIpLRPGlgtWRTHAVVPADDLIKV----PNDVDPEQA-ATLSVNPCTAYRLLEDFVKLQPGDWVIQNGANSAVGQAVI 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 160 QIAKLKGCKVVGAV----GSDEKVAYLQKLGFDVVFNYKTVESLE--ETLKKASPDGYDCYFDNVGGEFS 223
Cdd:cd08290   165 QLAKLLGIKTINVVrdrpDLEELKERLKALGADHVLTEEELRSLLatELLKSAPGGRPKLALNCVGGKSA 234
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
106-243 1.78e-16

Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176206 [Multi-domain]  Cd Length: 324  Bit Score: 77.41  E-value: 1.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 106 LTEWPDTIPLSLALgTVGMPGLTAyFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKL 185
Cdd:cd08244   109 LHPVPDGLDLEAAV-AVVHDGRTA-LGLLDLATLTPGDVVLVTAAAGGLGSLLVQLAKAAGATVVGAAGGPAKTALVRAL 186
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034664465 186 GFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAIS 243
Cdd:cd08244   187 GADVAVDYTRPDWPDQVREALGGGGVTVVLDGVGGAIGRAALALLAPGGRFLTYGWAS 244
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
22-237 2.24e-16

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 76.93  E-value: 2.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  22 FELKTAELPPLKNGEVLLEALFLTVDPymrVAAKRLKEG------DTMMGQQVAKVVES--KNVALPK-GTIVLASPGWT 92
Cdd:cd08271    15 LTLEEIEIPGPGAGEVLVKVHAAGLNP---VDWKVIAWGppawsyPHVPGVDGAGVVVAvgAKVTGWKvGDRVAYHASLA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  93 TH------SISDGKDLEKLltewPDTIPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKG 166
Cdd:cd08271    92 RGgsfaeyTVVDARAVLPL----PDSLSFEEA-AALPCAGLTAYQALFKKLRIEAGRTILITGGAGGVGSFAVQLAKRAG 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034664465 167 cKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIA 237
Cdd:cd08271   167 -LRVITTCSKRNFEYVKSLGADHVIDYNDEDVCERIKEITGGRGVDAVLDTVGGETAAALAPTLAFNGHLV 236
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
84-206 2.43e-16

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 76.27  E-value: 2.43e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465   84 IVLASPGWTTHSISDgkdlEKLLTEWPDTIPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAK 163
Cdd:smart00829  51 MGLAPGAFATRVVTD----ARLVVPIPDGWSFEEA-ATVPVVFLTAYYALVDLARLRPGESVLIHAAAGGVGQAAIQLAR 125
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034664465  164 LKGCKVVGAVGSDEKVAYLQKLGFDV--VFNYKTVeSLEETLKKA 206
Cdd:smart00829 126 HLGAEVFATAGSPEKRDFLRALGIPDdhIFSSRDL-SFADEILRA 169
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
106-254 2.21e-13

2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176252 [Multi-domain]  Cd Length: 324  Bit Score: 68.51  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 106 LTEWPDTIPLSLALGTVGMPgLTAYFgLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKL 185
Cdd:cd08292   106 LVPLPDGISDEVAAQLIAMP-LSALM-LLDFLGVKPGQWLIQNAAGGAVGKLVAMLAAARGINVINLVRRDAGVAELRAL 183
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 186 GFDVVFNyKTVESLEETLKKASPDGYDCY-FDNVGGEFSNTVIGQMKKFGRIAICGAIStyNRTGPLPPG 254
Cdd:cd08292   184 GIGPVVS-TEQPGWQDKVREAAGGAPISVaLDSVGGKLAGELLSLLGEGGTLVSFGSMS--GEPMQISSG 250
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
127-220 1.66e-12

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 66.21  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 127 LTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKKA 206
Cdd:PTZ00354  126 LTAWQLLKKHGDVKKGQSVLIHAGASGVGTAAAQLAEKYGAATIITTSSEEKVDFCKKLAAIILIRYPDEEGFAPKVKKL 205
                          90
                  ....*....|....*
gi 1034664465 207 -SPDGYDCYFDNVGG 220
Cdd:PTZ00354  206 tGEKGVNLVLDCVGG 220
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
103-254 7.09e-12

