NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446028188|ref|WP_000106043|]
View 

MULTISPECIES: L-galactonate oxidoreductase [Enterobacteriaceae]

Protein Classification

zinc-binding alcohol dehydrogenase family protein( domain architecture ID 10169614)

zinc-binding alcohol dehydrogenase family protein similar to Escherichia coli L-galactonate-5-dehydrogenase that catalyzes the oxidation of L-galactonate to D-tagaturonate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
4-340 8.56e-170

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: 475.53  E-value: 8.56e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQ 83
Cdd:cd08261    1 MKALVCEKPGRLEVVDIPEPVPGAGEVLVRVKRVGICGSDLHIYHGRNPFASYPRILGHELSGEVVEVGEGVAGLKVGDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  84 VAVIPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILPADGIDPQAAALIEPFAISAHAVRRAAIAPG 163
Cdd:cd08261   81 VVVDPYISCGECYACRKGRPNCCENLQVLGVHRDGGFAEYIVVPADALLVPEGLSLDQAALVEPLAIGAHAVRRAGVTAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 164 EQVLVVGAGPIGLGAAAIAKADGAQVVVADTSPARREHVATRLELPVLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQHA 243
Cdd:cd08261  161 DTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERLEFARELGADDTINVGDEDVAARLRELTDGEGADVVIDATGNPAS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 244 MNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMMLTHRYPFATLAETY 323
Cdd:cd08261  241 MEEAVELVAHGGRVVLVGLSKGPVTFPDPEFHKKELTILGSRNATREDFPDVIDLLESGKVDPEALITHRFPFEDVPEAF 320
                        330
                 ....*....|....*..
gi 446028188 324 ERDVINNRELIKGVITF 340
Cdd:cd08261  321 DLWEAPPGGVIKVLIEF 337
 
Name Accession Description Interval E-value
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
4-340 8.56e-170

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: 475.53  E-value: 8.56e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQ 83
Cdd:cd08261    1 MKALVCEKPGRLEVVDIPEPVPGAGEVLVRVKRVGICGSDLHIYHGRNPFASYPRILGHELSGEVVEVGEGVAGLKVGDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  84 VAVIPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILPADGIDPQAAALIEPFAISAHAVRRAAIAPG 163
Cdd:cd08261   81 VVVDPYISCGECYACRKGRPNCCENLQVLGVHRDGGFAEYIVVPADALLVPEGLSLDQAALVEPLAIGAHAVRRAGVTAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 164 EQVLVVGAGPIGLGAAAIAKADGAQVVVADTSPARREHVATRLELPVLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQHA 243
Cdd:cd08261  161 DTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERLEFARELGADDTINVGDEDVAARLRELTDGEGADVVIDATGNPAS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 244 MNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMMLTHRYPFATLAETY 323
Cdd:cd08261  241 MEEAVELVAHGGRVVLVGLSKGPVTFPDPEFHKKELTILGSRNATREDFPDVIDLLESGKVDPEALITHRFPFEDVPEAF 320
                        330
                 ....*....|....*..
gi 446028188 324 ERDVINNRELIKGVITF 340
Cdd:cd08261  321 DLWEAPPGGVIKVLIEF 337
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
4-340 9.89e-126

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: 363.69  E-value: 9.89e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQ 83
Cdd:COG1063    1 MKALVLHGPGDLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  84 VAVIPYVACQQCPACKSGRTNCCEKISVIGV-HQDGGFSEYLSVPVANILPA-DGIDPQAAALIEPFAISAHAVRRAAIA 161
Cdd:COG1063   81 VVVEPNIPCGECRYCRRGRYNLCENLQFLGIaGRDGGFAEYVRVPAANLVKVpDGLSDEAAALVEPLAVALHAVERAGVK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 162 PGEQVLVVGAGPIGLGAAAIAKAD-GAQVVVADTSPARREhVATRLELP-VLDPSAEDFDAQLRAQFGGSLAQKVIDATG 239
Cdd:COG1063  161 PGDTVLVIGAGPIGLLAALAARLAgAARVIVVDRNPERLE-LARELGADaVVNPREEDLVEAVRELTGGRGADVVIEAVG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 240 NQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMMLTHRYPFATL 319
Cdd:COG1063  240 APAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPLITHRFPLDDA 319
                        330       340
                 ....*....|....*....|.
gi 446028188 320 AETYERDVINNRELIKGVITF 340
Cdd:COG1063  320 PEAFEAAADRADGAIKVVLDP 340
PRK10083 PRK10083
putative oxidoreductase; Provisional
4-340 2.66e-59

