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Conserved domains on  [gi|332646003|gb|AEE79524|]
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GroES-like zinc-binding alcohol dehydrogenase family protein [Arabidopsis thaliana]

Protein Classification

NADPH:quinone oxidoreductase family protein( domain architecture ID 10169523)

NADPH:quinone oxidoreductase family protein, similar to Thermus thermophilus quinone oxidoreductase which catalyzes the NADPH-dependent reduction of p-benzoquinone

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
1-336 2.88e-142

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: 405.34  E-value: 2.88e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGDPTAtnpgspespVEVSKTHPIPSLnsDTSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIV 80
Cdd:cd08241    1 MKAVVCKELGGPED---------LVLEEVPPEPGA--PGEVRIRVEAAGVNFPDLLMIQGKYQVKPPLPFVPGSEVAGVV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  81 DAIGPAVTKFRVGDRVCSFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAA 160
Cdd:cd08241   70 EAVGEGVTGFKVGDRVVALTGQGGFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALVRRARLQPGETVLVLGAA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 161 GGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVGGKLTKESMK 240
Cdd:cd08241  150 GGVGLAAVQLAKALGARVIAAASSEEKLALARALGADHVIDYRDPDLRERVKALTGGR---GVDVVYDPVGGDVFEASLR 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 241 VLKWGAQILVIGFASGEIPVIPANIALVKNWTVHGLYWGSYRIHQPNVLEDSIKELLSWLSRGLITIHISHTYSLSQANL 320
Cdd:cd08241  227 SLAWGGRLLVIGFASGEIPQIPANLLLLKNISVVGVYWGAYARREPELLRANLAELFDLLAEGKIRPHVSAVFPLEQAAE 306
                        330
                 ....*....|....*.
gi 332646003 321 AFGDLKDRKAIGKVMI 336
Cdd:cd08241  307 ALRALADRKATGKVVL 322
 
Name Accession Description Interval E-value
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
1-336 2.88e-142

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: 405.34  E-value: 2.88e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGDPTAtnpgspespVEVSKTHPIPSLnsDTSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIV 80
Cdd:cd08241    1 MKAVVCKELGGPED---------LVLEEVPPEPGA--PGEVRIRVEAAGVNFPDLLMIQGKYQVKPPLPFVPGSEVAGVV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  81 DAIGPAVTKFRVGDRVCSFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAA 160
Cdd:cd08241   70 EAVGEGVTGFKVGDRVVALTGQGGFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALVRRARLQPGETVLVLGAA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 161 GGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVGGKLTKESMK 240
Cdd:cd08241  150 GGVGLAAVQLAKALGARVIAAASSEEKLALARALGADHVIDYRDPDLRERVKALTGGR---GVDVVYDPVGGDVFEASLR 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 241 VLKWGAQILVIGFASGEIPVIPANIALVKNWTVHGLYWGSYRIHQPNVLEDSIKELLSWLSRGLITIHISHTYSLSQANL 320
Cdd:cd08241  227 SLAWGGRLLVIGFASGEIPQIPANLLLLKNISVVGVYWGAYARREPELLRANLAELFDLLAEGKIRPHVSAVFPLEQAAE 306
                        330
                 ....*....|....*.
gi 332646003 321 AFGDLKDRKAIGKVMI 336
Cdd:cd08241  307 ALRALADRKATGKVVL 322
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
1-339 2.61e-85

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: 260.47  E-value: 2.61e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGDPTATnpgspeSPVEVskthPIPSLnSDTSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIV 80
Cdd:COG0604    1 MKAIVITEFGGPEVL------ELEEV----PVPEP-GPGEVLVRVKAAGVNPADLLIRRGLYPLPPGLPFIPGSDAAGVV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  81 DAIGPAVTKFRVGDRVCSFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVllvlgaa 160
Cdd:COG0604   70 VAVGEGVTGFKVGDRVAGLGRGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKPGETvlvhgaa 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 161 ggvgLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVGGKLTKESMK 240
Cdd:COG0604  150 ggvgSAAVQLAKALGARVIATASSPEKAELLRALGADHVIDYREEDFAERVRALTGGR---GVDVVLDTVGGDTLARSLR 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 241 VLKWGAQILVIGFASGEIPVIPANIALVKNWTVHGLYWGSYrihQPNVLEDSIKELLSWLSRGLITIHISHTYSLSQANL 320
Cdd:COG0604  227 ALAPGGRLVSIGAASGAPPPLDLAPLLLKGLTLTGFTLFAR---DPAERRAALAELARLLAAGKLRPVIDRVFPLEEAAE 303
                        330
                 ....*....|....*....
gi 332646003 321 AFGDLKDRKAIGKVMIALD 339
Cdd:COG0604  304 AHRLLESGKHRGKVVLTVD 322
quinone_pig3 TIGR02824
putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative ...
14-336 5.53e-47

putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative quinone oxidoreductases that belong to the broader superfamily (modeled by Pfam pfam00107) of zinc-dependent alcohol (of medium chain length) dehydrogenases and quinone oxiooreductases. The alignment shows no motif of conserved Cys residues as are found in zinc-binding members of the superfamily, and members are likely to be quinone oxidoreductases instead. A member of this family in Homo sapiens, PIG3, is induced by p53 but is otherwise uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274316 [Multi-domain]  Cd Length: 325  Bit Score: 161.66  E-value: 5.53e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   14 ATNPGSPESpVEVSKThPIPSLNSDtSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVG 93
Cdd:TIGR02824   6 ITEPGGPEV-LVLVEV-PLPVPKAG-EVLIRVAAAGVNRPDLLQRAGKYPPPPGASDILGLEVAGEVVAVGEGVSRWKVG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   94 DRVCSFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAAGGVGLAAVQIGKV 173
Cdd:TIGR02824  83 DRVCALVAGGGYAEYVAVPAGQVLPVPEGLSLVEAAALPETFFTVWSNLFQRGGLKAGETVLIHGGASGIGTTAIQLAKA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  174 CGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTrklKGVDVLYDPVGGKLTKESMKVLKWGAQILVIGF 253
Cdd:TIGR02824 163 FGARVFTTAGSDEKCAACEALGADIAINYREEDFVEVVKAETGG---KGVDVILDIVGGSYLNRNIKALALDGRIVQIGF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  254 ASGEIPVIPANIALVKNWTVHGLYWGSYRIHQPNVLEDSIKE-LLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIG 332
Cdd:TIGR02824 240 QGGRKAELDLGPLLAKRLTITGSTLRARPVAEKAAIAAELREhVWPLLASGRVRPVIDKVFPLEDAAQAHALMESGDHIG 319

                  ....
gi 332646003  333 KVMI 336
Cdd:TIGR02824 320 KIVL 323
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
43-336 9.32e-34

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 125.96  E-value: 9.32e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003    43 VRVIATSLNYANYLQILGKYQEKPPLpfipGSDYSGIVDAIGPAVTKFRVGDRVCSFADlGSFAQFIVADQSRLFLVPER 122
Cdd:smart00829   1 IEVRAAGLNFRDVLIALGLYPGEAVL----GGECAGVVTRVGPGVTGLAVGDRVMGLAP-GAFATRVVTDARLVVPIPDG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   123 CDMVAAAALPVAFGTSHVALVHRARLTSGQvllvlgaaggvgLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHvvdl 202
Cdd:smart00829  76 WSFEEAATVPVVFLTAYYALVDLARLRPGEsvlihaaaggvgQAAIQLARHLGAEVFATAGSPEKRDFLRALGIPD---- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   203 gtENVISS-----VKEFIKTRKLKGVDVLYDPVGGKLTKESMKVLKWGAQILVIG----FASGEIPVIPA--NIalvknw 271
Cdd:smart00829 152 --DHIFSSrdlsfADEILRATGGRGVDVVLNSLSGEFLDASLRCLAPGGRFVEIGkrdiRDNSQLAMAPFrpNV------ 223
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332646003   272 tvhglywgSYR-------IHQPNVLEDSIKELLSWLSRGLIT-IHIsHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:smart00829 224 --------SYHavdldalEEGPDRIRELLAEVLELFAEGVLRpLPV-TVFPISDAEDAFRYMQQGKHIGKVVL 287
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
1-337 2.57e-31

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 120.52  E-value: 2.57e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGDPTATNPGspespvevskTHPIPSLNSDtSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIV 80
Cdd:PTZ00354   2 MRAVTLKGFGGVDVLKIG----------ESPKPAPKRN-DVLIKVSAAGVNRADTLQRQGKYPPPPGSSEILGLEVAGYV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  81 DAIGPAVTKFRVGDRVCSFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAA 160
Cdd:PTZ00354  71 EDVGSDVKRFKEGDRVMALLPGGGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQSVLIHAGA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 161 GGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTE-NVISSVKEFIKTrklKGVDVLYDPVGGKLTKESM 239
Cdd:PTZ00354 151 SGVGTAAAQLAEKYGAATIITTSSEEKVDFCKKLAAIILIRYPDEeGFAPKVKKLTGE---KGVNLVLDCVGGSYLSETA 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 240 KVLKWGAQILVIGFASGeipvipaniALVKNWTVHGLYWGSYRI-----------HQPNVLEDSIKELLSWLSRGLITIH 308
Cdd:PTZ00354 228 EVLAVDGKWIVYGFMGG---------AKVEKFNLLPLLRKRASIifstlrsrsdeYKADLVASFEREVLPYMEEGEIKPI 298
                        330       340
                 ....*....|....*....|....*....
gi 332646003 309 ISHTYSLSQANLAFGDLKDRKAIGKVMIA 337
Cdd:PTZ00354 299 VDRTYPLEEVAEAHTFLEQNKNIGKVVLT 327
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
168-302 1.51e-17

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 77.65  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  168 VQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTrklKGVDVLYDPVGGKLT-KESMKVLKWGA 246
Cdd:pfam00107   7 IQLAKAAGAKVIAVDGSEEKLELAKELGADHVINPKETDLVEEIKELTGG---KGVDVVFDCVGSPATlEQALKLLRPGG 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 332646003  247 QILVIGFASGEIPVIPANIALvKNWTVHGLYWGSYrihqpnvleDSIKELLSWLSR 302
Cdd:pfam00107  84 RVVVVGLPGGPLPLPLAPLLL-KELTILGSFLGSP---------EEFPEALDLLAS 129
 
Name Accession Description Interval E-value
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
1-336 2.88e-142

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: 405.34  E-value: 2.88e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGDPTAtnpgspespVEVSKTHPIPSLnsDTSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIV 80
Cdd:cd08241    1 MKAVVCKELGGPED---------LVLEEVPPEPGA--PGEVRIRVEAAGVNFPDLLMIQGKYQVKPPLPFVPGSEVAGVV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  81 DAIGPAVTKFRVGDRVCSFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAA 160
Cdd:cd08241   70 EAVGEGVTGFKVGDRVVALTGQGGFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALVRRARLQPGETVLVLGAA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 161 GGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVGGKLTKESMK 240
Cdd:cd08241  150 GGVGLAAVQLAKALGARVIAAASSEEKLALARALGADHVIDYRDPDLRERVKALTGGR---GVDVVYDPVGGDVFEASLR 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 241 VLKWGAQILVIGFASGEIPVIPANIALVKNWTVHGLYWGSYRIHQPNVLEDSIKELLSWLSRGLITIHISHTYSLSQANL 320
Cdd:cd08241  227 SLAWGGRLLVIGFASGEIPQIPANLLLLKNISVVGVYWGAYARREPELLRANLAELFDLLAEGKIRPHVSAVFPLEQAAE 306
                        330
                 ....*....|....*.
gi 332646003 321 AFGDLKDRKAIGKVMI 336
Cdd:cd08241  307 ALRALADRKATGKVVL 322
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
1-339 2.61e-85

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: 260.47  E-value: 2.61e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGDPTATnpgspeSPVEVskthPIPSLnSDTSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIV 80
Cdd:COG0604    1 MKAIVITEFGGPEVL------ELEEV----PVPEP-GPGEVLVRVKAAGVNPADLLIRRGLYPLPPGLPFIPGSDAAGVV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  81 DAIGPAVTKFRVGDRVCSFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVllvlgaa 160
Cdd:COG0604   70 VAVGEGVTGFKVGDRVAGLGRGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKPGETvlvhgaa 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 161 ggvgLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVGGKLTKESMK 240
Cdd:COG0604  150 ggvgSAAVQLAKALGARVIATASSPEKAELLRALGADHVIDYREEDFAERVRALTGGR---GVDVVLDTVGGDTLARSLR 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 241 VLKWGAQILVIGFASGEIPVIPANIALVKNWTVHGLYWGSYrihQPNVLEDSIKELLSWLSRGLITIHISHTYSLSQANL 320
Cdd:COG0604  227 ALAPGGRLVSIGAASGAPPPLDLAPLLLKGLTLTGFTLFAR---DPAERRAALAELARLLAAGKLRPVIDRVFPLEEAAE 303
                        330
                 ....*....|....*....
gi 332646003 321 AFGDLKDRKAIGKVMIALD 339
Cdd:COG0604  304 AHRLLESGKHRGKVVLTVD 322
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
17-336 5.18e-52

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: 174.94  E-value: 5.18e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  17 PGSPEspVEVSKTHPIPSLNSDTsVRVRVIATSLNYANYLQILGKYqeKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRV 96
Cdd:cd05286    8 TGGPE--VLEYEDVPVPEPGPGE-VLVRNTAIGVNFIDTYFRSGLY--PLPLPFVLGVEGAGVVEAVGPGVTGFKVGDRV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  97 CSFADLGSFAQFIVADQSRLFLVPERCDMVAAAAL---------------PVAFGtsHVALVHRARLTSGQvllvlgaag 161
Cdd:cd05286   83 AYAGPPGAYAEYRVVPASRLVKLPDGISDETAAALllqgltahyllretyPVKPG--DTVLVHAAAGGVGL--------- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 162 gvglAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVGGKLTKESMKV 241
Cdd:cd05286  152 ----LLTQWAKALGATVIGTVSSEEKAELARAAGADHVINYRDEDFVERVREITGGR---GVDVVYDGVGKDTFEGSLDS 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 242 LKWGAQILVIGFASGEIPVIPANIALVKNWTVHGLYWGSYrIHQPNVLEDSIKELLSWLSRGLITIHISHTYSLSQANLA 321
Cdd:cd05286  225 LRPRGTLVSFGNASGPVPPFDLLRLSKGSLFLTRPSLFHY-IATREELLARAAELFDAVASGKLKVEIGKRYPLADAAQA 303
                        330
                 ....*....|....*
gi 332646003 322 FGDLKDRKAIGKVMI 336
Cdd:cd05286  304 HRDLESRKTTGKLLL 318
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
15-336 1.42e-49

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: 168.12  E-value: 1.42e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  15 TNPGSPEspVEVSKTHPIPSLNSDtSVRVRVIATSLNYANYLQILGKYQEKPP--LPFIPGSDYSGIVDAIGPAVTKFRV 92
Cdd:cd05289    7 HEYGGPE--VLELADVPTPEPGPG-EVLVKVHAAGVNPVDLKIREGLLKAAFPltLPLIPGHDVAGVVVAVGPGVTGFKV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  93 GDRVCSFADL---GSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAAGGVGLAAVQ 169
Cdd:cd05289   84 GDEVFGMTPFtrgGAYAEYVVVPADELALKPANLSFEEAAALPLAGLTAWQALFELGGLKAGQTVLIHGAAGGVGSFAVQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 170 IGKVCGAIVIAVArGTEKIQLLKSMGVDHVVDLGTENvissvkeFIKTRKLKGVDVLYDPVGGKLTKESMKVLKWGAQIL 249
Cdd:cd05289  164 LAKARGARVIATA-SAANADFLRSLGADEVIDYTKGD-------FERAAAPGGVDAVLDTVGGETLARSLALVKPGGRLV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 250 -VIGFASGEIPVIPANIAlvknwtvhglywGSYRIHQPN--VLEdsikELLSWLSRGLITIHISHTYSLSQANLAFGDLK 326
Cdd:cd05289  236 sIAGPPPAEQAAKRRGVR------------AGFVFVEPDgeQLA----ELAELVEAGKLRPVVDRVFPLEDAAEAHERLE 299
                        330
                 ....*....|
gi 332646003 327 DRKAIGKVMI 336
Cdd:cd05289  300 SGHARGKVVL 309
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
31-336 8.94e-49

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: 166.61  E-value: 8.94e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  31 PIPSLNSDtSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRV-CSFADL----GSF 105
Cdd:cd08253   21 PVPTPGPG-EVLVRVHASGVNPVDTYIRAGAYPGLPPLPYVPGSDGAGVVEAVGEGVDGLKVGDRVwLTNLGWgrrqGTA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 106 AQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAAGGVGLAAVQIGKVCGAIVIAVARGT 185
Cdd:cd08253  100 AEYVVVPADQLVPLPDGVSFEQGAALGIPALTAYRALFHRAGAKAGETVLVHGGSGAVGHAAVQLARWAGARVIATASSA 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 186 EKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVGGKLTKESMKVLKWGAQILVIGFASGEiPVIPANI 265
Cdd:cd08253  180 EGAELVRQAGADAVFNYRAEDLADRILAATAGQ---GVDVIIEVLANVNLAKDLDVLAPGGRIVVYGSGGLR-GTIPINP 255
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332646003 266 ALVKNWTVHGLYWGSyriHQPNVLEDSIKELLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:cd08253  256 LMAKEASIRGVLLYT---ATPEERAAAAEAIAAGLADGALRPVIAREYPLEEAAAAHEAVESGGAIGKVVL 323
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-337 4.58e-48

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: 164.65  E-value: 4.58e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVcrklgdptATNPGSPES--PVEVSKTHPIPslnsdTSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSG 78
Cdd:cd08272    1 MKALV--------LESFGGPEVfeLREVPRPQPGP-----GQVLVRVHASGVNPLDTKIRRGGAAARPPLPAILGCDVAG 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  79 IVDAIGPAVTKFRVGDRV--CS--FADL-GSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQV 153
Cdd:cd08272   68 VVEAVGEGVTRFRVGDEVygCAggLGGLqGSLAEYAVVDARLLALKPANLSMREAAALPLVGITAWEGLVDRAAVQAGQT 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 154 LLVLGAAGGVGLAAVQIGKVCGAIVIAVARGtEKIQLLKSMGVDHVVDLgTENVISSVKEFikTRKlKGVDVLYDPVGGK 233
Cdd:cd08272  148 VLIHGGAGGVGHVAVQLAKAAGARVYATASS-EKAAFARSLGADPIIYY-RETVVEYVAEH--TGG-RGFDVVFDTVGGE 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 234 LTKESMKVLKWGAQILVIgFASGEIPVIPANIalvKNWTVHG------LYWGSYRIHQPNVLEdsikELLSWLSRGLITI 307
Cdd:cd08272  223 TLDASFEAVALYGRVVSI-LGGATHDLAPLSF---RNATYSGvftllpLLTGEGRAHHGEILR----EAARLVERGQLRP 294
                        330       340       350
                 ....*....|....*....|....*....|.
gi 332646003 308 HIS-HTYSLSQANLAFGDLKDRKAIGKVMIA 337
Cdd:cd08272  295 LLDpRTFPLEEAAAAHARLESGSARGKIVID 325
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
1-336 2.55e-47