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group contains proteins that share the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenase family. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176220 [Multi-domain]  Cd Length: 332  Bit Score: 64.26  E-value: 7.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 103 EKLLTEWPDTIPL-SLALgtVGMPGLTAYFGLlEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAY 181
Cdd:cd08259   126 ERSLVKLPDNVSDeSAAL--AACVVGTAVHAL-KRAGVKKGDTVLVTGAGGGVGIHAIQLAKALGARVIAVTRSPEKLKI 202
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034664465 182 LQKLGFDVVFNYKtveSLEETLKKASpdGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGaistyNRTG---PLPPG 254
Cdd:cd08259   203 LKELGADYVIDGS---KFSEDVKKLG--GADVVIELVGSPTIEESLRSLNKGGRLVLIG-----NVTPdpaPLRPG 268
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
126-235 1.10e-11

polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176213 [Multi-domain]  Cd Length: 303  Bit Score: 63.60  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 126 GLTAYFGLlEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKK 205
Cdd:cd08251   106 FLTVIDAF-ARAGLAKGEHILIQTATGGTGLMAVQLARLKGAEIYATASSDDKLEYLKQLGVPHVINYVEEDFEEEIMRL 184
                          90       100       110
                  ....*....|....*....|....*....|
gi 1034664465 206 ASPDGYDCYFDNVGGEFSNTVIGQMKKFGR 235
Cdd:cd08251   185 TGGRGVDVVINTLSGEAIQKGLNCLAPGGR 214
PRK10754 PRK10754
NADPH:quinone reductase;
110-204 5.31e-11

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 61.67  E-value: 5.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 110 PDTIPLSLALGTVgMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDV 189
Cdd:PRK10754  110 PDAISFEQAAASF-LKGLTVYYLLRKTYEIKPDEQFLFHAAAGGVGLIACQWAKALGAKLIGTVGSAQKAQRAKKAGAWQ 188
                          90
                  ....*....|....*
gi 1034664465 190 VFNYKTvESLEETLK 204
Cdd:PRK10754  189 VINYRE-ENIVERVK 202
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
126-253 7.33e-11

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 61.40  E-value: 7.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 126 GLTAYFGLLEICGVKGGETVMVNAAaGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKK 205
Cdd:cd08276   145 GLTAWNALFGLGPLKPGDTVLVQGT-GGVSLFALQFAKAAGARVIATSSSDEKLERAKALGADHVINYRTTPDWGEEVLK 223
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1034664465 206 ASPD-GYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAISTYNRTGPLPP 253
Cdd:cd08276   224 LTGGrGVDHVVEVGGPGTLAQSIKAVAPGGVISLIGFLSGFEAPVLLLP 272
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
86-240 1.92e-10

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 60.15  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  86 LASPGWTTHSISDGKDLEKL-LTEwpdtiPLSlalgtvgmpglTAYFGLlEICGVKGGETVMVnAAAGAVGSVVGQIAKL 164
Cdd:COG1063   122 VRVPAANLVKVPDGLSDEAAaLVE-----PLA-----------VALHAV-ERAGVKPGDTVLV-IGAGPIGLLAALAARL 183
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034664465 165 KGCKVVGAVG-SDEKVAYLQKLGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGEFS-NTVIGQMKKFGRIAICG 240
Cdd:COG1063   184 AGAARVIVVDrNPERLELARELGADAVVNPREEDLVEAVRELTGGRGADVVIEAVGAPAAlEQALDLVRPGGTVVLVG 261
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
126-234 2.17e-10

Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member of the medium chain dehydrogenase/ reductase (MDR) family. Riticulons are endoplasmic reticulum associated proteins involved in membrane trafficking and neuroendocrine secretion. The MDR/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 59.93  E-value: 2.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 126 GLTAYFGLLEICGVKGGET----VMVNAAAGAVGSVVGQIAKLKGCKVVgAVGSDEKVAYLQKLGFDVVFNYKTvESLEE 201
Cdd:cd08248   143 GLTAWSALVNVGGLNPKNAagkrVLILGGSGGVGTFAIQLLKAWGAHVT-TTCSTDAIPLVKSLGADDVIDYNN-EDFEE 220
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1034664465 202 TLKkaSPDGYDCYFDNVGGEFSNTVIGQMKKFG 234
Cdd:cd08248   221 ELT--ERGKFDVILDTVGGDTEKWALKLLKKGG 251
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
127-243 8.19e-10

2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176251 [Multi-domain]  Cd Length: 324  Bit Score: 58.00  E-value: 8.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 127 LTAyFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNyKTVESLEETLKKA 206
Cdd:cd08291   130 LTA-LGMLETAREEGAKAVVHTAAASALGRMLVRLCKADGIKVINIVRRKEQVDLLKKIGAEYVLN-SSDPDFLEDLKEL 207
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034664465 207 SPD-GYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAIS 243
Cdd:cd08291   208 IAKlNATIFFDAVGGGLTGQILLAMPYGSTLYVYGYLS 245
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
121-240 1.61e-09

Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176183 [Multi-domain]  Cd Length: 325  Bit Score: 57.17  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 121 TVGMPGLTAyfGL----LEICGVKG--GEtVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNyk 194
Cdd:cd05280   123 ILGTAGFTA--ALsvhrLEDNGQTPedGP-VLVTGATGGVGSIAVAILAKLGYTVVALTGKEEQADYLKSLGASEVLD-- 197
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034664465 195 tVESLEETLKKA-SPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICG 240
Cdd:cd05280   198 -REDLLDESKKPlLKARWAGAIDTVGGDVLANLLKQTKYGGVVASCG 243
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
71-240 2.34e-09

putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of pfam00107 as defined by Pfam, a superfamily in which some members are zinc-binding medium-chain alcohol dehydrogenases while others are quinone oxidoreductases with no bound zinc. This subfamily includes proteins studied crystallographically for insight into function: YhdH from Escherichia coli and YhfP from Bacillus subtilis. Members bind NADPH or NAD, but not zinc. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274315 [Multi-domain]  Cd Length: 323  Bit Score: 56.80  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  71 VVESKNVALPKGTIVLASpGWTTHSISDG--KDLEKLLTEW----PDTIPL--SLALGTVGmpgLTAYFGL--LEICGVK 140
Cdd:TIGR02823  68 VVSSEDPRFREGDEVIVT-GYGLGVSHDGgySQYARVPADWlvplPEGLSLreAMALGTAG---FTAALSVmaLERNGLT 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 141 GGE-TVMVNAAAGAVGSV-VGQIAKLkGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKKASPDGYdcyFDNV 218
Cdd:TIGR02823 144 PEDgPVLVTGATGGVGSLaVAILSKL-GYEVVASTGKAEEEDYLKELGASEVIDREDLSPPGKPLEKERWAGA---VDTV 219
                         170       180
                  ....*....|....*....|..
gi 1034664465 219 GGEFSNTVIGQMKKFGRIAICG 240
Cdd:TIGR02823 220 GGHTLANVLAQLKYGGAVAACG 241
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
110-252 3.86e-09

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 56.27  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 110 PDTIPLSLAlGTVGMPGLTAYFGLlEICGVKGGETVMVNAAaGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDV 189
Cdd:COG1064   133 PDGLDPAEA-APLLCAGITAYRAL-RRAGVGPGDRVAVIGA-GGLGHLAVQIAKALGAEVIAVDRSPEKLELARELGADH 209
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034664465 190 VFNYKTVESLEETlkkASPDGYDCYFDNVGGEFS-NTVIGQMKKFGRIAICGAIstynrTGPLP 252
Cdd:COG1064   210 VVNSSDEDPVEAV---RELTGADVVIDTVGAPATvNAALALLRRGGRLVLVGLP-----GGPIP 265
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
110-221 4.64e-09

Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (aka ADH3) may be the ancestral form of alcohol dehydrogenase, which evolved to detoxify formaldehyde. This CD contains glutathione dependant FDH, glutathione independent FDH, and related alcohol dehydrogenases. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 55.74  E-value: 4.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 110 PDTIPL--SLALGTVgMPglTAYFGLlEICGVKGGETVMVnAAAGAVGSVVGQIAKLKGCKVVGAVGSD-EKVAYLQKLG 186
Cdd:cd05278   138 PDGLPDedALMLSDI-LP--TGFHGA-ELAGIKPGSTVAV-IGAGPVGLCAVAGARLLGAARIIAVDSNpERLDLAKEAG 212
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034664465 187 FDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGE 221
Cdd:cd05278   213 ATDIINPKNGDIVEQILELTGGRGVDCVIEAVGFE 247
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
110-210 6.70e-09

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 55.23  E-value: 6.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 110 PDTIPLSLAlGTVGMPGLTAYFGLLEiCGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDV 189
Cdd:cd08297   136 PDGLSFEQA-APLLCAGVTVYKALKK-AGLKPGDWVVISGAGGGLGHLGVQYAKAMGLRVIAIDVGDEKLELAKELGADA 213
                          90       100
                  ....*....|....*....|.
gi 1034664465 190 VFNYKTVESLEETLKKASPDG 210
Cdd:cd08297   214 FVDFKKSDDVEAVKELTGGGG 234
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
107-243 7.44e-09

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 55.07  E-value: 7.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 107 TEWPDTIPLSLALG---TVGMPGLTAYFGLLEICGVKGGEtVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQ 183
Cdd:cd08270    96 TGWLAVLPDGVSFAqaaTLPVAGVTALRALRRGGPLLGRR-VLVTGASGGVGRFAVQLAALAGAHVVAVVGSPARAEGLR 174
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 184 KLGFDVVfnyktVESLEEtlkkASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAIS 243
Cdd:cd08270   175 ELGAAEV-----VVGGSE----LSGAPVDLVVDSVGGPQLARALELLAPGGTVVSVGSSS 225
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
11-240 5.16e-08

Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176249 [Multi-domain]  Cd Length: 326  Bit Score: 52.71  E-value: 5.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  11 KHFVGYPTNSDFELKTAELPP--LKNGEVLLEALFLTV---DPYMRVAAKRL-KEGDTMMGQQVA-KVVESKNVALPKGT 83
Cdd:cd08289     2 QALVVEKDEDDVSVSVKNLTLddLPEGDVLIRVAYSSVnykDGLASIPGGKIvKRYPFIPGIDLAgTVVESNDPRFKPGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  84 IVLAspgwTTHSISDGKD-----LEKLLTEW----PDTIPL--SLALGTVGmpgLTAYFGL--LEICGV--KGGEtVMVN 148
Cdd:cd08289    82 EVIV----TSYDLGVSHHggyseYARVPAEWvvplPKGLTLkeAMILGTAG---FTAALSIhrLEENGLtpEQGP-VLVT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 149 AAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKtvESLEETLKKASPDGYDCYFDNVGGEFSNTVIG 228
Cdd:cd08289   154 GATGGVGSLAVSILAKLGYEVVASTGKADAADYLKKLGAKEVIPRE--ELQEESIKPLEKQRWAGAVDPVGGKTLAYLLS 231
                         250
                  ....*....|..
gi 1034664465 229 QMKKFGRIAICG 240
Cdd:cd08289   232 TLQYGGSVAVSG 243
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
110-213 6.29e-08

enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176211 [Multi-domain]  Cd Length: 339  Bit Score: 52.59  E-value: 6.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 110 PDTIP------LSLALGTVGMpGLTAYFGL----LEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVgAVGSDEKV 179
Cdd:cd08249   114 PDNISfeeaatLPVGLVTAAL-ALFQKLGLplppPKPSPASKGKPVLIWGGSSSVGTLAIQLAKLAGYKVI-TTASPKNF 191
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1034664465 180 AYLQKLGFDVVFNYKTVESLEETLKKASPD---GYDC 213
Cdd:cd08249   192 DLVKSLGADAVFDYHDPDVVEDIRAATGGKlryALDC 228
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
106-252 1.76e-07