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 194.19  E-value: 2.66e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQ 83
Cdd:PRK10083   1 MKSIVIEKPNSLAIEERPIPQPAAGEVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGEGVDAARIGER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  84 VAVIPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILP-ADGIDPQAAALIEPFAISAHAVRRAAIAP 162
Cdd:PRK10083  81 VAVDPVISCGHCYPCSIGKPNVCTSLVVLGVHRDGGFSEYAVVPAKNAHRiPDAIADQYAVMVEPFTIAANVTGRTGPTE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 163 GEQVLVVGAGPIGLGAAAIAKA--DGAQVVVADtsparreHVATRLELP-------VLDPSAEDFDAQLRAQfgGSLAQK 233
Cdd:PRK10083 161 QDVALIYGAGPVGLTIVQVLKGvyNVKAVIVAD-------RIDERLALAkesgadwVINNAQEPLGEALEEK--GIKPTL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 234 VIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSR-NATpeDFAKVGRLMAEGKITADMMLTH 312
Cdd:PRK10083 232 IIDAACHPSILEEAVTLASPAARIVLMGFSSEPSEIVQQGITGKELSIFSSRlNAN--KFPVVIDWLSKGLIDPEKLITH 309
                        330       340
                 ....*....|....*....|....*...
gi 446028188 313 RYPFATLAETYERDVINNRELIKGVITF 340
Cdd:PRK10083 310 TFDFQHVADAIELFEKDQRHCCKVLLTF 337
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
28-133 1.49e-42

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: 143.13  E-value: 1.49e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   28 NEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYVACQQCPACKSGRTNCCE 107
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYNLCP 80
                          90       100
                  ....*....|....*....|....*.
gi 446028188  108 KISVIGVHQDGGFSEYLSVPVANILP 133
Cdd:pfam08240  81 NGRFLGYDRDGGFAEYVVVPERNLVP 106
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
112-262 4.29e-05

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


Pssm-ID: 274315 [Multi-domain]  Cd Length: 323  Bit Score: 44.86  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  112 IGVHQDGGFSEYLSVPVANILP-ADGIDP-QAAAL-IEPF--AISAHAVRRAAIAPGE-QVLVVGA-GPIG--------- 175
Cdd:TIGR02823  89 LGVSHDGGYSQYARVPADWLVPlPEGLSLrEAMALgTAGFtaALSVMALERNGLTPEDgPVLVTGAtGGVGslavailsk 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  176 LGAAaiakadgaqvVVADTspARREHVATRLEL---PVLDPsaEDFDAQLR----AQFGGslaqkVIDATGNqHAMNNTV 248
Cdd:TIGR02823 169 LGYE----------VVAST--GKAEEEDYLKELgasEVIDR--EDLSPPGKplekERWAG-----AVDTVGG-HTLANVL 228
                         170
                  ....*....|....
gi 446028188  249 NLIRHGGTVVFVGL 262
Cdd:TIGR02823 229 AQLKYGGAVAACGL 242
 
Name Accession Description Interval E-value
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
4-340 8.56e-170