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: 163.20  E-value: 2.55e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGDPTAtnpgspespVEVsKTHPIPSLNSDtSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIV 80
Cdd:cd08266    1 MKAVVIRGHGGPEV---------LEY-GDLPEPEPGPD-EVLVRVKAAALNHLDLWVRRGMPGIKLPLPHILGSDGAGVV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  81 DAIGPAVTKFRVGDRVCSFADL---------------------------GSFAQFIVADQSRLFLVPERCDMVAAAALPV 133
Cdd:cd08266   70 EAVGPGVTNVKPGQRVVIYPGIscgrceyclagrenlcaqygilgehvdGGYAEYVAVPARNLLPIPDNLSFEEAAAAPL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 134 AFGTSHVALVHRARLTSGQVLLVLGAAGGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKE 213
Cdd:cd08266  150 TFLTAWHMLVTRARLRPGETVLVHGAGSGVGSAAIQIAKLFGATVIATAGSEDKLERAKELGADYVIDYRKEDFVREVRE 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 214 FIKTRklkGVDVLYDPVGGKLTKESMKVLKWGAQILVIGFASGEIPviPANIALV--KNWTVHGLYWGSYrihqpnvleD 291
Cdd:cd08266  230 LTGKR---GVDVVVEHVGAATWEKSLKSLARGGRLVTCGATTGYEA--PIDLRHVfwRQLSILGSTMGTK---------A 295
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 332646003 292 SIKELLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:cd08266  296 ELDEALRLVFRGKLKPVIDSVFPLEEAAEAHRRLESREQFGKIVL 340
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
13-336 2.83e-47

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: 162.61  E-value: 2.83e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  13 TATNPGSPES--PVEVSKthPIPSlnsDTSVRVRVIATSLNYANYLQILGKYqekPPLPF---IPGSDYSGIVDAIGPAV 87
Cdd:cd05276    5 VIKEPGGPEVleLGEVPK--PAPG---PGEVLIRVAAAGVNRADLLQRQGLY---PPPPGasdILGLEVAGVVVAVGPGV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  88 TKFRVGDRVCSFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAAGGVGLAA 167
Cdd:cd05276   77 TGWKVGDRVCALLAGGGYAEYVVVPAGQLLPVPEGLSLVEAAALPEVFFTAWQNLFQLGGLKAGETVLIHGGASGVGTAA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 168 VQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVGGKLTKESMKVLKWGAQ 247
Cdd:cd05276  157 IQLAKALGARVIATAGSEEKLEACRALGADVAINYRTEDFAEEVKEATGGR---GVDVILDMVGGDYLARNLRALAPDGR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 248 ILVIGFASGEIPVIPANIALVKNWTVHglywGS--------YRIhqpNVLEDSIKELLSWLSRGLITIHISHTYSLSQAN 319
Cdd:cd05276  234 LVLIGLLGGAKAELDLAPLLRKRLTLT----GStlrsrsleEKA---ALAAAFREHVWPLFASGRIRPVIDKVFPLEEAA 306
                        330
                 ....*....|....*..
gi 332646003 320 LAFGDLKDRKAIGKVMI 336
Cdd:cd05276  307 EAHRRMESNEHIGKIVL 323
quinone_pig3 TIGR02824
putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative ...
14-336 5.53e-47

putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative quinone oxidoreductases that belong to the broader superfamily (modeled by Pfam pfam00107) of zinc-dependent alcohol (of medium chain length) dehydrogenases and quinone oxiooreductases. The alignment shows no motif of conserved Cys residues as are found in zinc-binding members of the superfamily, and members are likely to be quinone oxidoreductases instead. A member of this family in Homo sapiens, PIG3, is induced by p53 but is otherwise uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274316 [Multi-domain]  Cd Length: 325  Bit Score: 161.66  E-value: 5.53e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   14 ATNPGSPESpVEVSKThPIPSLNSDtSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVG 93
Cdd:TIGR02824   6 ITEPGGPEV-LVLVEV-PLPVPKAG-EVLIRVAAAGVNRPDLLQRAGKYPPPPGASDILGLEVAGEVVAVGEGVSRWKVG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   94 DRVCSFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAAGGVGLAAVQIGKV 173
Cdd:TIGR02824  83 DRVCALVAGGGYAEYVAVPAGQVLPVPEGLSLVEAAALPETFFTVWSNLFQRGGLKAGETVLIHGGASGIGTTAIQLAKA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  174 CGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTrklKGVDVLYDPVGGKLTKESMKVLKWGAQILVIGF 253
Cdd:TIGR02824 163 FGARVFTTAGSDEKCAACEALGADIAINYREEDFVEVVKAETGG---KGVDVILDIVGGSYLNRNIKALALDGRIVQIGF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  254 ASGEIPVIPANIALVKNWTVHGLYWGSYRIHQPNVLEDSIKE-LLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIG 332
Cdd:TIGR02824 240 QGGRKAELDLGPLLAKRLTITGSTLRARPVAEKAAIAAELREhVWPLLASGRVRPVIDKVFPLEDAAQAHALMESGDHIG 319

                  ....
gi 332646003  333 KVMI 336
Cdd:TIGR02824 320 KIVL 323
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
28-336 8.72e-46

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: 158.90  E-value: 8.72e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  28 KTHPIPSLNSDtSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRVCSFADLGSFAQ 107
Cdd:cd08275   17 EKEALPEPSSG-EVRVRVEACGLNFADLMARQGLYDSAPKPPFVPGFECAGTVEAVGEGVKDFKVGDRVMGLTRFGGYAE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 108 FIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAAGGVGLAAVQIGK-VCGAIVIAVArGTE 186
Cdd:cd08275   96 VVNVPADQVFPLPDGMSFEEAAAFPVNYLTAYYALFELGNLRPGQSVLVHSAAGGVGLAAGQLCKtVPNVTVVGTA-SAS 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 187 KIQLLKSMGVDHVVDLGTENVISSVKEFiktrKLKGVDVLYDPVGGKLTKESMKVLKWGAQILVIGFA---SGEIPVIpa 263
Cdd:cd08275  175 KHEALKENGVTHVIDYRTQDYVEEVKKI----SPEGVDIVLDALGGEDTRKSYDLLKPMGRLVVYGAAnlvTGEKRSW-- 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 264 nIALVKNW----------------TVHGLYWGsYRIHQPNVLEDSIKELLSWLSRGLITIHISHTYSLSQANLAFGDLKD 327
Cdd:cd08275  249 -FKLAKKWwnrpkvdpmklisenkSVLGFNLG-WLFEERELLTEVMDKLLKLYEEGKIKPKIDSVFPFEEVGEAMRRLQS 326

                 ....*....
gi 332646003 328 RKAIGKVMI 336
Cdd:cd08275  327 RKNIGKVVL 335
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
41-334 4.28e-45

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: 156.99  E-value: 4.28e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  41 VRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRVCSFA-----DLGSFAQFIVADQSR 115
Cdd:cd08268   30 VLIRVEAIGLNRADAMFRRGAYIEPPPLPARLGYEAAGVVEAVGAGVTGFAVGDRVSVIPaadlgQYGTYAEYALVPAAA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 116 LFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAAGGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMG 195
Cdd:cd08268  110 VVKLPDGLSFVEAAALWMQYLTAYGALVELAGLRPGDSVLITAASSSVGLAAIQIANAAGATVIATTRTSEKRDALLALG 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 196 VDHVVDLGTENVISSVKEFIKTrklKGVDVLYDPVGGKLTKESMKVLKWGAQILVIGFASGEIPVIPANIALVKNWTVHG 275
Cdd:cd08268  190 AAHVIVTDEEDLVAEVLRITGG---KGVDVVFDPVGGPQFAKLADALAPGGTLVVYGALSGEPTPFPLKAALKKSLTFRG 266
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332646003 276 LYWGSYrIHQPNVLEDSIKELLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIGKV 334
Cdd:cd08268  267 YSLDEI-TLDPEARRRAIAFILDGLASGALKPVVDRVFPFDDIVEAHRYLESGQQIGKI 324
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
14-336 4.45e-44

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 154.50  E-value: 4.45e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  14 ATNPGSPESPVEVskthPIPSLNSDtSVRVRVIATSLNYANYLQILGKYqEKPPLPFIPGSDYSGIVDAIGPAVTKFRVG 93
Cdd:COG1064    6 LTEPGGPLELEEV----PRPEPGPG-EVLVKVEACGVCHSDLHVAEGEW-PVPKLPLVPGHEIVGRVVAVGPGVTGFKVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  94 DRV----------CSF------------------ADlGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHr 145
Cdd:COG1064   80 DRVgvgwvdscgtCEYcrsgrenlcengrftgytTD-GGYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITAYRALRR- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 146 ARLTSGQVllvlgaaggvglAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEfiktrkLKGVDV 225
Cdd:COG1064  158 AGVGPGDRvaviga-gglghLAVQIAKALGAEVIAVDRSPEKLELARELGADHVVNSSDEDPVEAVRE------LTGADV 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 226 LYDPVG-GKLTKESMKVLKWGAQILVIGFASGEIPVIPANIaLVKNWTVHGLYWGSYRihqpnvledSIKELLSWLSRGL 304
Cdd:COG1064  231 VIDTVGaPATVNAALALLRRGGRLVLVGLPGGPIPLPPFDL-ILKERSIRGSLIGTRA---------DLQEMLDLAAEGK 300
                        330       340       350
                 ....*....|....*....|....*....|..
gi 332646003 305 ITIHIsHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:COG1064  301 IKPEV-ETIPLEEANEALERLRAGKVRGRAVL 331
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
37-336 5.12e-44

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: 153.35  E-value: 5.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  37 SDTSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRVCSFA--DLGSFAQFIVADQS 114
Cdd:cd08251    6 GPGEVRIQVRAFSLNFGDLLCVRGLYPTMPPYPFTPGFEASGVVRAVGPHVTRLAVGDEVIAGTgeSMGGHATLVTVPED 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 115 RLFLVPERCDMVAAAALPVAFGTSHVALvHRARLTSGQVLLVLGAAGGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSM 194
Cdd:cd08251   86 QVVRKPASLSFEEACALPVVFLTVIDAF-ARAGLAKGEHILIQTATGGTGLMAVQLARLKGAEIYATASSDDKLEYLKQL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 195 GVDHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVGGKLTKESMKVLKWGAQILVIGF-ASGEIPVIPANIaLVKNWTV 273
Cdd:cd08251  165 GVPHVINYVEEDFEEEIMRLTGGR---GVDVVINTLSGEAIQKGLNCLAPGGRYVEIAMtALKSAPSVDLSV-LSNNQSF 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332646003 274 HGLYWGSYRIHQPNVLEDSIKELLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:cd08251  241 HSVDLRKLLLLDPEFIADYQAEMVSLVEEGELRPTVSRIFPFDDIGEAYRYLSDRENIGKVVV 303
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
31-338 5.96e-42

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: 148.84  E-value: 5.96e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  31 PIPSLNsDTSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRVCS------------ 98
Cdd:cd08276   21 PVPEPG-PGEVLVRVHAVSLNYRDLLILNGRYPPPVKDPLIPLSDGAGEVVAVGEGVTRFKVGDRVVPtffpnwldgppt 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  99 ----FADLGS-----FAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQvllvlgaaggvglaaV- 168
Cdd:cd08276  100 aedeASALGGpidgvLAEYVVLPEEGLVRAPDHLSFEEAATLPCAGLTAWNALFGLGPLKPGD---------------Tv 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 169 -------------QIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSvkefiKTRKL---KGVDVLYDPVGG 232
Cdd:cd08276  165 lvqgtggvslfalQFAKAAGARVIATSSSDEKLERAKALGADHVINYRTTPDWGE-----EVLKLtggRGVDHVVEVGGP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 233 KLTKESMKVLKWGAQILVIGFASGEIPVIPANIALVKNWTVHGLYWGSYRIHQpnvledsikELLSWLSRGLITIHISHT 312
Cdd:cd08276  240 GTLAQSIKAVAPGGVISLIGFLSGFEAPVLLLPLLTKGATLRGIAVGSRAQFE---------AMNRAIEAHRIRPVIDRV 310
                        330       340
                 ....*....|....*....|....*.
gi 332646003 313 YSLSQANLAFGDLKDRKAIGKVMIAL 338
Cdd:cd08276  311 FPFEEAKEAYRYLESGSHFGKVVIRV 336
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
41-337 1.52e-40

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: 144.73  E-value: 1.52e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  41 VRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRVCSFADLGSFAQFIVADQSRLFLVP 120
Cdd:cd05282   29 VLVRMLAAPINPSDLITISGAYGSRPPLPAVPGNEGVGVVVEVGSGVSGLLVGQRVLPLGGEGTWQEYVVAPADDLIPVP 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 121 ERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAAGGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVV 200
Cdd:cd05282  109 DSISDEQAAMLYINPLTAWLMLTEYLKLPPGDWVIQNAANSAVGRMLIQLAKLLGFKTINVVRRDEQVEELKALGADEVI 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 201 DLGTENVISSVKEFIKTrklKGVDVLYDPVGGKLTKESMKVLKWGAQILVIGFASGEIPVIPANIALVKNWTVHGLY-WG 279
Cdd:cd05282  189 DSSPEDLAQRVKEATGG---AGARLALDAVGGESATRLARSLRPGGTLVNYGLLSGEPVPFPRSVFIFKDITVRGFWlRQ 265
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332646003 280 SYRIHQPNVLEDSIKELLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIGKVMIA 337
Cdd:cd05282  266 WLHSATKEAKQETFAEVIKLVEAGVLTTPVGAKFPLEDFEEAVAAAEQPGRGGKVLLT 323
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
41-282 5.16e-40

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: 142.08  E-value: 5.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  41 VRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRVC----------------------- 97
Cdd:cd05188    2 VLVRVEAAGLCGTDLHIRRGGYPPPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVvlpnlgcgtcelcrelcpgggil 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  98 SFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQvllvlgaaggvglaavQIGKVCGAI 177
Cdd:cd05188   82 GEGLDGGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVLKPGDtvlvlgag-gvgllaaQLAKAAGAR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 178 VIAVARGTEKIQLLKSMGVDHVVDLGTENvissVKEFIKTRKLKGVDVLYDPVGGKLT-KESMKVLKWGAQILVIGFASG 256
Cdd:cd05188  161 VIVTDRSDEKLELAKELGADHVIDYKEED----LEEELRLTGGGGADVVIDAVGGPETlAQALRLLRPGGRIVVVGGTSG 236
                        250       260
                 ....*....|....*....|....*.
gi 332646003 257 EIPVIPANIALVKNWTVHGLYWGSYR 282
Cdd:cd05188  237 GPPLDDLRRLLFKELTIIGSTGGTRE 262
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
13-336 1.42e-39

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: 142.35  E-value: 1.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  13 TATNPGSPESPVEVSKTHPIPSLnSDTSVRVRVIATSLNYANYlqilgKYQEKPPL-------PFIPGSDYSGIVDAIGP 85
Cdd:cd08267    2 VYTRYGSPEVLLLLEVEVPIPTP-KPGEVLVKVHAASVNPVDW-----KLRRGPPKlllgrpfPPIPGMDFAGEVVAVGS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  86 AVTKFRVGDRVCSFADL---GSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQvllvlgaagg 162
Cdd:cd08267   76 GVTRFKVGDEVFGRLPPkggGALAEYVVAPESGLAKKPEGVSFEEAAALPVAGLTALQALRDAGKVKPGQrvlingasgg 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 163 vglAAVQIGKVCGAIVIAVArGTEKIQLLKSMGVDHVVDLGTENVISsvkefiKTRKLKGVDVLYDPVGG---KLTKESm 239
Cdd:cd08267  156 vgtFAVQIAKALGAHVTGVC-STRNAELVRSLGADEVIDYTTEDFVA------LTAGGEKYDVIFDAVGNspfSLYRAS- 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 240 KVLKWGAQILVIGFASGEIPVIPANIALVKNWTVHGLYWGSYRihqpNVLEDsIKELLSWLSRGLITIHISHTYSLSQAN 319
Cdd:cd08267  228 LALKPGGRYVSVGGGPSGLLLVLLLLPLTLGGGGRRLKFFLAK----PNAED-LEQLAELVEEGKLKPVIDSVYPLEDAP 302
                        330
                 ....*....|....*..
gi 332646003 320 LAFGDLKDRKAIGKVMI 336
Cdd:cd08267  303 EAYRRLKSGRARGKVVI 319
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
41-336 1.83e-37

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: 135.77  E-value: 1.83e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  41 VRVRVIATSLNYANYLQILGKYQEKPPLPfipGSDYSGIVDAIGPAVTKFRVGDRVCSFADlGSFAQFIVADQSRLFLVP 120
Cdd:cd05195    3 VEVEVKAAGLNFRDVLVALGLLPGDETPL---GLECSGIVTRVGSGVTGLKVGDRVMGLAP-GAFATHVRVDARLVVKIP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 121 ERCDMVAAAALPVAFGTSHVALVHRARLTSGQvllvlgaaggvgLAAVQIGKVCGAIVIAVARGTEKIQLLKSMG--VDH 198
Cdd:cd05195   79 DSLSFEEAATLPVAYLTAYYALVDLARLQKGEsvlihaaaggvgQAAIQLAQHLGAEVFATVGSEEKREFLRELGgpVDH 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 199 VVDlgtENVISSVKEFIKTRKLKGVDVLYDPVGGKLTKESMKVLKWGAQILVIG----FASGEIPVIPaniaLVKNWTVH 274
Cdd:cd05195  159 IFS---SRDLSFADGILRATGGRGVDVVLNSLSGELLRASWRCLAPFGRFVEIGkrdiLSNSKLGMRP----FLRNVSFS 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332646003 275 GLYWGSYRIHQPNVLEDSIKELLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:cd05195  232 SVDLDQLARERPELLRELLREVLELLEAGVLKPLPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
15-336 8.51e-36