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176224 [Multi-domain]  Cd Length: 367  Bit Score: 51.22  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 106 LTEWPDTIPLSlALGTVGMPGLTAYFGLLEICGVKGGETVMVnAAAGAVGSVVGQIAKLKGCKVVGAVG-SDEKVAYLQK 184
Cdd:cd08263   153 LAPLPESLDYT-ESAVLGCAGFTAYGALKHAADVRPGETVAV-IGVGGVGSSAIQLAKAFGASPIIAVDvRDEKLAKAKE 230
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034664465 185 LGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGG-EFSNTVIGQMKKFGRIAICGaISTYNRTGPLP 252
Cdd:cd08263   231 LGATHTVNAAKEDAVAAIREITGGRGVDVVVEALGKpETFKLALDVVRDGGRAVVVG-LAPGGATAEIP 298
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
128-240 1.90e-07

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176243 [Multi-domain]  Cd Length: 386  Bit Score: 51.00  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 128 TAYFGLlEICGVKGGETVMVnAAAGAVGSVVGQIAKLKGCKVVGAVgsdEKVAY-L----QKLGFDVVfNYKTVESLEET 202
Cdd:cd08283   172 TGYHAA-ELAEVKPGDTVAV-WGCGPVGLFAARSAKLLGAERVIAI---DRVPErLemarSHLGAETI-NFEEVDDVVEA 245
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034664465 203 LKKASP-DGYDCYFDNVGGEFSNTVIGQM----------------------KKFGRIAICG 240
Cdd:cd08283   246 LRELTGgRGPDVCIDAVGMEAHGSPLHKAeqallkletdrpdalreaiqavRKGGTVSIIG 306
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
82-221 3.80e-07

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 49.95  E-value: 3.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  82 GTIVLASP---GWTTHSISDGKDLEKLltewPDTIPLSLAlgtVGMP--GLTAYfGLLEICG-VKGGETVMVNAAAGAVG 155
Cdd:cd08273    82 GDRVAALTrvgGNAEYINLDAKYLVPV----PEGVDAAEA---VCLVlnYVTAY-QMLHRAAkVLTGQRVLIHGASGGVG 153
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034664465 156 SVVGQIAKLKGCKVVGAVgSDEKVAYLQKLGfDVVFNYKTVESLEETLkkaSPDGYDCYFDNVGGE 221
Cdd:cd08273   154 QALLELALLAGAEVYGTA-SERNHAALRELG-ATPIDYRTKDWLPAML---TPGGVDVVFDGVGGE 214
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
53-233 5.05e-07

AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group contains members identified in targeting of yeast membrane proteins ATPase. AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast, identified as a multicopy suppressor of pma1 mutants which cause temperature sensitive growth arrest due to the inability of ATPase to target to the cell surface. This family is homologous to the medium chain family of dehydrogenases and reductases. Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176209 [Multi-domain]  Cd Length: 352  Bit Score: 49.96  E-value: 5.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  53 AAKRLKEGDTMMGQQVAkvvesknVALPKGTIvlaspgwTTHSISDGKDLEKLLTEWPDTIPLSLALGTVGMPGlTAYfG 132
Cdd:cd08247    77 VASEWKVGDEVCGIYPH-------PYGGQGTL-------SQYLLVDPKKDKKSITRKPENISLEEAAAWPLVLG-TAY-Q 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 133 LLEICGVKGGET--VMVNAAAGAVGSVVGQIAK--LKGCKVVGaVGSDEKVAYLQKLGFDVVFNY---KTVESLEETLKK 205
Cdd:cd08247   141 ILEDLGQKLGPDskVLVLGGSTSVGRFAIQLAKnhYNIGTVVG-TCSSRSAELNKKLGADHFIDYdahSGVKLLKPVLEN 219
                         170       180
                  ....*....|....*....|....*....
gi 1034664465 206 ASPDG-YDCYFDNVGGefsNTVIGQMKKF 233
Cdd:cd08247   220 VKGQGkFDLILDCVGG---YDLFPHINSI 245
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
124-212 1.16e-06