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: 475.53  E-value: 8.56e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQ 83
Cdd:cd08261    1 MKALVCEKPGRLEVVDIPEPVPGAGEVLVRVKRVGICGSDLHIYHGRNPFASYPRILGHELSGEVVEVGEGVAGLKVGDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  84 VAVIPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILPADGIDPQAAALIEPFAISAHAVRRAAIAPG 163
Cdd:cd08261   81 VVVDPYISCGECYACRKGRPNCCENLQVLGVHRDGGFAEYIVVPADALLVPEGLSLDQAALVEPLAIGAHAVRRAGVTAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 164 EQVLVVGAGPIGLGAAAIAKADGAQVVVADTSPARREHVATRLELPVLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQHA 243
Cdd:cd08261  161 DTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERLEFARELGADDTINVGDEDVAARLRELTDGEGADVVIDATGNPAS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 244 MNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMMLTHRYPFATLAETY 323
Cdd:cd08261  241 MEEAVELVAHGGRVVLVGLSKGPVTFPDPEFHKKELTILGSRNATREDFPDVIDLLESGKVDPEALITHRFPFEDVPEAF 320
                        330
                 ....*....|....*..
gi 446028188 324 ERDVINNRELIKGVITF 340
Cdd:cd08261  321 DLWEAPPGGVIKVLIEF 337
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
4-340 9.89e-126

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: 363.69  E-value: 9.89e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQ 83
Cdd:COG1063    1 MKALVLHGPGDLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  84 VAVIPYVACQQCPACKSGRTNCCEKISVIGV-HQDGGFSEYLSVPVANILPA-DGIDPQAAALIEPFAISAHAVRRAAIA 161
Cdd:COG1063   81 VVVEPNIPCGECRYCRRGRYNLCENLQFLGIaGRDGGFAEYVRVPAANLVKVpDGLSDEAAALVEPLAVALHAVERAGVK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 162 PGEQVLVVGAGPIGLGAAAIAKAD-GAQVVVADTSPARREhVATRLELP-VLDPSAEDFDAQLRAQFGGSLAQKVIDATG 239
Cdd:COG1063  161 PGDTVLVIGAGPIGLLAALAARLAgAARVIVVDRNPERLE-LARELGADaVVNPREEDLVEAVRELTGGRGADVVIEAVG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 240 NQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMMLTHRYPFATL 319
Cdd:COG1063  240 APAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPLITHRFPLDDA 319
                        330       340
                 ....*....|....*....|.
gi 446028188 320 AETYERDVINNRELIKGVITF 340
Cdd:COG1063  320 PEAFEAAADRADGAIKVVLDP 340
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
4-338 2.22e-89

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: 271.41  E-value: 2.22e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFsYPRVLGHEICGEIVGLGKNIANLKNGQQ 83
Cdd:cd08236    1 MKALVLTGPGDLRYEDIPKPEPGPGEVLVKVKACGICGSDIPRYLGTGAYH-PPLVLGHEFSGTVEEVGSGVDDLAVGDR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  84 VAVIPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILP-ADGIDPQAAALIEPFAISAHAVRRAAIAP 162
Cdd:cd08236   80 VAVNPLLPCGKCEYCKKGEYSLCSNYDYIGSRRDGAFAEYVSVPARNLIKiPDHVDYEEAAMIEPAAVALHAVRLAGITL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 163 GEQVLVVGAGPIG-LGAAAIAKADGAQVVVADTSPARREhVATRLELP-VLDPSAEDFDaQLRAQFGGSLAQKVIDATGN 240
Cdd:cd08236  160 GDTVVVIGAGTIGlLAIQWLKILGAKRVIAVDIDDEKLA-VARELGADdTINPKEEDVE-KVRELTEGRGADLVIEAAGS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 241 QHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHK---KETTMMGSRNAT-----PEDFAKVGRLMAEGKITADMMLTH 312
Cdd:cd08236  238 PATIEQALALARPGGKVVLVGIPYGDVTLSEEAFEKilrKELTIQGSWNSYsapfpGDEWRTALDLLASGKIKVEPLITH 317
                        330       340
                 ....*....|....*....|....*.
gi 446028188 313 RYPFATLAETYERDVINNRELIKGVI 338
Cdd:cd08236  318 RLPLEDGPAAFERLADREEFSGKVLL 343
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
4-325 2.18e-83