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: 132.39  E-value: 8.51e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  15 TNPGSPESPVEVSKTHPIPSLNSdtsVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGD 94
Cdd:cd08273    7 TRRGGPEVLKVVEADLPEPAAGE---VVVKVEASGVSFADVQMRRGLYPDQPPLPFTPGYDLVGRVDALGSGVTGFEVGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  95 RVCSFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPV----AFGtshvaLVHRARLT-SGQVLLVLGAAGGVGLAAVQ 169
Cdd:cd08273   84 RVAALTRVGGNAEYINLDAKYLVPVPEGVDAAEAVCLVLnyvtAYQ-----MLHRAAKVlTGQRVLIHGASGGVGQALLE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 170 IGKVCGAIVIAVARgTEKIQLLKSMGVDHvVDLGTENVISSVKEfiktrkLKGVDVLYDPVGGKLTKESMKVLKWGAQIL 249
Cdd:cd08273  159 LALLAGAEVYGTAS-ERNHAALRELGATP-IDYRTKDWLPAMLT------PGGVDVVFDGVGGESYEESYAALAPGGTLV 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 250 VIGFASGEI-------PVIPANIALVKNW-------TVHGLYWGSYRIHQPNVLEDsIKELLSWLSRGLITIHISHTYSL 315
Cdd:cd08273  231 CYGGNSSLLqgrrslaALGSLLARLAKLKllptgrrATFYYVWRDRAEDPKLFRQD-LTELLDLLAKGKIRPKIAKRLPL 309
                        330       340
                 ....*....|....*....|.
gi 332646003 316 SQANLAFGDLKDRKAIGKVMI 336
Cdd:cd08273  310 SEVAEAHRLLESGKVVGKIVL 330
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
43-336 9.32e-34

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 125.96  E-value: 9.32e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003    43 VRVIATSLNYANYLQILGKYQEKPPLpfipGSDYSGIVDAIGPAVTKFRVGDRVCSFADlGSFAQFIVADQSRLFLVPER 122
Cdd:smart00829   1 IEVRAAGLNFRDVLIALGLYPGEAVL----GGECAGVVTRVGPGVTGLAVGDRVMGLAP-GAFATRVVTDARLVVPIPDG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   123 CDMVAAAALPVAFGTSHVALVHRARLTSGQvllvlgaaggvgLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHvvdl 202
Cdd:smart00829  76 WSFEEAATVPVVFLTAYYALVDLARLRPGEsvlihaaaggvgQAAIQLARHLGAEVFATAGSPEKRDFLRALGIPD---- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   203 gtENVISS-----VKEFIKTRKLKGVDVLYDPVGGKLTKESMKVLKWGAQILVIG----FASGEIPVIPA--NIalvknw 271
Cdd:smart00829 152 --DHIFSSrdlsfADEILRATGGRGVDVVLNSLSGEFLDASLRCLAPGGRFVEIGkrdiRDNSQLAMAPFrpNV------ 223
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332646003   272 tvhglywgSYR-------IHQPNVLEDSIKELLSWLSRGLIT-IHIsHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:smart00829 224 --------SYHavdldalEEGPDRIRELLAEVLELFAEGVLRpLPV-TVFPISDAEDAFRYMQQGKHIGKVVL 287
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
41-336 1.77e-32

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: 123.58  E-value: 1.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  41 VRVRVIATSLNYANYLQILGKYQE-KPPLpfIPGSDYSGIVDAIGPAVTKFRVGDRV---------------------C- 97
Cdd:cd08259   28 VLIKVKAAGVCYRDLLFWKGFFPRgKYPL--ILGHEIVGTVEEVGEGVERFKPGDRVilyyyipcgkceyclsgeenlCr 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  98 -----SFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALvHRARLTSGQVLLVLGAAGGVGLAAVQIGK 172
Cdd:cd08259  106 nraeyGEEVDGGFAEYVKVPERSLVKLPDNVSDESAALAACVVGTAVHAL-KRAGVKKGDTVLVTGAGGGVGIHAIQLAK 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 173 VCGAIVIAVARGTEKIQLLKSMGVDHVVDLGtenviSSVKEFiktRKLKGVDVLYDPVGGKLTKESMKVLKWGAQILVIG 252
Cdd:cd08259  185 ALGARVIAVTRSPEKLKILKELGADYVIDGS-----KFSEDV---KKLGGADVVIELVGSPTIEESLRSLNKGGRLVLIG 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 253 FASGEIPVIPANIALVKNWTVHGlywgsyriHQPNVLEDsIKELLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIG 332
Cdd:cd08259  257 NVTPDPAPLRPGLLILKEIRIIG--------SISATKAD-VEEALKLVKEGKIKPVIDRVVSLEDINEALEDLKSGKVVG 327

                 ....
gi 332646003 333 KVMI 336
Cdd:cd08259  328 RIVL 331
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
15-337 1.20e-31

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: 121.29  E-value: 1.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  15 TNPGSPESPVEVSKThPIPSLNSDtSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGD 94
Cdd:cd08292    7 TQFGDPADVLEIGEV-PKPTPGAG-EVLVRTTLSPIHNHDLWTIRGTYGYKPELPAIGGSEAVGVVDAVGEGVKGLQVGQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  95 RVCSFADLGSFAQFIVADQSRLFLVPERCDMVAAAALpVAFGTSHVALVHRARLTSGQVLLVLGAAGGVGLAAVQIGKVC 174
Cdd:cd08292   85 RVAVAPVHGTWAEYFVAPADGLVPLPDGISDEVAAQL-IAMPLSALMLLDFLGVKPGQWLIQNAAGGAVGKLVAMLAAAR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 175 GAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRKLKgvdVLYDPVGGKLTKESMKVLKWGAQILVIGFA 254
Cdd:cd08292  164 GINVINLVRRDAGVAELRALGIGPVVSTEQPGWQDKVREAAGGAPIS---VALDSVGGKLAGELLSLLGEGGTLVSFGSM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 255 SGEIPVIPANIALVKNWTVHGLyWGSYRIHQPNVlEDS---IKELLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAI 331
Cdd:cd08292  241 SGEPMQISSGDLIFKQATVRGF-WGGRWSQEMSV-EYRkrmIAELLTLALKGQLLLPVEAVFDLGDAAKAAAASMRPGRA 318

                 ....*.
gi 332646003 332 GKVMIA 337
Cdd:cd08292  319 GKVLLR 324
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
15-251 1.42e-31

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: 120.84  E-value: 1.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  15 TNPGSPESPVEVSKTHPIPSLnSDTSVRVRVIATSLNYANYLQILGKYQEKPPlPFIPGSDYSGIVDAIGPAVTKFRVGD 94
Cdd:cd08271    5 VLPKPGAALQLTLEEIEIPGP-GAGEVLVKVHAAGLNPVDWKVIAWGPPAWSY-PHVPGVDGAGVVVAVGAKVTGWKVGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  95 RVCSFADL---GSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAAGGVGLAAVQIG 171
Cdd:cd08271   83 RVAYHASLargGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYQALFKKLRIEAGRTILITGGAGGVGSFAVQLA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 172 KVCGAIVIAVARgTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVGGKLTKESMKVLKWGAQILVI 251
Cdd:cd08271  163 KRAGLRVITTCS-KRNFEYVKSLGADHVIDYNDEDVCERIKEITGGR---GVDAVLDTVGGETAAALAPTLAFNGHLVCI 238
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
1-337 2.57e-31

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 120.52  E-value: 2.57e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGDPTATNPGspespvevskTHPIPSLNSDtSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIV 80
Cdd:PTZ00354   2 MRAVTLKGFGGVDVLKIG----------ESPKPAPKRN-DVLIKVSAAGVNRADTLQRQGKYPPPPGSSEILGLEVAGYV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  81 DAIGPAVTKFRVGDRVCSFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAA 160
Cdd:PTZ00354  71 EDVGSDVKRFKEGDRVMALLPGGGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQSVLIHAGA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 161 GGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTE-NVISSVKEFIKTrklKGVDVLYDPVGGKLTKESM 239
Cdd:PTZ00354 151 SGVGTAAAQLAEKYGAATIITTSSEEKVDFCKKLAAIILIRYPDEeGFAPKVKKLTGE---KGVNLVLDCVGGSYLSETA 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 240 KVLKWGAQILVIGFASGeipvipaniALVKNWTVHGLYWGSYRI-----------HQPNVLEDSIKELLSWLSRGLITIH 308
Cdd:PTZ00354 228 EVLAVDGKWIVYGFMGG---------AKVEKFNLLPLLRKRASIifstlrsrsdeYKADLVASFEREVLPYMEEGEIKPI 298
                        330       340
                 ....*....|....*....|....*....
gi 332646003 309 ISHTYSLSQANLAFGDLKDRKAIGKVMIA 337
Cdd:PTZ00354 299 VDRTYPLEEVAEAHTFLEQNKNIGKVVLT 327
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
2-336 1.56e-30

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: 118.24  E-value: 1.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   2 EALVCRKLGDPtATNPGSPESPVEVSKTHPIpslnsDTSVRvrviatslnyanylQILGKYQEKPPLPFIPGSDYSGIVD 81
Cdd:cd08244   13 EVLVPEDVPDP-VPGPGQVRIAVAAAGVHFV-----DTQLR--------------SGWGPGPFPPELPYVPGGEVAGVVD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  82 AIGPAVTKFRVGDRVCSF--ADLGSFAQFIVADQSRLFLVPERCDMVAAAALpVAFGTSHVALVHRARLTSGQVLLVLGA 159
Cdd:cd08244   73 AVGPGVDPAWLGRRVVAHtgRAGGGYAELAVADVDSLHPVPDGLDLEAAVAV-VHDGRTALGLLDLATLTPGDVVLVTAA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 160 AGGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVGGKLTKESM 239
Cdd:cd08244  152 AGGLGSLLVQLAKAAGATVVGAAGGPAKTALVRALGADVAVDYTRPDWPDQVREALGGG---GVTVVLDGVGGAIGRAAL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 240 KVLKWGAQILVIGFASGEIPVIPANIALVKNWTVHGLYWGSYrihQPNVLEDSIKELLSWLSRGLITIHISHTYSLSQAN 319
Cdd:cd08244  229 ALLAPGGRFLTYGWASGEWTALDEDDARRRGVTVVGLLGVQA---ERGGLRALEARALAEAAAGRLVPVVGQTFPLERAA 305
                        330
                 ....*....|....*..
gi 332646003 320 LAFGDLKDRKAIGKVMI 336
Cdd:cd08244  306 EAHAALEARSTVGKVLL 322
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
1-336 9.85e-30

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: 116.55  E-value: 9.85e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGDPtatnpgspeSPVEVSKTHPIPSLNSDTSVRVRVIATSLN---------YANYL-----QILGKYQEKP 66
Cdd:cd08248    1 MKAWQIHSYGGI---------DSLLLLENARIPVIRKPNQVLIKVHAASVNpidvlmrsgYGRTLlnkkrKPQSCKYSGI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  67 PLPFIPGSDYSGIVDAIGPAVTKFRVGDRVCSFADL---GSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALV 143
Cdd:cd08248   72 EFPLTLGRDCSGVVVDIGSGVKSFEIGDEVWGAVPPwsqGTHAEYVVVPENEVSKKPKNLSHEEAASLPYAGLTAWSALV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 144 HRARL----TSGQVLLVLGAAGGVGLAAVQIGKVCGAIVIAVARgTEKIQLLKSMGVDHVVDLGTENVISSVKEfiktrk 219
Cdd:cd08248  152 NVGGLnpknAAGKRVLILGGSGGVGTFAIQLLKAWGAHVTTTCS-TDAIPLVKSLGADDVIDYNNEDFEEELTE------ 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 220 LKGVDVLYDPVGGKLTKESMKVLKWGAQILVI-----------GFASGEipVIPANIALVKNWtVHGLYWGSYRIHQPNV 288
Cdd:cd08248  225 RGKFDVILDTVGGDTEKWALKLLKKGGTYVTLvspllkntdklGLVGGM--LKSAVDLLKKNV-KSLLKGSHYRWGFFSP 301
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 332646003 289 LEDSIKELLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:cd08248  302 SGSALDELAKLVEDGKIKPVIDKVFPFEEVPEAYEKVESGHARGKTVI 349
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
1-339 3.89e-29

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: 114.85  E-value: 3.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGDptatnpgspespVEVsKTHPIPSLNsDTSVRVRVIATS-----LNYanylqILGKYQEKPPlPFIPGSD 75
Cdd:COG1063    1 MKALVLHGPGD------------LRL-EEVPDPEPG-PGEVLVRVTAVGicgsdLHI-----YRGGYPFVRP-PLVLGHE 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  76 YSGIVDAIGPAVTKFRVGDRVCS---------------------------FADL-GSFAQFIVADQSRLFLVPERCDMVA 127
Cdd:COG1063   61 FVGEVVEVGEGVTGLKVGDRVVVepnipcgecrycrrgrynlcenlqflgIAGRdGGFAEYVRVPAANLVKVPDGLSDEA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 128 AAA---LPVAFgtsHValVHRARLTSGQvllvlgaaggvglaavqigKV----CGAI---------------VIAVARGT 185
Cdd:COG1063  141 AALvepLAVAL---HA--VERAGVKPGD-------------------TVlvigAGPIgllaalaarlagaarVIVVDRNP 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 186 EKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVGGKLT-KESMKVLKWGAQILVIGFASGEIPvIPAN 264
Cdd:COG1063  197 ERLELARELGADAVVNPREEDLVEAVRELTGGR---GADVVIEAVGAPAAlEQALDLVRPGGTVVLVGVPGGPVP-IDLN 272
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332646003 265 IALVKNWTVHglywGSYRihqpNVLEDsIKELLSWLSRGLITIH--ISHTYSLSQANLAFGDLKDRKA-IGKVMIALD 339
Cdd:COG1063  273 ALVRKELTLR----GSRN----YTRED-FPEALELLASGRIDLEplITHRFPLDDAPEAFEAAADRADgAIKVVLDPD 341
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
19-242 7.80e-28

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: 111.14  E-value: 7.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  19 SPESPVEVSKTHPIPSLNSDTsVRVRVIATSLNYANYLQIlgKYQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRVCS 98
Cdd:cd08249    8 GPGGGLLVVVDVPVPKPGPDE-VLVKVKAVALNPVDWKHQ--DYGFIPSYPAILGCDFAGTVVEVGSGVTRFKVGDRVAG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  99 FA--------DLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAAGGVG------ 164
Cdd:cd08249   85 FVhggnpndpRNGAFQEYVVADADLTAKIPDNISFEEAATLPVGLVTAALALFQKLGLPLPPPKPSPASKGKPVliwggs 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 165 ----LAAVQIGKVCGAIVIAVArGTEKIQLLKSMGVDHVVDLGTenviSSVKEFIKTRKLKGVDVLYDPVGgklTKESMK 240
Cdd:cd08249  165 ssvgTLAIQLAKLAGYKVITTA-SPKNFDLVKSLGADAVFDYHD----PDVVEDIRAATGGKLRYALDCIS---TPESAQ 236

                 ..
gi 332646003 241 VL 242
Cdd:cd08249  237 LC 238
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
15-339 3.85e-26

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 106.27  E-value: 3.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  15 TNPGSPESPVEVSKTHPIPSlnsdtSVRVRVIATSLNYANYLQILGKYQeKPPLPFIPGSDYSGIVDAIGPAVTKFRVGD 94
Cdd:PRK13771   7 PGFKQGYRIEEVPDPKPGKD-----EVVIKVNYAGLCYRDLLQLQGFYP-RMKYPVILGHEVVGTVEEVGENVKGFKPGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  95 RV----------CSFA----------------DL-GSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALvHRAR 147
Cdd:PRK13771  81 RVasllyapdgtCEYCrsgeeaycknrlgygeELdGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVTGMVYRGL-RRAG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 148 LTSGQVLLVLGAAGGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGvDHVVdlgTENVISSvkefiKTRKLKGVDVLY 227
Cdd:PRK13771 160 VKKGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSSESKAKIVSKYA-DYVI---VGSKFSE-----EVKKIGGADIVI 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 228 DPVGGKLTKESMKVLKWGAQILVIG-FASGEIPVIPANIALVKNWTVHGLYWGSYRihqpnvledSIKELLSWLSRGLIT 306
Cdd:PRK13771 231 ETVGTPTLEESLRSLNMGGKIIQIGnVDPSPTYSLRLGYIILKDIEIIGHISATKR---------DVEEALKLVAEGKIK 301
                        330       340       350
                 ....*....|....*....|....*....|...
gi 332646003 307 IHISHTYSLSQANLAFGDLKDRKAIGKVMIALD 339
Cdd:PRK13771 302 PVIGAEVSLSEIDKALEELKDKSRIGKILVKPS 334
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
26-336 4.22e-25

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: 103.49  E-value: 4.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  26 VSKTHPIPSlnsDTSVRVRVI-----ATSLNYANylqilGKYQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRVCSFA 100
Cdd:cd08250   21 VDVPVPLPG---PGEVLVKNRfvginASDINFTA-----GRYDPGVKPPFDCGFEGVGEVVAVGEGVTDFKVGDAVATMS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 101 dLGSFAQFIVADQSRLFLVPErcdmVAAAALP--VAFGTSHVALVHRARLTSGQVLLVLGAAGGVGLAAVQIGKVCGAIV 178
Cdd:cd08250   93 -FGAFAEYQVVPARHAVPVPE----LKPEVLPllVSGLTASIALEEVGEMKSGETVLVTAAAGGTGQFAVQLAKLAGCHV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 179 IAVARGTEKIQLLKSMGVDHVVDLGTENvissVKEFIKTRKLKGVDVLYDPVGGKLTKESMKVLKWGAQILVIGFASG-- 256
Cdd:cd08250  168 IGTCSSDEKAEFLKSLGCDRPINYKTED----LGEVLKKEYPKGVDVVYESVGGEMFDTCVDNLALKGRLIVIGFISGyq 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 257 --------EIPVIPANIaLVKNWTVHGLYWGSYRIHQPNVLEdsikELLSWLSRGLITIHISHT--YSLSQANLAFGDLK 326
Cdd:cd08250  244 sgtgpspvKGATLPPKL-LAKSASVRGFFLPHYAKLIPQHLD----RLLQLYQRGKLVCEVDPTrfRGLESVADAVDYLY 318
                        330
                 ....*....|
gi 332646003 327 DRKAIGKVMI 336
Cdd:cd08250  319 SGKNIGKVVV 328
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
15-305 5.98e-25