Arginate lyase and other MDR family members; This group contains a structure identified as an arginate lyase. Other members are identified quinone reductases, alginate lyases, and other proteins related to the zinc-dependent dehydrogenases/reductases. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 48.68  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 124 MP--GLTAYFGLLEICGVK-----GGETVMVNAAAGAVGSVVGQIAK-LKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKt 195
Cdd:cd08252   125 LPltSLTAWEALFDRLGISedaenEGKTLLIIGGAGGVGSIAIQLAKqLTGLTVIATASRPESIAWVKELGADHVINHH- 203
                          90
                  ....*....|....*..
gi 1034664465 196 vESLEETLKKASPDGYD 212
Cdd:cd08252   204 -QDLAEQLEALGIEPVD 219
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
128-242 1.24e-06

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 48.49  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 128 TAYFGLLEIcGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKtvesLEETLKKAS 207
Cdd:PRK13771  150 MVYRGLRRA-GVKKGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSSESKAKIVSKYADYVIVGSK----FSEEVKKIG 224
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034664465 208 pdGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAI 242
Cdd:PRK13771  225 --GADIVIETVGTPTLEESLRSLNMGGKIIQIGNV 257
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
86-240 2.51e-06

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 47.61  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  86 LASPGWTTHSISDGKDLEKL-LTEwpdtiPLSLALGTVGMPGLTAyfglleicgvkgGETVMVnAAAGAVGSVVGQIAKL 164
Cdd:cd08236   120 VSVPARNLIKIPDHVDYEEAaMIE-----PAAVALHAVRLAGITL------------GDTVVV-IGAGTIGLLAIQWLKI 181
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034664465 165 KGCKVVGAVG-SDEKVAYLQKLGFDVVFNYKTvESLEETLKKASPDGYDCYFDNVG-GEFSNTVIGQMKKFGRIAICG 240
Cdd:cd08236   182 LGAKRVIAVDiDDEKLAVARELGADDTINPKE-EDVEKVRELTEGRGADLVIEAAGsPATIEQALALARPGGKVVLVG 258
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
138-219 6.85e-06

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 46.41  E-value: 6.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 138 GVKGGETVMVnAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKKASPDGYDCYFDN 217
Cdd:cd08261   156 GVTAGDTVLV-VGAGPIGLGVIQVAKARGARVIVVDIDDERLEFARELGADDTINVGDEDVAARLRELTDGEGADVVIDA 234

                  ..
gi 1034664465 218 VG 219
Cdd:cd08261   235 TG 236
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
17-242 8.83e-06

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase family. However, this subgroup does not contain the characteristic catalytic zinc site. Also, it contains an atypical structural zinc-binding pattern: DxxCxxCxxxxxxxC. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176225 [Multi-domain]  Cd Length: 325  Bit Score: 46.19  E-value: 8.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  17 PTNSDFELKTAELPPLKNGEVLLEALFLTVDP--YMRVAAKRLKEGDTMMGQQVAKVVE--SKNVALPK----------- 81
Cdd:cd08264     9 SGIENLKVEDVKDPKPGPGEVLIRVKMAGVNPvdYNVINAVKVKPMPHIPGAEFAGVVEevGDHVKGVKkgdrvvvynrv 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  82 ------------------GTI--VLASPGWTTHSISDGKDLEKLltewPDTIPLSLAlGTVGMPGLTAYFGLLEIcGVKG 141
Cdd:cd08264    89 fdgtcdmclsgnemlcrnGGIigVVSNGGYAEYIVVPEKNLFKI----PDSISDELA-ASLPVAALTAYHALKTA-GLGP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 142 GETVMVNAAAGAVGSVVGQIAKLKGCKVVgAVGSDEkvaYLQKLGFDVVFNYKTV-ESLEETLKKAspdgyDCYFDNVGG 220
Cdd:cd08264   163 GETVVVFGASGNTGIFAVQLAKMMGAEVI-AVSRKD---WLKEFGADEVVDYDEVeEKVKEITKMA-----DVVINSLGS 233
                         250       260
                  ....*....|....*....|..
gi 1034664465 221 EFSNTVIGQMKKFGRIAICGAI 242
Cdd:cd08264   234 SFWDLSLSVLGRGGRLVTFGTL 255
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
127-219 1.98e-05

Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 44.91  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 127 LTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFnyktVE--SLEETLK 204
Cdd:cd08243   128 YTAWGSLFRSLGLQPGDTLLIRGGTSSVGLAALKLAKALGATVTATTRSPERAALLKELGADEVV----IDdgAIAEQLR 203
                          90
                  ....*....|....*
gi 1034664465 205 KAsPDGYDCYFDNVG 219
Cdd:cd08243   204 AA-PGGFDKVLELVG 217
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
106-219 3.56e-05

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 44.13  E-value: 3.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 106 LTEWPDTIPLSLALGTvGMPGLTAYFGLLEICGVKGGETVMVNAAAGaVG-SVVgQIAKLKGCKVVGAVGSDEKVAYLQK 184
Cdd:cd08260   131 LVRLPDDVDFVTAAGL-GCRFATAFRALVHQARVKPGEWVAVHGCGG-VGlSAV-MIASALGARVIAVDIDDDKLELARE 207
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034664465 185 LGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVG 219
Cdd:cd08260   208 LGAVATVNASEVEDVAAAVRDLTGGGAHVSVDALG 242
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
126-219 4.56e-05

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 43.77  E-value: 4.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 126 GLTAYFGLLEICGVKGGETVMVnAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEEtLKK 205
Cdd:cd08254   150 VLTPYHAVVRAGEVKPGETVLV-IGLGGLGLNAVQIAKAMGAAVIAVDIKEEKLELAKELGADEVLNSLDDSPKDK-KAA 227
                          90
                  ....*....|....
gi 1034664465 206 ASPDGYDCYFDNVG 219
Cdd:cd08254   228 GLGGGFDVIFDFVG 241
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
138-248 7.62e-05

crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase/reductase family, catalyzes the NADPH-dependent conversion of crotonyl-CoA to butyryl-CoA, a step in (2S)-methylmalonyl-CoA production for straight-chain fatty acid biosynthesis. Like enoyl reductase, another enzyme in fatty acid synthesis, crotonyl-CoA reductase is a member of the zinc-dependent alcohol dehydrogenase-like medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 43.17  E-value: 7.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 138 GVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLG---------FDVVFNYKTVESLEET--LKKA 206
Cdd:cd08246   190 TVKPGDNVLIWGASGGLGSMAIQLARAAGANPVAVVSSEEKAEYCRALGaegvinrrdFDHWGVLPDVNSEAYTawTKEA 269
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034664465 207 ------------SPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAISTYNRT 248
Cdd:cd08246   270 rrfgkaiwdilgGREDPDIVFEHPGRATFPTSVFVCDRGGMVVICAGTTGYNHT 323
MDR_yhdh cd08288
Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR ...
118-240 1.26e-04

Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176248 [Multi-domain]  Cd Length: 324  Bit Score: 42.52  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 118 ALGTvgmPGLTAYFGL--LEICGVK-GGETVMVNAAAGAVGSV-VGQIAKLkGCKVVGAVGSDEKVAYLQKLGFDVVFNY 193
Cdd:cd08288   123 AIGT---AGFTAMLCVmaLEDHGVTpGDGPVLVTGAAGGVGSVaVALLARL-GYEVVASTGRPEEADYLRSLGASEIIDR 198
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034664465 194 KTVESLEETLKKASpdgYDCYFDNVGGEFSNTVIGQMKKFGRIAICG 240
Cdd:cd08288   199 AELSEPGRPLQKER---WAGAVDTVGGHTLANVLAQTRYGGAVAACG 242
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
110-240 1.07e-03