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 255.81  E-value: 2.18e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKE-LVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQ 82
Cdd:COG1064    1 MKAAVLTEPGGpLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGVTGFKVGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  83 QVAVIPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILP-ADGIDP-QAAALIEPFAISAHAVRRAAI 160
Cdd:COG1064   81 RVGVGWVDSCGTCEYCRSGRENLCENGRFTGYTTDGGYAEYVVVPARFLVKlPDGLDPaEAAPLLCAGITAYRALRRAGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 161 APGEQVLVVGAGPIGLGAAAIAKADGAQVVVADTSPARREHvATRL---ElpVLDPSAEDFDAQLRAQFGgslAQKVIDA 237
Cdd:COG1064  161 GPGDRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPEKLEL-ARELgadH--VVNSSDEDPVEAVRELTG---ADVVIDT 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 238 TGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADmmlTHRYPFA 317
Cdd:COG1064  235 VGAPATVNAALALLRRGGRLVLVGLPGGPIPLPPFDLILKERSIRGSLIGTRADLQEMLDLAAEGKIKPE---VETIPLE 311

                 ....*...
gi 446028188 318 TLAETYER 325
Cdd:COG1064  312 EANEALER 319
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
4-339 1.02e-80

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: 249.43  E-value: 1.02e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQ 83
Cdd:cd08235    1 MKAAVLHGPNDVRLEEVPVPEPGPGEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGDGVTGFKVGDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  84 VAVIPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVP-------VANILPaDGIDPQAAALIEPFAISAHAVR 156
Cdd:cd08235   81 VFVAPHVPCGECHYCLRGNENMCPNYKKFGNLYDGGFAEYVRVPawavkrgGVLKLP-DNVSFEEAALVEPLACCINAQR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 157 RAAIAPGEQVLVVGAGPIG-LGAAAIAKADGAQVVVADTSPARREHVATRLELPVLDPSAEDFDAQLRAQFGGSLAQKVI 235
Cdd:cd08235  160 KAGIKPGDTVLVIGAGPIGlLHAMLAKASGARKVIVSDLNEFRLEFAKKLGADYTIDAAEEDLVEKVRELTDGRGADVVI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 236 DATGNQHAMNNTVNLIRHGGTVV-FVGLFKGELQFSDPE-FHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMMLTHR 313
Cdd:cd08235  240 VATGSPEAQAQALELVRKGGRILfFGGLPKGSTVNIDPNlIHYREITITGSYAASPEDYKEALELIASGKIDVKDLITHR 319
                        330       340
                 ....*....|....*....|....*.
gi 446028188 314 YPFATLAETYERdvINNRELIKGVIT 339
Cdd:cd08235  320 FPLEDIEEAFEL--AADGKSLKIVIT 343
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
19-332 3.94e-79

(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: 245.53  E-value: 3.94e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  19 QREIPIPGDNEALIKIKSVGICGTDIHAW-GGnqPFF------------SYPRVLGHEICGEIVGLGKNIANLKNGQQVA 85
Cdd:cd08233   16 EVPEPPVKPGEVKIKVAWCGICGSDLHEYlDG--PIFipteghphltgeTAPVTLGHEFSGVVVEVGSGVTGFKVGDRVV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  86 VIPYVACQQCPACKSGRTNCCEKISVIGVH-QDGGFSEYLSVPVANILP-ADGIDPQAAALIEPFAISAHAVRRAAIAPG 163
Cdd:cd08233   94 VEPTIKCGTCGACKRGLYNLCDSLGFIGLGgGGGGFAEYVVVPAYHVHKlPDNVPLEEAALVEPLAVAWHAVRRSGFKPG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 164 EQVLVVGAGPIGLGAAAIAKAD-GAQVVVADTSPARREHVATRLELPVLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQH 242
Cdd:cd08233  174 DTALVLGAGPIGLLTILALKAAgASKIIVSEPSEARRELAEELGATIVLDPTEVDVVAEVRKLTGGGGVDVSFDCAGVQA 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 243 AMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMMLTHRYPFATLAET 322
Cdd:cd08233  254 TLDTAIDALRPRGTAVNVAIWEKPISFNPNDLVLKEKTLTGSICYTREDFEEVIDLLASGKIDAEPLITSRIPLEDIVEK 333
                        330
                 ....*....|
gi 446028188 323 YERDVINNRE 332
Cdd:cd08233  334 GFEELINDKE 343
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
4-339 2.31e-77