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: 103.07  E-value: 5.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  15 TNPGSPESPVEVsKTHPIPSLNSDTSVRVRVIATSLNYANYLQILGKYQEKPP----LPFIPGSDYSGIVDAIGPAVTKF 90
Cdd:cd08290    7 TEHGEPKEVLQL-ESYEIPPPGPPNEVLVKMLAAPINPADINQIQGVYPIKPPttpePPAVGGNEGVGEVVKVGSGVKSL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  91 RVGDRVC-SFADLGSFAQFIVADQSRLFLVPERCDMVAAAAL----PVAF-------------------GTSHVALVhra 146
Cdd:cd08290   86 KPGDWVIpLRPGLGTWRTHAVVPADDLIKVPNDVDPEQAATLsvnpCTAYrlledfvklqpgdwviqngANSAVGQA--- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 147 rltsgqvllvlgaaggvglaAVQIGKVCGAIVIAVARGTEKI----QLLKSMGVDHVVdlgTENVISSV--KEFIKTRKL 220
Cdd:cd08290  163 --------------------VIQLAKLLGIKTINVVRDRPDLeelkERLKALGADHVL---TEEELRSLlaTELLKSAPG 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 221 KGVDVLYDPVGGKLTKESMKVLKWGAQILVIGFASGEIPVIPANIALVKNWTVHGlYWGS--YRIHQPNVLEDSIKELLS 298
Cdd:cd08290  220 GRPKLALNCVGGKSATELARLLSPGGTMVTYGGMSGQPVTVPTSLLIFKDITLRG-FWLTrwLKRANPEEKEDMLEELAE 298

                 ....*..
gi 332646003 299 WLSRGLI 305
Cdd:cd08290  299 LIREGKL 305
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
33-335 1.37e-24

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: 102.04  E-value: 1.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  33 PSLNSDtSVRVRVIATSLNYANYLQIlGKYQEKPpLPFIPGSDYSGIVDAIGPAVTKFRVGDRV---------------- 96
Cdd:cd08264   22 PKPGPG-EVLIRVKMAGVNPVDYNVI-NAVKVKP-MPHIPGAEFAGVVEEVGDHVKGVKKGDRVvvynrvfdgtcdmcls 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  97 -----C------SFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALvHRARLTSGQVLLVLGAAGGVGL 165
Cdd:cd08264   99 gnemlCrnggiiGVVSNGGYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYHAL-KTAGLGPGETVVVFGASGNTGI 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 166 AAVQIGKVCGAIVIAVARGtekiQLLKSMGVDHVVDlgTENVISSVKEFIKTrklkgVDVLYDPVGGKLTKESMKVLKWG 245
Cdd:cd08264  178 FAVQLAKMMGAEVIAVSRK----DWLKEFGADEVVD--YDEVEEKVKEITKM-----ADVVINSLGSSFWDLSLSVLGRG 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 246 AQILVIG-FASGEIPVipaNIALVknWTVHGLYWGSYRihqpnvleDSIKELLSWLSR-GLITIHISHTYSLSQANLAFG 323
Cdd:cd08264  247 GRLVTFGtLTGGEVKL---DLSDL--YSKQISIIGSTG--------GTRKELLELVKIaKDLKVKVWKTFKLEEAKEALK 313
                        330
                 ....*....|..
gi 332646003 324 DLKDRKAIGKVM 335
Cdd:cd08264  314 ELFSKERDGRIL 325
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
63-332 1.56e-24

D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related alcohol dehydrogenases. AraDH is a member of the medium chain dehydrogenase/reductase family and catalyzes the NAD(P)-dependent oxidation of D-arabinose and other pentoses, the initial step in the metabolism of d-arabinose into 2-oxoglutarate. Like the alcohol dehydrogenases, AraDH binds a zinc in the catalytic cleft as well as a distal structural zinc. AraDH forms homotetramers as a dimer of dimers. AraDH replaces a conserved catalytic His with replace with Arg, compared to the canonical ADH site. 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: 176187 [Multi-domain]  Cd Length: 340  Bit Score: 102.25  E-value: 1.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  63 QEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRV---------------------CSFADL------GSFAQFIVADQSR 115
Cdd:cd05284   52 ILPYKLPFTLGHENAGWVEEVGSGVDGLKEGDPVvvhppwgcgtcrycrrgeenyCENARFpgigtdGGFAEYLLVPSRR 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 116 LFLVPERCDMVAAAALPVAFGTSHVALV-HRARLTSGQVLLVlgaaggvglaavqIG-------------KVCGAIVIAV 181
Cdd:cd05284  132 LVKLPRGLDPVEAAPLADAGLTAYHAVKkALPYLDPGSTVVV-------------IGvgglghiavqilrALTPATVIAV 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 182 ARGTEKIQLLKSMGVDHVVDlGTENVISSVKEFIKTRklkGVDVLYDPVGGKLTKE-SMKVLKWGAQILVIGFAsGEIPv 260
Cdd:cd05284  199 DRSEEALKLAERLGADHVLN-ASDDVVEEVRELTGGR---GADAVIDFVGSDETLAlAAKLLAKGGRYVIVGYG-GHGR- 272
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332646003 261 IPANIALVKNWTVHGLYWGSYrihqpNVLEDSIKellswLSR-GLITIHIShTYSLSQANLAFGDLKDRKAIG 332
Cdd:cd05284  273 LPTSDLVPTEISVIGSLWGTR-----AELVEVVA-----LAEsGKVKVEIT-KFPLEDANEALDRLREGRVTG 334
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
1-336 3.11e-24

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: 101.07  E-value: 3.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGDPtatnpgspesPVEVsKTHPIPSlNSDTSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIV 80
Cdd:cd08297    1 MKAAVVEEFGEK----------PYEV-KDVPVPE-PGPGEVLVKLEASGVCHTDLHAALGDWPVKPKLPLIGGHEGAGVV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  81 DAIGPAVTKFRVGDRV----------------------CSFADL------GSFAQFIVADQSRLFLVPERCDMVAAAALP 132
Cdd:cd08297   69 VAVGPGVSGLKVGDRVgvkwlydacgkceycrtgdetlCPNQKNsgytvdGTFAEYAIADARYVTPIPDGLSFEQAAPLL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 133 VAFGTSHVALVhRARLTSGQVLLVLGAAGGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVK 212
Cdd:cd08297  149 CAGVTVYKALK-KAGLKPGDWVVISGAGGGLGHLGVQYAKAMGLRVIAIDVGDEKLELAKELGADAFVDFKKSDDVEAVK 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 213 EFIKTRKLKGVDVLydPVGGKLTKESMKVLKWGAQILVIGFASGEIPVIPANIALVKNWTVHGLYWGSyrihqpnvLEDS 292
Cdd:cd08297  228 ELTGGGGAHAVVVT--AVSAAAYEQALDYLRPGGTLVCVGLPPGGFIPLDPFDLVLRGITIVGSLVGT--------RQDL 297
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 332646003 293 iKELLSWLSRGLITIHIShTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:cd08297  298 -QEALEFAARGKVKPHIQ-VVPLEDLNEVFEKMEEGKIAGRVVV 339
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
69-336 4.59e-24

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: 100.83  E-value: 4.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  69 PFIPGSDYSGIVDAIGPAVTKFRVGDRVCSFADL-------------------GSFAQFIVADQSRLFLVPERCDMVAAA 129
Cdd:cd08274   78 PRIQGADIVGRVVAVGEGVDTARIGERVLVDPSIrdppeddpadidyigserdGGFAEYTVVPAENAYPVNSPLSDVELA 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 130 ALPVAFGTSHVALvHRARLTSGQVLLVLGAAGGVGLAAVQIGKVCGAIVIAVArGTEKIQLLKSMGVDHVVDLGTENVis 209
Cdd:cd08274  158 TFPCSYSTAENML-ERAGVGAGETVLVTGASGGVGSALVQLAKRRGAIVIAVA-GAAKEEAVRALGADTVILRDAPLL-- 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 210 svkEFIKTRKLKGVDVLYDPVGGKLTKESMKVLKWGAQILVIGFASGEIPVIPANIALVKNWTVHGLYWGSYRIhqpnvl 289
Cdd:cd08274  234 ---ADAKALGGEPVDVVADVVGGPLFPDLLRLLRPGGRYVTAGAIAGPVVELDLRTLYLKDLTLFGSTLGTREV------ 304
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 332646003 290 edsIKELLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:cd08274  305 ---FRRLVRYIEEGEIRPVVAKTFPLSEIREAQAEFLEKRHVGKLVL 348
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
15-334 1.46e-23

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: 99.32  E-value: 1.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  15 TNPGSPESPVEVSKTHPIPSLnsdtsVRVRVIATSLNYANYLQILGKYQEkPPLPFIPGSDYSGIVDAIGPAVTKFRVGD 94
Cdd:cd08245    6 HAAGGPLEPEEVPVPEPGPGE-----VLIKIEACGVCHTDLHAAEGDWGG-SKYPLVPGHEIVGEVVEVGAGVEGRKVGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  95 RV----------------------------CSFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHrA 146
Cdd:cd08245   80 RVgvgwlvgscgrceycrrglenlcqkavnTGYTTQGGYAEYMVADAEYTVLLPDGLPLAQAAPLLCAGITVYSALRD-A 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 147 RLTSGQvLLVLGAAGGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSvkefiktrKLKGVDVL 226
Cdd:cd08245  159 GPRPGE-RVAVLGIGGLGHLAVQYARAMGFETVAITRSPDKRELARKLGADEVVDSGAELDEQA--------AAGGADVI 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 227 YDPV-GGKLTKESMKVLKWGAQILVIGFASGEIPVIPANIALVKNWTVHGLYWGSYRIHQpnvledsikELLSWLSRGLI 305
Cdd:cd08245  230 LVTVvSGAAAEAALGGLRRGGRIVLVGLPESPPFSPDIFPLIMKRQSIAGSTHGGRADLQ---------EALDFAAEGKV 300
                        330       340
                 ....*....|....*....|....*....
gi 332646003 306 TIHIsHTYSLSQANLAFgdlkDRKAIGKV 334
Cdd:cd08245  301 KPMI-ETFPLDQANEAY----ERMEKGDV 324
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
16-334 2.72e-23

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: 98.47  E-value: 2.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  16 NPGSPESPVEVSKthPIPSLNSDtSVRVRVIA-----TSLNYanylqILGKYQEKPPLPFIPGSDYSGIVDAIGPAVTKF 90
Cdd:cd08254    7 HKGSKGLLVLEEV--PVPEPGPG-EVLVKVKAagvchSDLHI-----LDGGVPTLTKLPLTLGHEIAGTVVEVGAGVTNF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  91 RVGDRVCSFADL---------------------------GSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALV 143
Cdd:cd08254   79 KVGDRVAVPAVIpcgacalcrrgrgnlclnqgmpglgidGGFAEYIVVPARALVPVPDGVPFAQAAVATDAVLTPYHAVV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 144 HRARLTSGQvLLVLGAAGGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTEnviSSVKEFIKTRKLkGV 223
Cdd:cd08254  159 RAGEVKPGE-TVLVIGLGGLGLNAVQIAKAMGAAVIAVDIKEEKLELAKELGADEVLNSLDD---SPKDKKAAGLGG-GF 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 224 DVLYDPVGGKLTKES-MKVLKWGAQILVIGFASGEIPvIPANIALVKNWTVHGLYWGSYrihqpnvleDSIKELLSWLSR 302
Cdd:cd08254  234 DVIFDFVGTQPTFEDaQKAVKPGGRIVVVGLGRDKLT-VDLSDLIARELRIIGSFGGTP---------EDLPEVLDLIAK 303
                        330       340       350
                 ....*....|....*....|....*....|..
gi 332646003 303 GLITIhISHTYSLSQANLAFGDLKDRKAIGKV 334
Cdd:cd08254  304 GKLDP-QVETRPLDEIPEVLERLHKGKVKGRV 334
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
1-336 1.12e-21

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: 94.21  E-value: 1.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGDPTAtnpgspespvevSKTHPIPSLNSDTSVrVRVIATSLNYANYLQILGkYQEKPPLPFIPGSDYSGIV 80
Cdd:cd08260    1 MRAAVYEEFGEPLE------------IREVPDPEPPPDGVV-VEVEACGVCRSDWHGWQG-HDPDVTLPHVPGHEFAGVV 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  81 DAIGPAVTKFRVGDRV-------------CS--------------FADLGSFAQFIVADQSRLFLV--PERCDMVAAAAL 131
Cdd:cd08260   67 VEVGEDVSRWRVGDRVtvpfvlgcgtcpyCRagdsnvcehqvqpgFTHPGSFAEYVAVPRADVNLVrlPDDVDFVTAAGL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 132 PVAFGTSHVALVHRARLTSGQVLLVLGAAGGVGlAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDL-GTENVISS 210
Cdd:cd08260  147 GCRFATAFRALVHQARVKPGEWVAVHGCGGVGL-SAVMIASALGARVIAVDIDDDKLELARELGAVATVNAsEVEDVAAA 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 211 VKEFIKtrklKGVDVLYDPVGGKLT-KESMKVLKWGAQILVIGFASGEIPVIPANIALVKNWT-----VHGLYWGSYRih 284
Cdd:cd08260  226 VRDLTG----GGAHVSVDALGIPETcRNSVASLRKRGRHVQVGLTLGEEAGVALPMDRVVAREleivgSHGMPAHRYD-- 299
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 332646003 285 qpnvledsikELLSWLSRGLITIH--ISHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:cd08260  300 ----------AMLALIASGKLDPEplVGRTISLDEAPDALAAMDDYATAGITVI 343
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
20-336 2.64e-21

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: 93.59  E-value: 2.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  20 PESPVEVSKTH-PIPSLNSdtsVRVRVIATSLNYANyLQILgKYQEKPPLPFIPGSDYSGIVDAIGPAVT---KFRVGDR 95
Cdd:cd08263    9 PNPPLTIEEIPvPRPKEGE---ILIRVAACGVCHSD-LHVL-KGELPFPPPFVLGHEISGEVVEVGPNVEnpyGLSVGDR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  96 V----------CSFA-----DL----------------------------------GSFAQFIVADQSRLFLVPERCDMV 126
Cdd:cd08263   84 VvgsfimpcgkCRYCargkeNLcedffaynrlkgtlydgttrlfrldggpvymysmGGLAEYAVVPATALAPLPESLDYT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 127 AAAALPVAFGTSHVALVHRARLTSGQVLLVLGAAGGVGlAAVQIGKVCGA-IVIAVARGTEKIQLLKSMGVDHVVDLGTE 205
Cdd:cd08263  164 ESAVLGCAGFTAYGALKHAADVRPGETVAVIGVGGVGS-SAIQLAKAFGAsPIIAVDVRDEKLAKAKELGATHTVNAAKE 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 206 NVISSVKEFIKTRklkGVDVLYDPVGGKLT-KESMKVLKWGAQILVIGFASG--EIPvIPANIALVKNWTVHGLYWGSYR 282
Cdd:cd08263  243 DAVAAIREITGGR---GVDVVVEALGKPETfKLALDVVRDGGRAVVVGLAPGgaTAE-IPITRLVRRGIKIIGSYGARPR 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332646003 283 IHQPnvledsikELLSWLSRGLITIH--ISHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:cd08263  319 QDLP--------ELVGLAASGKLDPEalVTHKYKLEEINEAYENLRKGLIHGRAIV 366
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
43-334 4.21e-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: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 88.97  E-value: 4.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  43 VRVIATSLNYANylqiLGKYQEKPPlPFIPGSDYSGIV-----DAIGPAVtkfrvGDRVCSFADLGSFAQFIVADQSRLF 117
Cdd:cd08270   31 VRVAAISLNRGE----LKFAAERPD-GAVPGWDAAGVVeraaaDGSGPAV-----GARVVGLGAMGAWAELVAVPTGWLA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 118 LVPERCDMVAAAALPVAfGTSHVALVHRARLTSGQVLLVLGAAGGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVD 197
Cdd:cd08270  101 VLPDGVSFAQAATLPVA-GVTALRALRRGGPLLGRRVLVTGASGGVGRFAVQLAALAGAHVVAVVGSPARAEGLRELGAA 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 198 HVVDLGTEnvISSVKefiktrklkgVDVLYDPVGGKLTKESMKVLKWGAQILVIGFASGEIPVIPANiALVKNWTVHGLY 277
Cdd:cd08270  180 EVVVGGSE--LSGAP----------VDLVVDSVGGPQLARALELLAPGGTVVSVGSSSGEPAVFNPA-AFVGGGGGRRLY 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332646003 278 WGSYRIHQPnvLEDSIKELLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIGKV 334
Cdd:cd08270  247 TFFLYDGEP--LAADLARLLGLVAAGRLDPRIGWRGSWTEIDEAAEALLARRFRGKA 301
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
31-336 5.99e-20

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: 89.21  E-value: 5.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  31 PIPSLNSDtSVRVRVIATSLNYANYLQILGKYQEKPPLpfIPGSDYSGIVDAIGPAVTKFRVGDRV----------CSFA 100
Cdd:cd08236   18 PKPEPGPG-EVLVKVKACGICGSDIPRYLGTGAYHPPL--VLGHEFSGTVEEVGSGVDDLAVGDRVavnpllpcgkCEYC 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 101 D------------LGS-----FAQFIVADQSRLFLVPERCDMVAAAAL-PVAfgtshVAL--VHRARLTSGQVLLVlgaa 160
Cdd:cd08236   95 KkgeyslcsnydyIGSrrdgaFAEYVSVPARNLIKIPDHVDYEEAAMIePAA-----VALhaVRLAGITLGDTVVV---- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 161 ggvglaavqIGkvCGAI---------------VIAVARGTEKIQLLKSMGVDHVVDLGTENViSSVKEFIKTRklkGVDV 225
Cdd:cd08236  166 ---------IG--AGTIgllaiqwlkilgakrVIAVDIDDEKLAVARELGADDTINPKEEDV-EKVRELTEGR---GADL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 226 LYDPVGGKLTKE-SMKVLKWGAQILVIGFASGE--IPVIPANIALVKNWTVHGlYWGSYRIHQPNvleDSIKELLSWLSR 302
Cdd:cd08236  231 VIEAAGSPATIEqALALARPGGKVVLVGIPYGDvtLSEEAFEKILRKELTIQG-SWNSYSAPFPG---DEWRTALDLLAS 306
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 332646003 303 GLITI--HISHTYSLSQANLAFGDLKDRK-AIGKVMI 336
Cdd:cd08236  307 GKIKVepLITHRLPLEDGPAAFERLADREeFSGKVLL 343
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
15-336 1.65e-19