6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the zinc-dependent alcohol dehydrogenase-like family of medium chain dehydrogenases/reductases catalyzes the conversion of 6-hydroxyhexanoate and NAD(+) to 6-oxohexanoate + NADH and H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176202 [Multi-domain]  Cd Length: 350  Bit Score: 39.52  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 110 PDTIPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVnAAAGAVGSVVGQIAK-LKGCKVVGAVGSDEKVAYLQKLGFD 188
Cdd:cd08240   145 PGGLDPALA-ATLACSGLTAYSAVKKLMPLVADEPVVI-IGAGGLGLMALALLKaLGPANIIVVDIDEAKLEAAKAAGAD 222
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034664465 189 VVFNYKTVESLEEtLKKASPDGYDCYFDNVGGEFSNTVIGQ-MKKFGRIAICG 240
Cdd:cd08240   223 VVVNGSDPDAAKR-IIKAAGGGVDAVIDFVNNSATASLAFDiLAKGGKLVLVG 274
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
68-254 1.23e-03

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 39.18  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465  68 VAKVVES-KNVALPK-GTIVlASPGWT-THSISDGKDLEKLltewPDTIPLSLA-LGTVGMpglTAYFGLLeICGVKGGE 143
Cdd:cd08255    29 VGRVVEVgSGVTGFKpGDRV-FCFGPHaERVVVPANLLVPL----PDGLPPERAaLTALAA---TALNGVR-DAEPRLGE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 144 TVMVnAAAGAVGSVVGQIAKLKGCKVVGAVG-SDEKVAYLQKLGFDvvfnYKTVESLEETLkkaSPDGYDCYFDnVGGEF 222
Cdd:cd08255   100 RVAV-VGLGLVGLLAAQLAKAAGAREVVGVDpDAARRELAEALGPA----DPVAADTADEI---GGRGADVVIE-ASGSP 170
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034664465 223 S--NTVIGQMKKFGRIAICGaistYNRTGPLPPG 254
Cdd:cd08255   171 SalETALRLLRDRGRVVLVG----WYGLKPLLLG 200
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
126-205 3.31e-03

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 38.09  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 126 GLTAYFGLlEICGVKGGETVMVnAAAGAVGSVVGQIAK-LKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLK 204
Cdd:PRK09422  148 GVTTYKAI-KVSGIKPGQWIAI-YGAGGLGNLALQYAKnVFNAKVIAVDINDDKLALAKEVGADLTINSKRVEDVAKIIQ 225

                  .
gi 1034664465 205 K 205
Cdd:PRK09422  226 E 226
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
143-219 4.42e-03

Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenases of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176218 [Multi-domain]  Cd Length: 350  Bit Score: 37.77  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 143 ETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVG-SDEKVAYLQKLGFDVVFNYKTVESLEETLKKAspDGYDC--YFDNVG 219
Cdd:cd08256   175 DDVVVLAGAGPLGLGMIGAARLKNPKKLIVLDlKDERLALARKFGADVVLNPPEVDVVEKIKELT--GGYGCdiYIEATG 252
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
110-241 7.54e-03

Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes, or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176207 [Multi-domain]  Cd Length: 330  Bit Score: 36.92  E-value: 7.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664465 110 PDTIPLSLAlGTVGMPGLTAYFGLlEICGVKGGETVMVnAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDV 189
Cdd:cd08245   133 PDGLPLAQA-APLLCAGITVYSAL-RDAGPRPGERVAV-LGIGGLGHLAVQYARAMGFETVAITRSPDKRELARKLGADE 209
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034664465 190 VfnyktVESLEETLKKASPDGYDCYFDNV-GGEFSNTVIGQMKKFGRIAICGA 241
Cdd:cd08245   210 V-----VDSGAELDEQAAAGGADVILVTVvSGAAAEAALGGLRRGGRIVLVGL 257
 
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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