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: 240.51  E-value: 2.31e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGnQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQ 83
Cdd:cd08234    1 MKALVYEGPGELEVEEVPVPEPGPDEVLIKVAACGICGTDLHIYEG-EFGAAPPLVPGHEFAGVVVAVGSKVTGFKVGDR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  84 VAVIPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILP-ADGIDPQAAALIEPFAISAHAVRRAAIAP 162
Cdd:cd08234   80 VAVDPNIYCGECFYCRRGRPNLCENLTAVGVTRNGGFAEYVVVPAKQVYKiPDNLSFEEAALAEPLSCAVHGLDLLGIKP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 163 GEQVLVVGAGPIGL---------GaaaiakadGAQVVVADTSPARREhVATRLELP-VLDPSAEDFDAQLRAQFGGslAQ 232
Cdd:cd08234  160 GDSVLVFGAGPIGLllaqllklnG--------ASRVTVAEPNEEKLE-LAKKLGATeTVDPSREDPEAQKEDNPYG--FD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 233 KVIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFS-DP-EFHKKETTMMGSRnATPEDFAKVGRLMAEGKITADMML 310
Cdd:cd08234  229 VVIEATGVPKTLEQAIEYARRGGTVLVFGVYAPDARVSiSPfEIFQKELTIIGSF-INPYTFPRAIALLESGKIDVKGLV 307
                        330       340
                 ....*....|....*....|....*....
gi 446028188 311 THRYPFATLAETYERdvINNRELIKGVIT 339
Cdd:cd08234  308 SHRLPLEEVPEALEG--MRSGGALKVVVV 334
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
12-338 7.56e-69

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: 218.90  E-value: 7.56e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAW--GGNQPFFS-YPRVLGHEICGEIVGLGKNIANLKNGQQVAVIP 88
Cdd:cd05285    7 PGDLRLEERPIPEPGPGEVLVRVRAVGICGSDVHYYkhGRIGDFVVkEPMVLGHESAGTVVAVGSGVTHLKVGDRVAIEP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  89 YVACQQCPACKSGRTNCCEKI---SVIGVHqdGGFSEYLSVP--VANILPaDGIDPQAAALIEPFAISAHAVRRAAIAPG 163
Cdd:cd05285   87 GVPCRTCEFCKSGRYNLCPDMrfaATPPVD--GTLCRYVNHPadFCHKLP-DNVSLEEGALVEPLSVGVHACRRAGVRPG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 164 EQVLVVGAGPIGL---------GaaaiakadGAQVVVADTSPAR----REHVATRLeLPVLDPSAEDFDAQLRAQFGGSL 230
Cdd:cd05285  164 DTVLVFGAGPIGLltaavakafG--------ATKVVVTDIDPSRlefaKELGATHT-VNVRTEDTPESAEKIAELLGGKG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 231 AQKVIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGS---RNatpeDFAKVGRLMAEGKITAD 307
Cdd:cd05285  235 PDVVIECTGAESCIQTAIYATRPGGTVVLVGMGKPEVTLPLSAASLREIDIRGVfryAN----TYPTAIELLASGKVDVK 310
                        330       340       350
                 ....*....|....*....|....*....|.
gi 446028188 308 MMLTHRYPFATLAETYERDVINNRELIKGVI 338
Cdd:cd05285  311 PLITHRFPLEDAVEAFETAAKGKKGVIKVVI 341
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
20-302 1.64e-65