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: 87.66  E-value: 1.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  15 TNPGSPESPVEVSKTHPIPSLNSDTSVRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIVDAIGP-AVTKFRVG 93
Cdd:cd08291    7 EEYGKPLEVKELSLPEPEVPEPGPGEVLIKVEAAPINPSDLGFLKGQYGSTKALPVPPGFEGSGTVVAAGGgPLAQSLIG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  94 DRV-CSFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTS-----------HVALVHRARLTS-GQvllvlgaa 160
Cdd:cd08291   87 KRVaFLAGSYGTYAEYAVADAQQCLPLPDGVSFEQGASSFVNPLTAlgmletareegAKAVVHTAAASAlGR-------- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 161 ggvglAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKtrKLKgVDVLYDPVGGKLTKESMK 240
Cdd:cd08291  159 -----MLVRLCKADGIKVINIVRRKEQVDLLKKIGAEYVLNSSDPDFLEDLKELIA--KLN-ATIFFDAVGGGLTGQILL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 241 VLKWGAQILVIGFASG-EIPVIPANIALVKNWTVHGlYWGSYRIHQPNvlEDSIKELLSWLSRGLITIHISHtYSLSQAN 319
Cdd:cd08291  231 AMPYGSTLYVYGYLSGkLDEPIDPVDLIFKNKSIEG-FWLTTWLQKLG--PEVVKKLKKLVKTELKTTFASR-YPLALTL 306
                        330
                 ....*....|....*..
gi 332646003 320 LAFGDLKDRKAIGKVMI 336
Cdd:cd08291  307 EAIAFYSKNMSTGKKLL 323
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
31-336 1.25e-18

L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine, via NAD(H)-dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. 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. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176196 [Multi-domain]  Cd Length: 334  Bit Score: 85.27  E-value: 1.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  31 PIPSLNSDtSVRVRVIA-----TSLNYANylqilGKYQEKPPLpfIPGSDYSGIVDAIGPAVTKFRVGDRV--------- 96
Cdd:cd08234   18 PVPEPGPD-EVLIKVAAcgicgTDLHIYE-----GEFGAAPPL--VPGHEFAGVVVAVGSKVTGFKVGDRVavdpniycg 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  97 -CSF---------ADL--------GSFAQFIVADQSRLFLVPERCDMVAAAAL-PVAfgtshvALVH---RARLTSGQVL 154
Cdd:cd08234   90 eCFYcrrgrpnlcENLtavgvtrnGGFAEYVVVPAKQVYKIPDNLSFEEAALAePLS------CAVHgldLLGIKPGDSV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 155 LVlgaaggvglaavqIGkvCGAI---------------VIAVARGTEKIQLLKSMGVDHVVDLGTENVISsvkefIKTRK 219
Cdd:cd08234  164 LV-------------FG--AGPIglllaqllklngasrVTVAEPNEEKLELAKKLGATETVDPSREDPEA-----QKEDN 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 220 LKGVDVLYDPVGGKLTKESM-KVLKWGAQILVIGFASGE--IPVIPANIaLVKNWTVHglywGSYRihQPNVLEDSIkel 296
Cdd:cd08234  224 PYGFDVVIEATGVPKTLEQAiEYARRGGTVLVFGVYAPDarVSISPFEI-FQKELTII----GSFI--NPYTFPRAI--- 293
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 332646003 297 lSWLSRGLITIH--ISHTYSLSQANLAFGDLKDRKAIgKVMI 336
Cdd:cd08234  294 -ALLESGKIDVKglVSHRLPLEEVPEALEGMRSGGAL-KVVV 333
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
41-331 2.66e-18

Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 84.75  E-value: 2.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  41 VRVRVIATS-----LNYANylqilGKYQEkpPLPFIPGSDYSGIVDAIGPAVTKFRVGDRV-------------CS---- 98
Cdd:COG1062   19 VLVRIVAAGlchsdLHVRD-----GDLPV--PLPAVLGHEGAGVVEEVGPGVTGVAPGDHVvlsfipscghcryCAsgrp 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  99 --------------------------------FADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRA 146
Cdd:COG1062   92 alceagaalngkgtlpdgtsrlssadgepvghFFGQSSFAEYAVVPERSVVKVDKDVPLELAALLGCGVQTGAGAVLNTA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 147 RLTSGQVLLVlgaaggvglaavqIG------------KVCGA-IVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKE 213
Cdd:COG1062  172 KVRPGDTVAV-------------FGlggvglsavqgaRIAGAsRIIAVDPVPEKLELARELGATHTVNPADEDAVEAVRE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 214 FikTRklKGVDVLYDPVG-GKLTKESMKVLKWGAQILVIGFASGEIPV-IPANIALVKNWTVHGLYWGSYRIHQpnvled 291
Cdd:COG1062  239 L--TG--GGVDYAFETTGnPAVIRQALEALRKGGTVVVVGLAPPGAEIsLDPFQLLLTGRTIRGSYFGGAVPRR------ 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 332646003 292 SIKELLSWLSRGLITIH--ISHTYSLSQANLAFGDLKDRKAI 331
Cdd:COG1062  309 DIPRLVDLYRAGRLPLDelITRRYPLDEINEAFDDLRSGEVI 350
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
168-302 1.51e-17

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 77.65  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  168 VQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTrklKGVDVLYDPVGGKLT-KESMKVLKWGA 246
Cdd:pfam00107   7 IQLAKAAGAKVIAVDGSEEKLELAKELGADHVINPKETDLVEEIKELTGG---KGVDVVFDCVGSPATlEQALKLLRPGG 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 332646003  247 QILVIGFASGEIPVIPANIALvKNWTVHGLYWGSYrihqpnvleDSIKELLSWLSR 302
Cdd:pfam00107  84 RVVVVGLPGGPLPLPLAPLLL-KELTILGSFLGSP---------EEFPEALDLLAS 129
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
1-283 6.49e-17

Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination 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 an 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: 176219 [Multi-domain]  Cd Length: 306  Bit Score: 80.05  E-value: 6.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVcrklgdPTATNPGSpespVEVsKTHPIPSLNSDtSVRVRVIATSLNYANYLQILGKYqEKPPLPFIPGSDYSGIV 80
Cdd:cd08258    1 MKALV------KTGPGPGN----VEL-REVPEPEPGPG-EVLIKVAAAGICGSDLHIYKGDY-DPVETPVVLGHEFSGTI 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  81 DAIGPAVTKFRVGDRVCSFADL----------------------------GSFAQFIVADQSRLFLVPERCDMVAAAAL- 131
Cdd:cd08258   68 VEVGPDVEGWKVGDRVVSETTFstcgrcpycrrgdynlcphrkgigtqadGGFAEYVLVPEESLHELPENLSLEAAALTe 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 132 PVAfgTSHVALVHRARLTSGQVLLVLGAAGGVGLAAvQIGKVCGAIVIAVARGTEKIQL--LKSMGVDHvVDLGTENVIS 209
Cdd:cd08258  148 PLA--VAVHAVAERSGIRPGDTVVVFGPGPIGLLAA-QVAKLQGATVVVVGTEKDEVRLdvAKELGADA-VNGGEEDLAE 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332646003 210 SVKEFiktRKLKGVDVLYDPVGGKLT-KESMKVLKWGAQILVIGFASGEIPVIPANIALVKNWTVHGLY---WGSYRI 283
Cdd:cd08258  224 LVNEI---TDGDGADVVIECSGAVPAlEQALELLRKGGRIVQVGIFGPLAASIDVERIIQKELSVIGSRsstPASWET 298
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
195-334 8.77e-17

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 75.83  E-value: 8.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  195 GVDHVVDLGTENVISSVKEfiktrklKGVDVLYDPVGGKLTKESMKVLKWGAQILVIGFAsgeiPVIPANIALVKNWTVH 274
Cdd:pfam13602   2 GADEVIDYRTTDFVQATGG-------EGVDVVLDTVGGEAFEASLRVLPGGGRLVTIGGP----PLSAGLLLPARKRGGR 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  275 GLYWGSYrIHQPNVLEDSIKELLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIGKV 334
Cdd:pfam13602  71 GVKYLFL-FVRPNLGADILQELADLIEEGKLRPVIDRVFPLEEAAEAHRYLESGRARGKI 129
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
1-336 1.73e-16

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: 78.81  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVcrklgdptATNPGSPEspVEVSKTHPIPSLNSDTsVRVRVIATSLNYANYLQILGkyqEKPPLPF--IPGSDYSG 78
Cdd:cd08243    1 MKAIV--------IEQPGGPE--VLKLREIPIPEPKPGW-VLIRVKAFGLNRSEIFTRQG---HSPSVKFprVLGIEAVG 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  79 IVDAIGPavTKFRVGDRVCS------FADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQ 152
Cdd:cd08243   67 EVEEAPG--GTFTPGQRVATamggmgRTFDGSYAEYTLVPNEQVYAIDSDLSWAELAALPETYYTAWGSLFRSLGLQPGD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 153 VLLVLGAAGGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVdLGTENVISSVKEfiktrKLKGVDVLYDPVGG 232
Cdd:cd08243  145 TLLIRGGTSSVGLAALKLAKALGATVTATTRSPERAALLKELGADEVV-IDDGAIAEQLRA-----APGGFDKVLELVGT 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 233 KLTKESMKVLKWGAQILVIGFASGEiPVIP-----ANIALVKNWTVHGLYWGsyrihqpNVLEDSIKELLSWLSRGLITI 307
Cdd:cd08243  219 ATLKDSLRHLRPGGIVCMTGLLGGQ-WTLEdfnpmDDIPSGVNLTLTGSSSG-------DVPQTPLQELFDFVAAGHLDI 290
                        330       340
                 ....*....|....*....|....*....
gi 332646003 308 HISHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:cd08243  291 PPSKVFTFDEIVEAHAYMESNRAFGKVVV 319
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
69-338 6.81e-16

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays 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 GroES-like catalytic domain. 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. 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: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 77.66  E-value: 6.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  69 PFIPGSDYSGIVDAIGPAVTKFRVGDRV----------CSFAD------------LGS----------FAQFIVADQSRL 116
Cdd:cd08232   54 PMVLGHEVSGVVEAVGPGVTGLAPGQRVavnpsrpcgtCDYCRagrpnlclnmrfLGSamrfphvqggFREYLVVDASQC 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 117 FLVPERCDMVAAA-ALPVAfgtshVAL--VHRAR-------LTSGqvllvlgaaggvglaavqIGKVcGAIVIAVAR--G 184
Cdd:cd08232  134 VPLPDGLSLRRAAlAEPLA-----VALhaVNRAGdlagkrvLVTG------------------AGPI-GALVVAAARraG 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 185 TEKI----------QLLKSMGVDHVVDLGTEnvissvkEFIKTRKLKG-VDVLYDPVGGKLTKES-MKVLKWGAQILVIG 252
Cdd:cd08232  190 AAEIvatdladaplAVARAMGADETVNLARD-------PLAAYAADKGdFDVVFEASGAPAALASaLRVVRPGGTVVQVG 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 253 FASGEIPViPANIALVKNWTvhglYWGSYRIHqpnvleDSIKELLSWLSRGLITIH--ISHTYSLSQANLAFGDLKDRKA 330
Cdd:cd08232  263 MLGGPVPL-PLNALVAKELD----LRGSFRFD------DEFAEAVRLLAAGRIDVRplITAVFPLEEAAEAFALAADRTR 331

                 ....*...
gi 332646003 331 IGKVMIAL 338
Cdd:cd08232  332 SVKVQLSF 339
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
41-330 1.08e-15

Cinnamyl alcohol dehydrogenases (CAD); 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 (ADHs), 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: 176256 [Multi-domain]  Cd Length: 333  Bit Score: 76.90  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  41 VRVRVIATSLNYANYLQILGKYQeKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRV--------------CSFADL---- 102
Cdd:cd08296   28 VLIKVEACGVCHSDAFVKEGAMP-GLSYPRVPGHEVVGRIDAVGEGVSRWKVGDRVgvgwhgghcgtcdaCRRGDFvhce 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 103 ----------GSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSH-------------VA------LVHRArltsgqv 153
Cdd:cd08296  107 ngkvtgvtrdGGYAEYMLAPAEALARIPDDLDAAEAAPLLCAGVTTFnalrnsgakpgdlVAvqgiggLGHLA------- 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 154 llvlgaaggvglaaVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISsvkefiKTRKLKGVDVLYDPVG-G 232
Cdd:cd08296  180 --------------VQYAAKMGFRTVAISRGSDKADLARKLGAHHYIDTSKEDVAE------ALQELGGAKLILATAPnA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 233 KLTKESMKVLKWGAQILVIGFASGEIPVIPANIaLVKNWTVHGLYWGSyrihqPNVLEDSIKelLSWLS--RGLItihis 310
Cdd:cd08296  240 KAISALVGGLAPRGKLLILGAAGEPVAVSPLQL-IMGRKSIHGWPSGT-----ALDSEDTLK--FSALHgvRPMV----- 306
                        330       340
                 ....*....|....*....|
gi 332646003 311 HTYSLSQANLAFGDLKDRKA 330
Cdd:cd08296  307 ETFPLEKANEAYDRMMSGKA 326
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
41-331 1.27e-15

Liver alcohol dehydrogenase and related 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. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. 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. 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 an 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.


Pssm-ID: 176182 [Multi-domain]  Cd Length: 365  Bit Score: 77.09  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  41 VRVRVIATSLNYANYLQILGKYqeKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRV---------------------CSF 99
Cdd:cd05279   28 VRIKVVATGVCHTDLHVIDGKL--PTPLPVILGHEGAGIVESIGPGVTTLKPGDKViplfgpqcgkckqclnprpnlCSK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 100 ADL---------------------------GSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQ 152
Cdd:cd05279  106 SRGtngrglmsdgtsrftckgkpihhflgtSTFAEYTVVSEISLAKIDPDAPLEKVCLIGCGFSTGYGAAVNTAKVTPGS 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 153 VLLVLGAAGGVGlAAVQIGKVCGA-IVIAVARGTEKIQLLKSMGVDHVVDLGTENVisSVKEFIKTRKLKGVDVLYDPVG 231
Cdd:cd05279  186 TCAVFGLGGVGL-SVIMGCKAAGAsRIIAVDINKDKFEKAKQLGATECINPRDQDK--PIVEVLTEMTDGGVDYAFEVIG 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 232 gklTKESMK------VLKWGAQILVIGFASGEIPVIPANIaLVKNWTVHGLYWGSYrihqpnVLEDSIKELLSWLSRGLI 305
Cdd:cd05279  263 ---SADTLKqaldatRLGGGTSVVVGVPPSGTEATLDPND-LLTGRTIKGTVFGGW------KSKDSVPKLVALYRQKKF 332
                        330       340
                 ....*....|....*....|....*...
gi 332646003 306 TIH--ISHTYSLSQANLAFGDLKDRKAI 331
Cdd:cd05279  333 PLDelITHVLPFEEINDGFDLMRSGESI 360
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
1-332 5.36e-15

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: 176258 [Multi-domain]  Cd Length: 329  Bit Score: 74.91  E-value: 5.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGdPTATNPGSPEspvEVskthPIPSLNSDtSVRVRVIATSLNYANYLQILGKYQEkPPLPFIPGSDYSGIV 80
Cdd:cd08298    1 MKAMVLEKPG-PIEENPLRLT---EV----PVPEPGPG-EVLIKVEACGVCRTDLHIVEGDLPP-PKLPLIPGHEIVGRV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  81 DAIGPAVTKFRVGDRV-----------CSF------------------ADlGSFAQFIVADQSRLFLVPERCDMVAAAAL 131
Cdd:cd08298   71 EAVGPGVTRFSVGDRVgvpwlgstcgeCRYcrsgrenlcdnarftgytVD-GGYAEYMVADERFAYPIPEDYDDEEAAPL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 132 PVA-----------------------FGTS-HVALvhrarltsgqvllvlgaaggvglaavQIGKVCGAIVIAVARGTEK 187
Cdd:cd08298  150 LCAgiigyralklaglkpgqrlglygFGASaHLAL--------------------------QIARYQGAEVFAFTRSGEH 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 188 IQLLKSMGVDHVVDLgtenvissvkefiKTRKLKGVD--VLYDPVGgKLTKESMKVLKWGAQILVIGFASGEIPVIPANi 265
Cdd:cd08298  204 QELARELGADWAGDS-------------DDLPPEPLDaaIIFAPVG-ALVPAALRAVKKGGRVVLAGIHMSDIPAFDYE- 268
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332646003 266 alvknwtvhgLYWGSYRIHQ-PNVLEDSIKELLSWLSRGLITIHIsHTYSLSQANLAFGDLKDRKAIG 332
Cdd:cd08298  269 ----------LLWGEKTIRSvANLTRQDGEEFLKLAAEIPIKPEV-ETYPLEEANEALQDLKEGRIRG 325
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
69-338 1.15e-14

L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as a threonine dehydrogenase. L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Zinc-dependent ADHs are medium chain dehydrogenase/reductase type proteins (MDRs) and have a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. In addition to alcohol dehydrogenases, this group includes quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. These 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: 176201 [Multi-domain]  Cd Length: 339  Bit Score: 73.89  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  69 PFIPGSDYSGIVDAIGPAVTKFRVGDRV----CSFADL------------------------GSFAQFIVADQSRLFLVP 120
Cdd:cd08239   55 GVIPGHEPAGVVVAVGPGVTHFRVGDRVmvyhYVGCGAcrncrrgwmqlctskraaygwnrdGGHAEYMLVPEKTLIPLP 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 121 ERCDMVAAAALPVAFGTSHVALvHRARLTSGQVLLVLGaaggvglaavqIGKV-CGAIVIAVARGTEKI----------Q 189
Cdd:cd08239  135 DDLSFADGALLLCGIGTAYHAL-RRVGVSGRDTVLVVG-----------AGPVgLGALMLARALGAEDVigvdpsperlE 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 190 LLKSMGVDHVVDLGTENvissVKEFIKTRKLKGVDVLYD----PVGGKLTKESmkVLKWGAQILV-IGfasGEIPVIPAN 264
Cdd:cd08239  203 LAKALGADFVINSGQDD----VQEIRELTSGAGADVAIEcsgnTAARRLALEA--VRPWGRLVLVgEG---GELTIEVSN 273
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332646003 265 IALVKNWTVHGLYWGSYRIHQPNVLEdsIKELLSWLSRgLITihisHTYSLSQANLAFGDLkDRKAIGKVMIAL 338
Cdd:cd08239  274 DLIRKQRTLIGSWYFSVPDMEECAEF--LARHKLEVDR-LVT----HRFGLDQAPEAYALF-AQGESGKVVFVF 339
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
1-336 2.71e-14

L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish 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 GroES-like catalytic domain. 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: 176197 [Multi-domain]  Cd Length: 343  Bit Score: 72.63  E-value: 2.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGDptatnpgspespVEVSKThPIPSLNSDtSVRVRVIATSLNYANYLQILGKYQeKPPLPFIPGSDYSGIV 80
Cdd:cd08235    1 MKAAVLHGPND------------VRLEEV-PVPEPGPG-EVLVKVRACGICGTDVKKIRGGHT-DLKPPRILGHEIAGEI 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  81 DAIGPAVTKFRVGDRVC---------------------------SFADLGSFAQFIV-----ADQSRLFLVPERCDMVAA 128
Cdd:cd08235   66 VEVGDGVTGFKVGDRVFvaphvpcgechyclrgnenmcpnykkfGNLYDGGFAEYVRvpawaVKRGGVLKLPDNVSFEEA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 129 A-ALPVAfgtSHVALVHRARLTSGQVLLVlgaaggvglaavqIG------------KVCGA-IVIAVARGTEKIQLLKSM 194
Cdd:cd08235  146 AlVEPLA---CCINAQRKAGIKPGDTVLV-------------IGagpigllhamlaKASGArKVIVSDLNEFRLEFAKKL 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 195 GVDHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVGG-KLTKESMKVLKWGAQILVI-GFASGEIPVIPANIALVKNWT 272
Cdd:cd08235  210 GADYTIDAAEEDLVEKVRELTDGR---GADVVIVATGSpEAQAQALELVRKGGRILFFgGLPKGSTVNIDPNLIHYREIT 286
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332646003 273 VHGLYwGSYRIHQpnvledsiKELLSWLSRGLITIH--ISHTYSLSQANLAFGDLKDRKAIgKVMI 336
Cdd:cd08235  287 ITGSY-AASPEDY--------KEALELIASGKIDVKdlITHRFPLEDIEEAFELAADGKSL-KIVI 342
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
31-201 4.07e-14

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: 72.83  E-value: 4.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  31 PIPSLNSDtSVRVRVIATSLNYANYLQILGK--------YQEKPPLPF-IPGSDYSGIVDAIGPAVTKFRVGDRV---CS 98
Cdd:cd08246   36 PVPELGPG-EVLVAVMAAGVNYNNVWAALGEpvstfaarQRRGRDEPYhIGGSDASGIVWAVGEGVKNWKVGDEVvvhCS 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  99 FADL-------------------------GSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHR--ARLTSG 151
Cdd:cd08246  115 VWDGndperaggdpmfdpsqriwgyetnyGSFAQFALVQATQLMPKPKHLSWEEAAAYMLVGATAYRMLFGWnpNTVKPG 194
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 332646003 152 QVLLVLGAAGGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVD 201
Cdd:cd08246  195 DNVLIWGASGGLGSMAIQLARAAGANPVAVVSSEEKAEYCRALGAEGVIN 244
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
41-331 4.23e-14

Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, Class III ADH) are members 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. 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. Class III ADH are also known as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to corresponding carboxylic acid and alcohol. 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 an 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.


Pssm-ID: 176240 [Multi-domain]  Cd Length: 363  Bit Score: 72.57  E-value: 4.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  41 VRVRVIATSLNYANYLQILGKYqeKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRV-------------CS--------- 98
Cdd:cd08279   28 VLVRIAAAGLCHSDLHVVTGDL--PAPLPAVLGHEGAGVVEEVGPGVTGVKPGDHVvlswipacgtcryCSrgqpnlcdl 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  99 -------------------------FADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQV 153
Cdd:cd08279  106 gagilggqlpdgtrrftadgepvgaMCGLGTFAEYTVVPEASVVKIDDDIPLDRAALLGCGVTTGVGAVVNTARVRPGDT 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 154 LLVlgaaggvglaavqIGkvCGAI---------------VIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFikTR 218
Cdd:cd08279  186 VAV-------------IG--CGGVglnaiqgariagasrIIAVDPVPEKLELARRFGATHTVNASEDDAVEAVRDL--TD 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 219 KLkGVDVLYDPVG-GKLTKESMKVLKWGAQILVIGFASGEIPV-IPANIALVKNWTVHGLYWGSYRIHQpnvledSIKEL 296
Cdd:cd08279  249 GR-GADYAFEAVGrAATIRQALAMTRKGGTAVVVGMGPPGETVsLPALELFLSEKRLQGSLYGSANPRR------DIPRL 321
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 332646003 297 LSWLSRGLITIH--ISHTYSLSQANLAFGDLKDRKAI 331
Cdd:cd08279  322 LDLYRAGRLKLDelVTRRYSLDEINEAFADMLAGENA 358
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
89-336 4.43e-14

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: 72.13  E-value: 4.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  89 KFRVGDRVCSFADLGSFAqfIVADQSRLFLVPERCDMVAAAALPVaFG----TSHVALVHRARLTSGQVLLVLGAAGGVG 164
Cdd:cd05288   83 DFKVGDLVSGFLGWQEYA--VVDGASGLRKLDPSLGLPLSAYLGV-LGmtglTAYFGLTEIGKPKPGETVVVSAAAGAVG 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 165 LAAVQIGKVCGAIVIAVARGTEKIQLLKS-MGVDHVVDLGTENVISSVKEFIKtrklKGVDVLYDPVGGKLTKESMKVLK 243
Cdd:cd05288  160 SVVGQIAKLLGARVVGIAGSDEKCRWLVEeLGFDAAINYKTPDLAEALKEAAP----DGIDVYFDNVGGEILDAALTLLN 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 244 WGAQILVIGFASG---EIPVIPANIA--LVKNWTVHGLYWGSYRIHQPNVledsIKELLSWLSRGLITIHISHTYSLSQA 318
Cdd:cd05288  236 KGGRIALCGAISQynaTEPPGPKNLGniITKRLTMQGFIVSDYADRFPEA----LAELAKWLAEGKLKYREDVVEGLENA 311
                        250
                 ....*....|....*...
gi 332646003 319 NLAFGDLKDRKAIGKVMI 336
Cdd:cd05288  312 PEAFLGLFTGKNTGKLVV 329
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
20-201 1.27e-13

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: 70.63  E-value: 1.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  20 PESPVEVSKTHPIPSlnsDTSVRVRVIATSLNYANYlQILGKYQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRVC-- 97
Cdd:cd08252   15 PDSLIDIELPKPVPG---GRDLLVRVEAVSVNPVDT-KVRAGGAPVPGQPKILGWDASGVVEAVGSEVTLFKVGDEVYya 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  98 -SFADLGSFAQFIVADqSRLF-LVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAAGG-----VGLAAVQI 170
Cdd:cd08252   91 gDITRPGSNAEYQLVD-ERIVgHKPKSLSFAEAAALPLTSLTAWEALFDRLGISEDAENEGKTLLIIggaggVGSIAIQL 169
                        170       180       190
                 ....*....|....*....|....*....|..
gi 332646003 171 GKVCGAI-VIAVARGTEKIQLLKSMGVDHVVD 201
Cdd:cd08252  170 AKQLTGLtVIATASRPESIAWVKELGADHVIN 201
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
28-330 2.55e-13

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: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 69.69  E-value: 2.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  28 KTHPIPSLnSDTSVRVRVIATSLNYANYLQIlgkYQEKPP-----LPFIPGSDYSGIVDAIGPAVTKFRVGDRVCSFADl 102
Cdd:cd08269   10 EEHPRPTP-GPGQVLVRVEGCGVCGSDLPAF---NQGRPWfvypaEPGGPGHEGWGRVVALGPGVRGLAVGDRVAGLSG- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 103 GSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGtshVALVHRARLTSGQvLLVLGAAGGVGLAAVQIGKVCGA-IVIAV 181
Cdd:cd08269   85 GAFAEYDLADADHAVPLPSLLDGQAFPGEPLGCA---LNVFRRGWIRAGK-TVAVIGAGFIGLLFLQLAAAAGArRVIAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 182 ARGTEKIQLLKSMGVDHVVDLGTENVISSVkefiktRKL---KGVDVLYDPVG--------GKLTKEsmkvlkwGAQILV 250
Cdd:cd08269  161 DRRPARLALARELGATEVVTDDSEAIVERV------RELtggAGADVVIEAVGhqwpldlaGELVAE-------RGRLVI 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 251 IGFASGEIPVIPANIALVKNWTVHGLYWgsyriHQPNVLEDSIKELLSWLSRGLI--TIHISHTYSLSQANLAFGDLKDR 328
Cdd:cd08269  228 FGYHQDGPRPVPFQTWNWKGIDLINAVE-----RDPRIGLEGMREAVKLIADGRLdlGSLLTHEFPLEELGDAFEAARRR 302

                 ..
gi 332646003 329 KA 330
Cdd:cd08269  303 PD 304
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
13-336 6.82e-13

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: 68.83  E-value: 6.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  13 TATNPGSPesPVEVSKTHPIPSLNSDTSVRVRVIATSLN------YANYLQILgKYQEKPPlpfipGSDYSGIVDAIGPA 86
Cdd:cd08247    5 TFKNNTSP--LTITTIKLPLPNCYKDNEIVVKVHAAALNpvdlklYNSYTFHF-KVKEKGL-----GRDYSGVIVKVGSN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  87 V-TKFRVGDRVCS-----FADLGSFAQFIVADQSRLF----LVPERCDMVAAAALPVAFGTSHVALVHRAR-LTSGQVLL 155
Cdd:cd08247   77 VaSEWKVGDEVCGiyphpYGGQGTLSQYLLVDPKKDKksitRKPENISLEEAAAWPLVLGTAYQILEDLGQkLGPDSKVL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 156 VLGAAGGVGLAAVQIGKVCGAIVIAVARGTEK-IQLLKSMGVDHVVDLGTENVISSVKEFIKTRKLKG-VDVLYDPVGG- 232
Cdd:cd08247  157 VLGGSTSVGRFAIQLAKNHYNIGTVVGTCSSRsAELNKKLGADHFIDYDAHSGVKLLKPVLENVKGQGkFDLILDCVGGy 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 233 KLTKESMKVLKW----GAQILVIGFASGEIPVIPANIALVKNWTVHGLYW----GSYRIH----QPNVleDSIKELLSWL 300
Cdd:cd08247  237 DLFPHINSILKPksknGHYVTIVGDYKANYKKDTFNSWDNPSANARKLFGslglWSYNYQffllDPNA--DWIEKCAELI 314
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 332646003 301 SRGLITIHISHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:cd08247  315 ADGKVKPPIDSVYPFEDYKEAFERLKSNRAKGKVVI 350
PRK10754 PRK10754
NADPH:quinone reductase;
18-332 7.45e-13

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 68.61  E-value: 7.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  18 GSPESPVEVSKTHPIPSLNSdtsVRVRVIATSLNYANYLQILGKYqEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRVC 97
Cdd:PRK10754  11 GGPEVLQAVEFTPADPAENE---VQVENKAIGINYIDTYIRSGLY-PPPSLPSGLGTEAAGVVSKVGSGVKHIKVGDRVV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  98 -SFADLGSFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAAGGVGLAAVQIGKVCGA 176
Cdd:PRK10754  87 yAQSALGAYSSVHNVPADKAAILPDAISFEQAAASFLKGLTVYYLLRKTYEIKPDEQFLFHAAAGGVGLIACQWAKALGA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 177 IVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRKlkgVDVLYDPVGGKLTKESMKVLKWGAQILVIGFASG 256
Cdd:PRK10754 167 KLIGTVGSAQKAQRAKKAGAWQVINYREENIVERVKEITGGKK---VRVVYDSVGKDTWEASLDCLQRRGLMVSFGNASG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 257 eiPVIPANIALVKNwtvhglyWGSYRIHQPNV---------LEDSIKELLSWLSRGLITIHI--SHTYSLSQANLAFGDL 325
Cdd:PRK10754 244 --PVTGVNLGILNQ-------KGSLYVTRPSLqgyittreeLTEASNELFSLIASGVIKVDVaeQQKFPLKDAQRAHEIL 314

                 ....*..
gi 332646003 326 KDRKAIG 332
Cdd:PRK10754 315 ESRATQG 321
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
66-336 1.40e-12

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: 67.64  E-value: 1.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  66 PPLPFIPGSDYSGIVDAIGPAVTKFRVGDRV----------CSF-----------------ADLGSFAQFIVADQSRLFL 118
Cdd:cd08240   64 VKLPLVLGHEIVGEVVAVGPDAADVKVGDKVlvypwigcgeCPVclagdenlcakgralgiFQDGGYAEYVIVPHSRYLV 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 119 VPERCDMVAAAALPVAFGTSHVAlVHRARLTSGQVLLVLGAAGGVGLAAVQIGK-VCGAIVIAVARGTEKIQLLKSMGVD 197
Cdd:cd08240  144 DPGGLDPALAATLACSGLTAYSA-VKKLMPLVADEPVVIIGAGGLGLMALALLKaLGPANIIVVDIDEAKLEAAKAAGAD 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 198 HVVDLgteNVISSVKEFIKTRKlKGVDVLYDPVGGKLT-KESMKVLKWGAQILVIGFASGEIPVIPANIALvKNWTVHGL 276
Cdd:cd08240  223 VVVNG---SDPDAAKRIIKAAG-GGVDAVIDFVNNSATaSLAFDILAKGGKLVLVGLFGGEATLPLPLLPL-RALTIQGS 297
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 277 YWGSyrihqpnvLEDsIKELLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:cd08240  298 YVGS--------LEE-LRELVALAKAGKLKPIPLTERPLSDVNDALDDLKAGKVVGRAVL 348
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
3-331 3.44e-12

Liver alcohol dehydrogenase; 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. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. 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. 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 an 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.


Pssm-ID: 176238 [Multi-domain]  Cd Length: 365  Bit Score: 66.59  E-value: 3.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   3 ALVCRKLGDPTAtnpgspESPVEVSKTHPipslnsdTSVRVRVIATSLNYANYLQILGKYQekPPLPFIPGSDYSGIVDA 82
Cdd:cd08277    5 AAVAWEAGKPLV------IEEIEVAPPKA-------NEVRIKMLATSVCHTDILAIEGFKA--TLFPVILGHEGAGIVES 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  83 IGPAVTKFRVGDRV----------CS-------------------------------------FADLGSFAQFIVADQSR 115
Cdd:cd08277   70 VGEGVTNLKPGDKViplfigqcgeCSncrsgktnlcqkyranesglmpdgtsrftckgkkiyhFLGTSTFSQYTVVDENY 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 116 LFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAAGGVGLAAvqIG-KVCGAI-VIAVARGTEKIQLLKS 193
Cdd:cd08277  150 VAKIDPAAPLEHVCLLGCGFSTGYGAAWNTAKVEPGSTVAVFGLGAVGLSAI--MGaKIAGASrIIGVDINEDKFEKAKE 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 194 MGVDHVVDlgTENVISSVKEFIKTRKLKGVDVLYDPVG-GKLTKESMK--VLKWGAQILVIGFASGEIPVIPANiaLVKN 270
Cdd:cd08277  228 FGATDFIN--PKDSDKPVSEVIREMTGGGVDYSFECTGnADLMNEALEstKLGWGVSVVVGVPPGAELSIRPFQ--LILG 303
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332646003 271 WTVHGLYWGSYRIHQ--PNVLEDSIKEllswlsRGLITIHISHTYSLSQANLAFGDLKDRKAI 331
Cdd:cd08277  304 RTWKGSFFGGFKSRSdvPKLVSKYMNK------KFDLDELITHVLPFEEINKGFDLMKSGECI 360
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
31-336 5.53e-12

Sorbitol dehydrogenase; 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. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. 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: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 65.98  E-value: 5.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  31 PIPSLnSDTSVRVRVIATS-----LNYANYLQIlGKYQEKPPLpfIPGSDYSGIVDAIGPAVTKFRVGDRV--------- 96
Cdd:cd05285   16 PIPEP-GPGEVLVRVRAVGicgsdVHYYKHGRI-GDFVVKEPM--VLGHESAGTVVAVGSGVTHLKVGDRVaiepgvpcr 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  97 -CSF------------------ADLGSFAQFIVADQSRLFLVPERCDMVAAAAL-PVAFGtshVALVHRARLTSGQVLLv 156
Cdd:cd05285   92 tCEFcksgrynlcpdmrfaatpPVDGTLCRYVNHPADFCHKLPDNVSLEEGALVePLSVG---VHACRRAGVRPGDTVL- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 157 lgaaggvglaavqigkVCGA-----IVIAVARGT------------EKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRK 219
Cdd:cd05285  168 ----------------VFGAgpiglLTAAVAKAFgatkvvvtdidpSRLEFAKELGATHTVNVRTEDTPESAEKIAELLG 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 220 LKGVDVLYDPVGgkltKES-----MKVLKWGAQILVIGFASGEIPViPANIALVKNWTVHglywGSYRIHqpNVLEDSIk 294
Cdd:cd05285  232 GKGPDVVIECTG----AESciqtaIYATRPGGTVVLVGMGKPEVTL-PLSAASLREIDIR----GVFRYA--NTYPTAI- 299
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 332646003 295 ELlswLSRGLITIH--ISHTYSLSQANLAFGDLKDRK--AIgKVMI 336
Cdd:cd05285  300 EL---LASGKVDVKplITHRFPLEDAVEAFETAAKGKkgVI-KVVI 341
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
68-267 5.84e-12

(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin. BDH functions as a homodimer. 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. 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.