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: 209.09  E-value: 1.64e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  20 REIPIP--GDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQV-AVIPYVACQQCP 96
Cdd:cd08258   17 REVPEPepGPGEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEVGPDVEGWKVGDRVvSETTFSTCGRCP 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  97 ACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANI--LPaDGIDPQAAALIEPFAISAHAV-RRAAIAPGEQVLVVGAGP 173
Cdd:cd08258   97 YCRRGDYNLCPHRKGIGTQADGGFAEYVLVPEESLheLP-ENLSLEAAALTEPLAVAVHAVaERSGIRPGDTVVVFGPGP 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 174 IGLGAAAIAKADGAQVVVADTSP-ARREHVATRLELPVLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQHAMNNTVNLIR 252
Cdd:cd08258  176 IGLLAAQVAKLQGATVVVVGTEKdEVRLDVAKELGADAVNGGEEDLAELVNEITDGDGADVVIECSGAVPALEQALELLR 255
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446028188 253 HGGTVVFVGLFkGELQFS-DPEFHK-KETTMMGSRNATPEDFAKVGRLMAEG 302
Cdd:cd08258  256 KGGRIVQVGIF-GPLAASiDVERIIqKELSVIGSRSSTPASWETALRLLASG 306
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
11-325 1.10e-63

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: 205.17  E-value: 1.10e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  11 QPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHA-WGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPY 89
Cdd:cd08254   10 SKGLLVLEEVPVPEPGPGEVLVKVKAAGVCHSDLHIlDGGVPTLTKLPLTLGHEIAGTVVEVGAGVTNFKVGDRVAVPAV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  90 VACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILPA-DGIDP-QAAALIEPFAISAHAVRRAA-IAPGEQV 166
Cdd:cd08254   90 IPCGACALCRRGRGNLCLNQGMPGLGIDGGFAEYIVVPARALVPVpDGVPFaQAAVATDAVLTPYHAVVRAGeVKPGETV 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 167 LVVGAGPIGLGAAAIAKADGAQVVVADTSPARREhVATRLELPVLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQHAMNN 246
Cdd:cd08254  170 LVIGLGGLGLNAVQIAKAMGAAVIAVDIKEEKLE-LAKELGADEVLNSLDDSPKDKKAAGLGGGFDVIFDFVGTQPTFED 248
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446028188 247 TVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITadmMLTHRYPFATLAETYER 325
Cdd:cd08254  249 AQKAVKPGGRIVVVGLGRDKLTVDLSDLIARELRIIGSFGGTPEDLPEVLDLIAKGKLD---PQVETRPLDEIPEVLER 324
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
29-299 3.02e-63

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: 202.17  E-value: 3.02e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  29 EALIKIKSVGICGTDIHAW-GGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYVACQQCPACKsgrtNCCE 107
Cdd:cd05188    1 EVLVRVEAAGLCGTDLHIRrGGYPPPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNLGCGTCELCR----ELCP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 108 KISVIGVHQDGGFSEYLSVPVANILPA-DGIDP-QAAALIEPFAISAHAVRRAA-IAPGEQVLVVGAGPIGLGAAAIAKA 184
Cdd:cd05188   77 GGGILGEGLDGGFAEYVVVPADNLVPLpDGLSLeEAALLPEPLATAYHALRRAGvLKPGDTVLVLGAGGVGLLAAQLAKA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 185 DGAQVVVADTSPARREHVATRLELPVLDPSAEDFDAQLRAQFGGsLAQKVIDATGNQHAMNNTVNLIRHGGTVVFVGLFK 264
Cdd:cd05188  157 AGARVIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRLTGGG-GADVVIDAVGGPETLAQALRLLRPGGRIVVVGGTS 235
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446028188 265 GELQFSDP-EFHKKETTMMGSRNATPEDFAKVGRLM 299
Cdd:cd05188  236 GGPPLDDLrRLLFKELTIIGSTGGTREDFEEALDLL 271
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
12-324 2.28e-60