Pssm-ID: 176195 [Multi-domain]  Cd Length: 351  Bit Score: 66.02  E-value: 5.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  68 LPFIPGSDYSGIVDAIGPAVTKFRVGDRVC-----------------------------SFADlGSFAQFIVADQSRLFL 118
Cdd:cd08233   64 APVTLGHEFSGVVVEVGSGVTGFKVGDRVVveptikcgtcgackrglynlcdslgfiglGGGG-GGFAEYVVVPAYHVHK 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 119 VPERCDMvAAAAL--PVAfgtshVAL--VHRARLTSGQVLLvlgaaggvglaavqigkVCGA-------IVIAVARGTEK 187
Cdd:cd08233  143 LPDNVPL-EEAALvePLA-----VAWhaVRRSGFKPGDTAL-----------------VLGAgpiglltILALKAAGASK 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 188 I----------QLLKSMGVDHVVDLGTENVISSVKEfiKTRKlKGVDVLYDPVGGKLT-KESMKVLKWGAQILVIGFASG 256
Cdd:cd08233  200 IivsepsearrELAEELGATIVLDPTEVDVVAEVRK--LTGG-GGVDVSFDCAGVQATlDTAIDALRPRGTAVNVAIWEK 276
                        250
                 ....*....|.
gi 332646003 257 EIPVIPANIAL 267
Cdd:cd08233  277 PISFNPNDLVL 287
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
41-97 8.76e-11

Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure.


Pssm-ID: 400513 [Multi-domain]  Cd Length: 106  Bit Score: 58.39  E-value: 8.76e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 332646003   41 VRVRVIATSLNYANYLQILGKyQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRVC 97
Cdd:pfam08240   3 VLVKVKAAGICGSDLHIYKGG-NPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVV 58
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
64-332 9.08e-11

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: 61.52  E-value: 9.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  64 EKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRVCSFadlGSFAQFIVADQSRLFLVPERCDMVAAAALPVAfgtsHVAL- 142
Cdd:cd08255   16 EKLPLPLPPGYSSVGRVVEVGSGVTGFKPGDRVFCF---GPHAERVVVPANLLVPLPDGLPPERAALTALA----ATALn 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 143 -VHRARLTSGQvllvlgaaggvglaavqigKVC----GAIVIAVArgtekiQLLKSMGVDHVVD-------------LGT 204
Cdd:cd08255   89 gVRDAEPRLGE-------------------RVAvvglGLVGLLAA------QLAKAAGAREVVGvdpdaarrelaeaLGP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 205 EN-VISSVKEFIKTRklkGVDVLYDPVGGKLT-KESMKVLKWGAQILVIGFAsGEIPVIP-----ANIALVKNWTVHGLY 277
Cdd:cd08255  144 ADpVAADTADEIGGR---GADVVIEASGSPSAlETALRLLRDRGRVVLVGWY-GLKPLLLgeefhFKRLPIRSSQVYGIG 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332646003 278 WG--SYRIHQPNVLEDSIKELLSWLSRGLITihisHTYSLSQANLAFGDLKDRKAIG 332
Cdd:cd08255  220 RYdrPRRWTEARNLEEALDLLAEGRLEALIT----HRVPFEDAPEAYRLLFEDPPEC 272
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
69-336 1.80e-10

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: 61.44  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  69 PFIPGSDYSGIVDAIGPAVTKFRVGDRV---------------------CSFADL------GSFAQFIVadqsrlflVPE 121
Cdd:cd08261   54 PRILGHELSGEVVEVGEGVAGLKVGDRVvvdpyiscgecyacrkgrpncCENLQVlgvhrdGGFAEYIV--------VPA 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 122 RCDMVA------AAAL--PVAFGTsHValVHRARLTSGQVLLVLGAAGGVGlAAVQIGKVCGAIVIAVARGTEKIQLLKS 193
Cdd:cd08261  126 DALLVPeglsldQAALvePLAIGA-HA--VRRAGVTAGDTVLVVGAGPIGL-GVIQVAKARGARVIVVDIDDERLEFARE 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 194 MGVDHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVGGKLT-KESMKVLKWGAQILVIGFASGEIpVIPANIALVKNWT 272
Cdd:cd08261  202 LGADDTINVGDEDVAARLRELTDGE---GADVVIDATGNPASmEEAVELVAHGGRVVLVGLSKGPV-TFPDPEFHKKELT 277
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332646003 273 VHglywGSyRIHQPNVLEDSIKellsWLSRGLITIH--ISHTYSLSQANLAFGDLKDRKA-IGKVMI 336
Cdd:cd08261  278 IL----GS-RNATREDFPDVID----LLESGKVDPEalITHRFPFEDVPEAFDLWEAPPGgVIKVLI 335
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
66-336 2.28e-10

Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol dehydrogenase, but has some amino acid substitutions near the active site, which may determine the enzyme's specificity of oxidizing aromatic substrates. Also known as aryl-alcohol dehydrogenases, they catalyze the conversion of an aromatic alcohol + NAD+ to an aromatic aldehyde + NADH + 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: 176239 [Multi-domain]  Cd Length: 365  Bit Score: 60.98  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  66 PPLPFIPGSDYSGIVDAIGPAVTKFRVGDRVC-SFADLG----------------------------------------- 103
Cdd:cd08278   53 TPLPAVLGHEGAGVVEAVGSAVTGLKPGDHVVlSFASCGecanclsghpaycenffplnfsgrrpdgstplslddgtpvh 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 104 -------SFAQFIVADQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVlgaaggvglaavqIG----- 171
Cdd:cd08278  133 ghffgqsSFATYAVVHERNVVKVDKDVPLELLAPLGCGIQTGAGAVLNVLKPRPGSSIAV-------------FGagavg 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 172 -------KVCGA-IVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIktrkLKGVDVLYDPVG-GKLTKESMKVL 242
Cdd:cd08278  200 laavmaaKIAGCtTIIAVDIVDSRLELAKELGATHVINPKEEDLVAAIREIT----GGGVDYALDTTGvPAVIEQAVDAL 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 243 KWGAQILVIGFAS--GEIPvIPANIALVKNWTVHGLYWGSyrihqpNVLEDSIKELLSWLSRGLITIH-ISHTYSLSQAN 319
Cdd:cd08278  276 APRGTLALVGAPPpgAEVT-LDVNDLLVSGKTIRGVIEGD------SVPQEFIPRLIELYRQGKFPFDkLVTFYPFEDIN 348
                        330
                 ....*....|....*..
gi 332646003 320 LAFGDLKDRKAIGKVMI 336
Cdd:cd08278  349 QAIADSESGKVIKPVLR 365
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
69-273 7.54e-10

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. 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: 176223 [Multi-domain]  Cd Length: 341  Bit Score: 59.63  E-value: 7.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  69 PFIPGSDYSGIVDAIGPAV-TKFRVGDRVCSFADL-----------------GSFAQFIVADQSRLFLVPERCDMvAAAA 130
Cdd:cd08262   64 DIVLGHEFCGEVVDYGPGTeRKLKVGTRVTSLPLLlcgqgascgiglspeapGGYAEYMLLSEALLLRVPDGLSM-EDAA 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 131 L--PVAFGTSHVAlvhRARLTSGQVLLVlgaaggvglaavqIGkvCGAIVIAVA-----RGTEKI----------QLLKS 193
Cdd:cd08262  143 LtePLAVGLHAVR---RARLTPGEVALV-------------IG--CGPIGLAVIaalkaRGVGPIvasdfsperrALALA 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 194 MGVDHVVDLGTENVISSVKEFIKTRKLKGVDVLYDPVGGK-LTKESMKVLKWGAQILVIGFASGEIPVIPAnIALVKNWT 272
Cdd:cd08262  205 MGADIVVDPAADSPFAAWAAELARAGGPKPAVIFECVGAPgLIQQIIEGAPPGGRIVVVGVCMESDNIEPA-LAIRKELT 283

                 .
gi 332646003 273 V 273
Cdd:cd08262  284 L 284
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
31-334 2.59e-09

Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)- dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. 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. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 57.63  E-value: 2.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  31 PIPSLNSDtSVRVRVIATSlnyanylqILG------KYQE------KPPLpfIPGSDYSGIVDAIGPAVTKFRVGDRV-- 96
Cdd:cd05281   19 PVPKPGPG-EVLIKVLAAS--------ICGtdvhiyEWDEwaqsriKPPL--IFGHEFAGEVVEVGEGVTRVKVGDYVsa 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  97 -------------------CSFADL------GSFAQFIVadqsrlflVPERCDMVAAAALPVAFGTSHVAL---VHRArL 148
Cdd:cd05281   88 ethivcgkcyqcrtgnyhvCQNTKIlgvdtdGCFAEYVV--------VPEENLWKNDKDIPPEIASIQEPLgnaVHTV-L 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 149 TSGQVLLVLGAAGG--VGLAAVQIGKVCGA-IVIAVARGTEKIQLLKSMGVDHVVDLGTENvissVKEFIKTRKLKGVDV 225
Cdd:cd05281  159 AGDVSGKSVLITGCgpIGLMAIAVAKAAGAsLVIASDPNPYRLELAKKMGADVVINPREED----VVEVKSVTDGTGVDV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 226 LYDPVGGKLT-KESMKVLKWGAQILVIGFASGEIPVIPANIALVKNWTVHGLY----WGSYRIHQpnvledsikellSWL 300
Cdd:cd05281  235 VLEMSGNPKAiEQGLKALTPGGRVSILGLPPGPVDIDLNNLVIFKGLTVQGITgrkmFETWYQVS------------ALL 302
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 332646003 301 SRGLITIH--ISHTYSLSQANLAFGDLKDRKAiGKV 334
Cdd:cd05281  303 KSGKVDLSpvITHKLPLEDFEEAFELMRSGKC-GKV 337
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
169-338 4.29e-09

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: 56.99  E-value: 4.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 169 QIGKVCGAIVIAVARGTEKIQLLKS-MGVDHVVDLGTENVissvkefikTRKLK-----GVDVLYDPVGGKLTKESMKVL 242
Cdd:COG2130  165 QIAKLKGCRVVGIAGGAEKCRYLVEeLGFDAAIDYKAGDL---------AAALAaacpdGIDVYFDNVGGEILDAVLPLL 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 243 KWGAQILVIGFASG----EIPVIPANIA--LVKNWTVHGLYWGSYRIHQPnvleDSIKELLSWLSRGLITI--HISHtyS 314
Cdd:COG2130  236 NTFARIAVCGAISQynatEPPPGPRNLGqlLVKRLRMQGFIVFDHADRFP----EFLAELAGWVAEGKLKYreTVVE--G 309
                        170       180
                 ....*....|....*....|....
gi 332646003 315 LSQANLAFGDLKDRKAIGKVMIAL 338
Cdd:COG2130  310 LENAPEAFLGLFEGENFGKLLVKV 333
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
137-336 2.45e-08

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: 54.62  E-value: 2.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  137 TSHVALVHRARLTSGQVLLVLGAAGGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTenvISSVKEFIK 216
Cdd:TIGR02825 125 TAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKVAYLKKLGFDVAFNYKT---VKSLEETLK 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  217 TRKLKGVDVLYDPVGGKLTKESMKVLKWGAQILVIGFAS-----GEIPVIPA-NIALVKNWTVHGLYWGSYrihQPNVLE 290
Cdd:TIGR02825 202 KASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAIStynrtGPLPPGPPpEIVIYQELRMEGFIVNRW---QGEVRQ 278
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 332646003  291 DSIKELLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:TIGR02825 279 KALKELLKWVLEGKIQYKEYVIEGFENMPAAFMGMLKGENLGKTIV 324
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
31-330 4.33e-08

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: 54.20  E-value: 4.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  31 PIPSLNSDTSVRVRVIATSLNYANyLQIL-GKYQEKPPlPFIPGSDYSGIVDAIGPAVTKFRVGDRV----------CSF 99
Cdd:cd05278   18 PDPKIQGPHDAIVRVTATSICGSD-LHIYrGGVPGAKH-GMILGHEFVGEVVEVGSDVKRLKPGDRVsvpcitfcgrCRF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 100 ADL--------------------GSFAQFIV---ADQSrLFLVPERCDMVAAAALPVAFGTSHvalvHRARLTSGQVLLV 156
Cdd:cd05278   96 CRRgyhahcenglwgwklgnridGGQAEYVRvpyADMN-LAKIPDGLPDEDALMLSDILPTGF----HGAELAGIKPGST 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 157 LGAaggvglaavqIGkvCGAI---------------VIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRklk 221
Cdd:cd05278  171 VAV----------IG--AGPVglcavagarllgaarIIAVDSNPERLDLAKEAGATDIINPKNGDIVEQILELTGGR--- 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 222 GVDVLYDPVGGKLTKES-MKVLKWGAQILVIGFASGEIPVIPANIALVKNWTVHglyWG--SYRIHQPnvledsikELLS 298
Cdd:cd05278  236 GVDCVIEAVGFEETFEQaVKVVRPGGTIANVGVYGKPDPLPLLGEWFGKNLTFK---TGlvPVRARMP--------ELLD 304
                        330       340       350
                 ....*....|....*....|....*....|....
gi 332646003 299 WLSRGLI--TIHISHTYSLSQANLAFGDLKDRKA 330
Cdd:cd05278  305 LIEEGKIdpSKLITHRFPLDDILKAYRLFDNKPD 338
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
69-285 2.49e-07

Cinnamyl alcohol dehydrogenases (CAD); 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: 176186 [Multi-domain]  Cd Length: 337  Bit Score: 51.73  E-value: 2.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  69 PFIPGSDYSGIVDAIGPAVTKFRVGDRV-----------CSF------------------------ADLGSFAQFIVADQ 113
Cdd:cd05283   54 PLVPGHEIVGIVVAVGSKVTKFKVGDRVgvgcqvdscgtCEQcksgeeqycpkgvvtyngkypdgtITQGGYADHIVVDE 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 114 SRLFLVPERCDMVAAAAL---------P-VAFG---TSHVALV------HRArltsgqvllvlgaaggvglaaVQIGKVC 174
Cdd:cd05283  134 RFVFKIPEGLDSAAAAPLlcagitvysPlKRNGvgpGKRVGVVgigglgHLA---------------------VKFAKAL 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 175 GAIVIAVARGTEKIQLLKSMGVDHVVDlgtenviSSVKEFIKTRKlKGVDVLYDPVGGKLTKES-MKVLKWGAQILVIGF 253
Cdd:cd05283  193 GAEVTAFSRSPSKKEDALKLGADEFIA-------TKDPEAMKKAA-GSLDLIIDTVSASHDLDPyLSLLKPGGTLVLVGA 264
                        250       260       270
                 ....*....|....*....|....*....|..
gi 332646003 254 ASGEIPVIPANIaLVKNWTVHGLYWGSYRIHQ 285
Cdd:cd05283  265 PEEPLPVPPFPL-IFGRKSVAGSLIGGRKETQ 295
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
1-338 2.68e-07

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; Glutathione-dependent formaldehyde dehydrogenases (FDHs) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD to formate and NADH. 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. These tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. 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: 176244 [Multi-domain]  Cd Length: 344  Bit Score: 51.49  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGDptatnpgspespVEVsKTHPIPSLNSDTSVRVRVIATSLNYANyLQIL-GKYqeKPPLPFIPGSDYSGI 79
Cdd:cd08284    1 MKAVVFKGPGD------------VRV-EEVPIPQIQDPTDAIVKVTAAAICGSD-LHIYrGHI--PSTPGFVLGHEFVGE 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  80 VDAIGPAVTKFRVGDRV----------CSFADLGSF---------------------AQFI---VADQSrLFLVPERCDM 125
Cdd:cd08284   65 VVEVGPEVRTLKVGDRVvspftiacgeCFYCRRGQSgrcakgglfgyagspnldgaqAEYVrvpFADGT-LLKLPDGLSD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 126 VAAAALPVAFGTSHVAlVHRARLTSGqvllvlgaaggvgLAAVQIG------------KVCGA-IVIAVARGTEKIQLLK 192
Cdd:cd08284  144 EAALLLGDILPTGYFG-AKRAQVRPG-------------DTVAVIGcgpvglcavlsaQVLGAaRVFAVDPVPERLERAA 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 193 SMGVdHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVGGKLT-KESMKVLKWGAQILVIGF-ASGEIPViPANIALVKN 270
Cdd:cd08284  210 ALGA-EPINFEDAEPVERVREATEGR---GADVVLEAVGGAAAlDLAFDLVRPGGVISSVGVhTAEEFPF-PGLDAYNKN 284
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332646003 271 WTVHglyWGsyRIHQPNVLEDSIKELLSwlSRGLITIHISHTYSLSQANLAFgDLKDRKAIGKVMIAL 338
Cdd:cd08284  285 LTLR---FG--RCPVRSLFPELLPLLES--GRLDLEFLIDHRMPLEEAPEAY-RLFDKRKVLKVVLDP 344
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
31-231 3.97e-07

formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase (FDH), which is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. This family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Another member is identified as a dihydroxyacetone reductase. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). 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: 176246 [Multi-domain]  Cd Length: 345  Bit Score: 51.10  E-value: 3.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  31 PIPSLNSDTSVRVRVIATSLNYANyLQIL-GKYQEKPPlPFIPGSDYSGIVDAIGPAVTKFRVGDRV----------CSF 99
Cdd:cd08286   18 PKPTIQEPTDAIVKMLKTTICGTD-LHILkGDVPTVTP-GRILGHEGVGVVEEVGSAVTNFKVGDRVliscisscgtCGY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 100 --ADLGS-------------------FAQFIVADQSrLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLG 158
Cdd:cd08286   96 crKGLYShcesggwilgnlidgtqaeYVRIPHADNS-LYKLPEGVDEEAAVMLSDILPTGYECGVLNGKVKPGDTVAIVG 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332646003 159 AAGGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKTRklkGVDVLYDPVG 231
Cdd:cd08286  175 AGPVGLAALLTAQLYSPSKIIMVDLDDNRLEVAKKLGATHTVNSAKGDAIEQVLELTDGR---GVDVVIEAVG 244
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
67-277 4.62e-07

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 50.98  E-value: 4.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  67 PLPFIPGSDYSGIVDAIGPAVTKFRVGDRV-------CSF--------ADL------------GSFAQFIVADQSRLFLV 119
Cdd:PRK05396  56 PVPMVVGHEFVGEVVEVGSEVTGFKVGDRVsgeghivCGHcrncragrRHLcrntkgvgvnrpGAFAEYLVIPAFNVWKI 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 120 PERCDM-VAAAALPvaFGTS-HVAL----VHRARLTSGqvllvlgaaggvglaavqigkvCGAI---VIAVAR--GTEKI 188
Cdd:PRK05396 136 PDDIPDdLAAIFDP--FGNAvHTALsfdlVGEDVLITG----------------------AGPIgimAAAVAKhvGARHV 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 189 ----------QLLKSMGVDHVVDLGTENVISSVKEFIKTrklKGVDVLYDPVG-GKLTKESMKVLKWGAQILVIGFASGE 257
Cdd:PRK05396 192 vitdvneyrlELARKMGATRAVNVAKEDLRDVMAELGMT---EGFDVGLEMSGaPSAFRQMLDNMNHGGRIAMLGIPPGD 268
                        250       260
                 ....*....|....*....|..
gi 332646003 258 IPVipaNIALV--KNWTVHGLY 277
Cdd:PRK05396 269 MAI---DWNKVifKGLTIKGIY 287
PLN02827 PLN02827
Alcohol dehydrogenase-like
24-96 3.16e-06

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 48.36  E-value: 3.16e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332646003  24 VEVSKTHPIpslnsdtSVRVRVIATSLNYANylqiLGKYQEKPPLPFIPGSDYSGIVDAIGPAVTKFRVGDRV 96
Cdd:PLN02827  30 VEVSPPQPL-------EIRIKVVSTSLCRSD----LSAWESQALFPRIFGHEASGIVESIGEGVTEFEKGDHV 91
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
1-334 7.19e-06

Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group contains members identified as zinc dependent alcohol dehydrogenases (ADH), and class III ADG (aka formaldehyde dehydrogenase, FDH). 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. 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. Class III ADH are also know as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to the corresponding carboxylic acid and alcohol. 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: 176241 [Multi-domain]  Cd Length: 371  Bit Score: 47.37  E-value: 7.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003   1 MEALVCRKLGDPTATNPGSPESPVEVSKTHPIPSlnsdtSVRVRVIATSLNYANYLQILGkyqEKP-PLPFIPGSDYSGI 79
Cdd:cd08281    1 MRAAVLRETGAPTPYADSRPLVIEEVELDPPGPG-----EVLVKIAAAGLCHSDLSVING---DRPrPLPMALGHEAAGV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  80 VDAIGPAVTKFRVGDR-VCSFA-----------------------------------------------DLGSFAQFIVA 111
Cdd:cd08281   73 VVEVGEGVTDLEVGDHvVLVFVpscghcrpcaegrpalcepgaaangagtllsggrrlrlrggeinhhlGVSAFAEYAVV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 112 DQSRLFLVPERCDMVAAAALPVAFGTSHVALVHRARLTSGQVLLVLGAAGgvglaavqIG--KVCGAI------VIAVAR 183
Cdd:cd08281  153 SRRSVVKIDKDVPLEIAALFGCAVLTGVGAVVNTAGVRPGQSVAVVGLGG--------VGlsALLGAVaagasqVVAVDL 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 184 GTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKtrklKGVDVLYDPVGGKLTKES-MKVLKWGAQILVIGFASGE--IPV 260
Cdd:cd08281  225 NEDKLALARELGATATVNAGDPNAVEQVRELTG----GGVDYAFEMAGSVPALETaYEITRRGGTTVTAGLPDPEarLSV 300
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332646003 261 IPANIAlVKNWTVHGLYWGSyrihqpNVLEDSIKELLSWLSRGLITIH--ISHTYSLSQANLAFgdlkDRKAIGKV 334
Cdd:cd08281  301 PALSLV-AEERTLKGSYMGS------CVPRRDIPRYLALYLSGRLPVDklLTHRLPLDEINEGF----DRLAAGEA 365
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
67-337 1.03e-05

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, 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: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 46.87  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  67 PLPFIPGSDYSGIVDAIGPAVT------KFRVGDRV-------------------------------CSFAD---LGSFA 106
Cdd:cd08231   53 PLPIILGHEGVGRVVALGGGVTtdvagePLKVGDRVtwsvgapcgrcyrclvgdptkcenrkkygheASCDDphlSGGYA 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 107 QFIVADQ-SRLFLVPERCDMVAAAALPVAFGTShVALVHRARLTSGqvllvlgaaggvglaavqiGKV-----CG----- 175
Cdd:cd08231  133 EHIYLPPgTAIVRVPDNVPDEVAAPANCALATV-LAALDRAGPVGA-------------------GDTvvvqgAGplgly 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 176 AIVIAVARGTEKI----------QLLKSMGVDHVVDLgteNVISSVKEFIKTRKL---KGVDVLYDPVGGKLT-KESMKV 241
Cdd:cd08231  193 AVAAAKLAGARRVividgsperlELAREFGADATIDI---DELPDPQRRAIVRDItggRGADVVIEASGHPAAvPEGLEL 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 242 LKWGAQILVIG--FASGEIPVIPANIALvKNWTVHGLyWGSyrihQPNVLEDSIKELLSWLSRGLITIHISHTYSLSQAN 319
Cdd:cd08231  270 LRRGGTYVLVGsvAPAGTVPLDPERIVR-KNLTIIGV-HNY----DPSHLYRAVRFLERTQDRFPFAELVTHRYPLEDIN 343
                        330
                 ....*....|....*...
gi 332646003 320 LAFGDLKDRKAIgKVMIA 337
Cdd:cd08231  344 EALELAESGTAL-KVVID 360
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
41-256 2.16e-05

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: 45.61  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  41 VRVRVIATSLNYANYLQILGKYQEKPPLPFIPGSDYSGIVDAIGpaVTKFRVGDRV-CSFADLGS-----FAQFIVADQS 114
Cdd:cd05280   30 VLIRVHYSSLNYKDALAATGNGGVTRNYPHTPGIDAAGTVVSSD--DPRFREGDEVlVTGYDLGMntdggFAEYVRVPAD 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 115 RLFLVPE----RCDMV---AA--AALPVAFGTSHVALVHRARL-----TSGqvllvlgaaggVGLAAVQIGKVCGAIVIA 180
Cdd:cd05280  108 WVVPLPEglslREAMIlgtAGftAALSVHRLEDNGQTPEDGPVlvtgaTGG-----------VGSIAVAILAKLGYTVVA 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332646003 181 VARGTEKIQLLKSMGVDHVV---DLGTEnvisSVKEFIKTRKLKGVDVlydpVGGKLTKESMKVLKWGAQILVIGFASG 256
Cdd:cd05280  177 LTGKEEQADYLKSLGASEVLdreDLLDE----SKKPLLKARWAGAIDT----VGGDVLANLLKQTKYGGVVASCGNAAG 247
PTGR2 cd08293
Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the ...
73-336 3.44e-05

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: 45.07  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  73 GSDYSGIVDAIGPAVTKFRVGDRVCSFAdlGSFAQFIVADQSRLFLV-PERCD-----MVAAAALPVAfgTSHVALVHRA 146
Cdd:cd08293   73 VLDGGGVGVVEESKHQKFAVGDIVTSFN--WPWQTYAVLDGSSLEKVdPQLVDghlsyFLGAVGLPGL--TALIGIQEKG 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 147 RLTSG--QVLLVLGAAGGVGLAAVQIGKVCG-AIVIAVARGTEKIQLLKS-MGVDHVVDLGTENVISSVKEFIKtrklKG 222
Cdd:cd08293  149 HITPGanQTMVVSGAAGACGSLAGQIGRLLGcSRVVGICGSDEKCQLLKSeLGFDAAINYKTDNVAERLRELCP----EG 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 223 VDVLYDPVGGKLTKESMKVLKWGAQILVIGFAS---GEIPVIP------ANIALVKNWTVHGLYWGSYRihqpNVLEDSI 293
Cdd:cd08293  225 VDVYFDNVGGEISDTVISQMNENSHIILCGQISqynKDVPYPPplpeatEAILKERNITRERFLVLNYK----DKFEEAI 300
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 332646003 294 KELLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:cd08293  301 AQLSQWVKEGKLKVKETVYEGLENAGEAFQSMMNGGNIGKQIV 343
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
17-96 6.98e-05

class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group includes alcohol dehydrogenases corresponding to mammalian classes I, II, IV. 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: 176259 [Multi-domain]  Cd Length: 373  Bit Score: 44.23  E-value: 6.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  17 PGSPES--PVEVS--KTHpipslnsdtSVRVRVIATSLNYANYLQILGKyqEKPPLPFIPGSDYSGIVDAIGPAVTKFRV 92
Cdd:cd08299   16 PKKPFSieEIEVAppKAH---------EVRIKIVATGICRSDDHVVSGK--LVTPFPVILGHEAAGIVESVGEGVTTVKP 84

                 ....
gi 332646003  93 GDRV 96
Cdd:cd08299   85 GDKV 88
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
31-199 7.94e-05

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 44.06  E-value: 7.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  31 PIPSLNSDTSVRVRVIATSLNYANYLQILGKYQEKPPLPFipGSDYSGIVDAIGPAVTKFRVGDRV-------------- 96
Cdd:PRK10309  18 PIPEIKHQDDVLVKVASSGLCGSDIPRIFKNGAHYYPITL--GHEFSGYVEAVGSGVDDLHPGDAVacvpllpcftcpec 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  97 -------CSFADL------GSFAQFIVADQSRLFLVPERCDMVAAAAL-PVAFGtshVALVHRARLTSGQvLLVLGAAGG 162
Cdd:PRK10309  96 lrgfyslCAKYDFigsrrdGGNAEYIVVKRKNLFALPTDMPIEDGAFIePITVG---LHAFHLAQGCEGK-NVIIIGAGT 171
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 332646003 163 VGLAAVQIGKVCGA-IVIAVARGTEKIQLLKSMGVDHV 199
Cdd:PRK10309 172 IGLLAIQCAVALGAkSVTAIDINSEKLALAKSLGAMQT 209
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
31-107 5.05e-04

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: 41.75  E-value: 5.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  31 PIPSLNSDTSVRVRVIATSLN------YANYLQILGKyqekpplPFIPGSDYSGIVDAIGPAVTKFRVGDRV-------- 96
Cdd:cd08283   18 PDPKIEDPTDAIVRVTATAICgsdlhlYHGYIPGMKK-------GDILGHEFMGVVEEVGPEVRNLKVGDRVvvpftiac 90
                         90
                 ....*....|...
gi 332646003  97 --CSFADLGSFAQ 107
Cdd:cd08283   91 geCFYCKRGLYSQ 103
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
89-308 6.91e-04

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: 41.09  E-value: 6.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  89 KFRVGDRVCsfADLGSFAQFIV--ADQSRLFLVPERCDMVAAAALPV-AFG----TSHVALVHRARLTSGQVLLVLGAAG 161
Cdd:cd08294   77 KFPVGTIVV--ASFGWRTHTVSdgKDQPDLYKLPADLPDDLPPSLALgVLGmpglTAYFGLLEICKPKAGETVVVNGAAG 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 162 GVGLAAVQIGKVCGAIVIAVARGTEKIQLLKSMGVDHVVDLGTENVISSVKEFIKtrklKGVDVLYDPVGGKLTKESMKV 241
Cdd:cd08294  155 AVGSLVGQIAKIKGCKVIGCAGSDDKVAWLKELGFDAVFNYKTVSLEEALKEAAP----DGIDCYFDNVGGEFSSTVLSH 230
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332646003 242 LKWGAQILVIGFASG--EIPVIPANIA----LVKNWTVHGLYWGSYRIHQPnvleDSIKELLSWLSRGLITIH 308
Cdd:cd08294  231 MNDFGRVAVCGSISTynDKEPKKGPYVqetiIFKQLKMEGFIVYRWQDRWP----EALKQLLKWIKEGKLKYR 299
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
78-262 7.48e-04

NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol dehydrogenases; they exist as tetramers and exhibit specificity for NADP(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like other zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric ADHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains; however, they do not have and a structural zinc in a lobe of the catalytic domain. 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: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 41.07  E-value: 7.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  78 GIVDAIGPAVTKFRVGDRV---------------------CS-------FADL--GSFAQ-FIVAD-QSRLFLVPERCDM 125
Cdd:cd08285   63 GVVEEVGSEVKDFKPGDRVivpaitpdwrsvaaqrgypsqSGgmlggwkFSNFkdGVFAEyFHVNDaDANLAPLPDGLTD 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 126 VAAAALPVAFGTSHVAlVHRARLTSGQVLLVLGaaggvglaavqIGKV----------CGA-IVIAVARGTEKIQLLKSM 194
Cdd:cd08285  143 EQAVMLPDMMSTGFHG-AELANIKLGDTVAVFG-----------IGPVglmavagarlRGAgRIIAVGSRPNRVELAKEY 210
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 195 GVDHVVDLGTENVissVKEFIKTRKLKGVDVLYDPVGGKLTKES-MKVLKWGAQILVIGFASGEIPV-IP 262
Cdd:cd08285  211 GATDIVDYKNGDV---VEQILKLTGGKGVDAVIIAGGGQDTFEQaLKVLKPGGTISNVNYYGEDDYLpIP 277
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
41-256 1.10e-03

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: 40.39  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  41 VRVRVIATSLNYANYL------QILGKYqekpplPFIPGSDYSGIVdaIGPAVTKFRVGDRV-CSFADLG-----SFAQF 108
Cdd:cd08289   30 VLIRVAYSSVNYKDGLasipggKIVKRY------PFIPGIDLAGTV--VESNDPRFKPGDEViVTSYDLGvshhgGYSEY 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 109 IVADQSRLFLVPERCDMVAAAALPVAFGTSHVAlVHRAR---LTSGQVLLVLG-AAGGVGLAAVQIGKVCGAIVIAVARG 184
Cdd:cd08289  102 ARVPAEWVVPLPKGLTLKEAMILGTAGFTAALS-IHRLEengLTPEQGPVLVTgATGGVGSLAVSILAKLGYEVVASTGK 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332646003 185 TEKIQLLKSMGVDHVVdlGTENVISSVKEFIKTRKLKGVdvlYDPVGGKLTKESMKVLKWGAQILVIGFASG 256
Cdd:cd08289  181 ADAADYLKKLGAKEVI--PREELQEESIKPLEKQRWAGA---VDPVGGKTLAYLLSTLQYGGSVAVSGLTGG 247
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
41-96 3.23e-03

class III alcohol dehydrogenases; 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) 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. 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.


Pssm-ID: 176260 [Multi-domain]  Cd Length: 368  Bit Score: 39.13  E-value: 3.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332646003  41 VRVRVIATSLNYANYLQILGKYQEKPpLPFIPGSDYSGIVDAIGPAVTKFRVGDRV 96
Cdd:cd08300   30 VRIKILATGVCHTDAYTLSGADPEGL-FPVILGHEGAGIVESVGEGVTSVKPGDHV 84
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
24-97 3.38e-03

Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. PFDH converts 2 molecules of aldehydes to corresponding carboxylic acid and alcohol. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of an 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: 176242 [Multi-domain]  Cd Length: 375  Bit Score: 39.11  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  24 VEVsKTHPIPSLNSDTSVRVRVIATSL------NYAnylqilGKYQEKPPLPFipGSDYSGIVDAIGPAVTKFRVGDRVC 97
Cdd:cd08282   12 VAV-EDVPDPKIEHPTDAIVRITTTAIcgsdlhMYR------GRTGAEPGLVL--GHEAMGEVEEVGSAVESLKVGDRVV 82
PLN02702 PLN02702
L-idonate 5-dehydrogenase
32-338 3.67e-03

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 38.99  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  32 IPSLNSDtSVRVRVIA-----TSLNYANYLQIlGKYQEKPPLpfIPGSDYSGIVDAIGPAVTKFRVGDRV-------CSF 99
Cdd:PLN02702  36 LPPLGPH-DVRVRMKAvgicgSDVHYLKTMRC-ADFVVKEPM--VIGHECAGIIEEVGSEVKHLVVGDRValepgisCWR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 100 ADL---------------------GSFAQFIVADQSRLFLVPERCDMVAAAAL-PVAFGtshvalVHRARltsgqVLLVL 157
Cdd:PLN02702 112 CNLckegrynlcpemkffatppvhGSLANQVVHPADLCFKLPENVSLEEGAMCePLSVG------VHACR-----RANIG 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 158 GAAGGVGLAAVQIGKVC-------GA--IVIaVARGTEKIQLLKSMGVDHVVDLGT--ENVISSVKEfIKTRKLKGVDVL 226
Cdd:PLN02702 181 PETNVLVMGAGPIGLVTmlaarafGAprIVI-VDVDDERLSVAKQLGADEIVLVSTniEDVESEVEE-IQKAMGGGIDVS 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 227 YDPVG-GKLTKESMKVLKWGAQILVIGFASGEIPViPANIALVKNWTVHGLYwgSYRIHQPNVLEdsikellsWLSRGLI 305
Cdd:PLN02702 259 FDCVGfNKTMSTALEATRAGGKVCLVGMGHNEMTV-PLTPAAAREVDVVGVF--RYRNTWPLCLE--------FLRSGKI 327
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 332646003 306 TIH--ISHTYSLSQANL--AF-GDLKDRKAIgKVMIAL 338
Cdd:PLN02702 328 DVKplITHRFGFSQKEVeeAFeTSARGGNAI-KVMFNL 364
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
69-336 3.67e-03

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 38.67  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003  69 PFIPGSDYSG-----IVDAIGPavtKFRVGDRVCSFADLGSFAqFIVADQSRLFLVPERCDmvaaaaLPVAFgtsHVALV 143
Cdd:PLN03154  73 PFVPGQRIEGfgvskVVDSDDP---NFKPGDLISGITGWEEYS-LIRSSDNQLRKIQLQDD------IPLSY---HLGLL 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 144 HRARLTS------------GQVLLVLGAAGGVGLAAVQIGKVCGAIVIAVARGTEKIQLLKS-MGVDHVVDLGTE-NVIS 209
Cdd:PLN03154 140 GMAGFTAyagfyevcspkkGDSVFVSAASGAVGQLVGQLAKLHGCYVVGSAGSSQKVDLLKNkLGFDEAFNYKEEpDLDA 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646003 210 SVKEFIKtrklKGVDVLYDPVGGKLTKESMKVLKWGAQILVIGFASGEIPVIPANI-----ALVKNWTVHGLYWGSYRIH 284
Cdd:PLN03154 220 ALKRYFP----EGIDIYFDNVGGDMLDAALLNMKIHGRIAVCGMVSLNSLSASQGIhnlynLISKRIRMQGFLQSDYLHL 295
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 332646003 285 QPNVLEDsikeLLSWLSRGLITIHISHTYSLSQANLAFGDLKDRKAIGKVMI 336
Cdd:PLN03154 296 FPQFLEN----VSRYYKQGKIVYIEDMSEGLESAPAALVGLFSGKNVGKQVI 343
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
69-96 9.49e-03

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 37.55  E-value: 9.49e-03
                         10        20
                 ....*....|....*....|....*...
gi 332646003  69 PFIPGSDYSGIVDAIGPAVTKFRVGDRV 96
Cdd:PLN02586  67 PIVPGHEIVGIVTKLGKNVKKFKEGDRV 94
 
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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