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: 196.69  E-value: 2.28e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAW--GGNQPF-FSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIP 88
Cdd:cd08232    6 AGDLRVEERPAPEPGPGEVRVRVAAGGICGSDLHYYqhGGFGTVrLREPMVLGHEVSGVVEAVGPGVTGLAPGQRVAVNP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  89 YVACQQCPACKSGRTNCCEKISVIGV-----HQDGGFSEYLSVPVANILP-ADGIDPQAAALIEPFAISAHAVRRAAIAP 162
Cdd:cd08232   86 SRPCGTCDYCRAGRPNLCLNMRFLGSamrfpHVQGGFREYLVVDASQCVPlPDGLSLRRAALAEPLAVALHAVNRAGDLA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 163 GEQVLVVGAGPIG-LGAAAIAKADGAQVVVADTSPARREhVATRL---ELPVLDPSAEDFDAQLRAQFggslaQKVIDAT 238
Cdd:cd08232  166 GKRVLVTGAGPIGaLVVAAARRAGAAEIVATDLADAPLA-VARAMgadETVNLARDPLAAYAADKGDF-----DVVFEAS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 239 GNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEdFAKVGRLMAEGKITADMMLTHRYPFAT 318
Cdd:cd08232  240 GAPAALASALRVVRPGGTVVQVGMLGGPVPLPLNALVAKELDLRGSFRFDDE-FAEAVRLLAAGRIDVRPLITAVFPLEE 318

                 ....*.
gi 446028188 319 LAETYE 324
Cdd:cd08232  319 AAEAFA 324
PRK10083 PRK10083
putative oxidoreductase; Provisional
4-340 2.66e-59

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 194.19  E-value: 2.66e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQ 83
Cdd:PRK10083   1 MKSIVIEKPNSLAIEERPIPQPAAGEVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGEGVDAARIGER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  84 VAVIPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILP-ADGIDPQAAALIEPFAISAHAVRRAAIAP 162
Cdd:PRK10083  81 VAVDPVISCGHCYPCSIGKPNVCTSLVVLGVHRDGGFSEYAVVPAKNAHRiPDAIADQYAVMVEPFTIAANVTGRTGPTE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 163 GEQVLVVGAGPIGLGAAAIAKA--DGAQVVVADtsparreHVATRLELP-------VLDPSAEDFDAQLRAQfgGSLAQK 233
Cdd:PRK10083 161 QDVALIYGAGPVGLTIVQVLKGvyNVKAVIVAD-------RIDERLALAkesgadwVINNAQEPLGEALEEK--GIKPTL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 234 VIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSR-NATpeDFAKVGRLMAEGKITADMMLTH 312
Cdd:PRK10083 232 IIDAACHPSILEEAVTLASPAARIVLMGFSSEPSEIVQQGITGKELSIFSSRlNAN--KFPVVIDWLSKGLIDPEKLITH 309
                        330       340
                 ....*....|....*....|....*...
gi 446028188 313 RYPFATLAETYERDVINNRELIKGVITF 340
Cdd:PRK10083 310 TFDFQHVADAIELFEKDQRHCCKVLLTF 337
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
22-340 1.74e-57

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: 189.45  E-value: 1.74e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  22 IPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVL-GHEICGEIVGLGKNIANLKNGQQVAVIPYVACQQCPACKS 100
Cdd:cd08239   19 VPVPGPGEVLLRVKASGLCGSDLHYYYHGHRAPAYQGVIpGHEPAGVVVAVGPGVTHFRVGDRVMVYHYVGCGACRNCRR 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 101 GRTNCCE-KISVIGVHQDGGFSEYLSVPVANILPADG--IDPQAAALIEPFAISAHAVRRAAIAPGEQVLVVGAGPIGLG 177
Cdd:cd08239   99 GWMQLCTsKRAAYGWNRDGGHAEYMLVPEKTLIPLPDdlSFADGALLLCGIGTAYHALRRVGVSGRDTVLVVGAGPVGLG 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 178 AAAIAKAD-GAQVVVADTSPARRE--------HVATRLELPVLDPSaedfdaQLRAQFGGSLAqkvIDATGNQHAMNNTV 248
Cdd:cd08239  179 ALMLARALgAEDVIGVDPSPERLElakalgadFVINSGQDDVQEIR------ELTSGAGADVA---IECSGNTAARRLAL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 249 NLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMMLTHRYPFATLAETYERdvI 328
Cdd:cd08239  250 EAVRPWGRLVLVGEGGELTIEVSNDLIRKQRTLIGSWYFSVPDMEECAEFLARHKLEVDRLVTHRFGLDQAPEAYAL--F 327
                        330
                 ....*....|..
gi 446028188 329 NNRELIKGVITF 340
Cdd:cd08239  328 AQGESGKVVFVF 339
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
4-325 2.57e-57

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: 189.06  E-value: 2.57e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQpKELVWKQREIPIPGDNEALIKIKSVGICGTDIHA---------WGGNQPFFSYPR--VLGHEICGEIVGLG 72
Cdd:cd08262    1 MRAAVFRD-GPLVVRDVPDPEPGPGQVLVKVLACGICGSDLHAtahpeamvdDAGGPSLMDLGAdiVLGHEFCGEVVDYG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  73 KNIAN-LKNGQQVAVIPYVACQQCPACKSGRTNccekisvigvHQDGGFSEYLSVPVANILPA-DGIDPQAAALIEPFAI 150
Cdd:cd08262   80 PGTERkLKVGTRVTSLPLLLCGQGASCGIGLSP----------EAPGGYAEYMLLSEALLLRVpDGLSMEDAALTEPLAV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 151 SAHAVRRAAIAPGEQVLVVGAGPIGLGAAAIAKAD-GAQVVVADTSPARReHVATRLELP-VLDPSAED---FDAQLRAQ 225
Cdd:cd08262  150 GLHAVRRARLTPGEVALVIGCGPIGLAVIAALKARgVGPIVASDFSPERR-ALALAMGADiVVDPAADSpfaAWAAELAR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 226 FGGSLAQKVIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKIT 305
Cdd:cd08262  229 AGGPKPAVIFECVGAPGLIQQIIEGAPPGGRIVVVGVCMESDNIEPALAIRKELTLQFSLGYTPEEFADALDALAEGKVD 308
                        330       340
                 ....*....|....*....|
gi 446028188 306 ADMMLTHRYPFATLAETYER 325
Cdd:cd08262  309 VAPMVTGTVGLDGVPDAFEA 328
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
1-304 1.39e-55

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: 184.74  E-value: 1.39e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   1 MSTMNVLICQQPKELVwkQREIPIPGDNEALIKIKSVGICGTDIHAW-------GGNQPFFS-----YPRVLGHEICGEI 68
Cdd:cd08240    1 MKAAAVVEPGKPLEEV--EIDTPKPPGTEVLVKVTACGVCHSDLHIWdggydlgGGKTMSLDdrgvkLPLVLGHEIVGEV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  69 VGLGKNIANLKNGQQVAVIPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANIL-PADGIDPQAAALIEP 147
Cdd:cd08240   79 VAVGPDAADVKVGDKVLVYPWIGCGECPVCLAGDENLCAKGRALGIFQDGGYAEYVIVPHSRYLvDPGGLDPALAATLAC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 148 FAISAH-AVRRAAIAPGEQ-VLVVGAGPIGL-GAAAIAKADGAQVVVADTSPARREHVATRLELPVLDPSAEDFDAQLRA 224
Cdd:cd08240  159 SGLTAYsAVKKLMPLVADEpVVIIGAGGLGLmALALLKALGPANIIVVDIDEAKLEAAKAAGADVVVNGSDPDAAKRIIK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 225 QFGGSLAQkVIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKI 304
Cdd:cd08240  239 AAGGGVDA-VIDFVNNSATASLAFDILAKGGKLVLVGLFGGEATLPLPLLPLRALTIQGSYVGSLEELRELVALAKAGKL 317
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
12-304 1.66e-55

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: 184.06  E-value: 1.66e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYVA 91
Cdd:cd08259   10 NKPLQIEEVPDPEPGPGEVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVGEGVERFKPGDRVILYYYIP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  92 CQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILPA-DGIDPQAAALIE-PFAISAHAVRRAAIAPGEQVLVV 169
Cdd:cd08259   90 CGKCEYCLSGEENLCRNRAEYGEEVDGGFAEYVKVPERSLVKLpDNVSDESAALAAcVVGTAVHALKRAGVKKGDTVLVT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 170 GA-GPIGLGAAAIAKADGAQVVVADTSPARREHVATRLELPVLDpsAEDFDAQLRAQFGgslAQKVIDATGNqHAMNNTV 248
Cdd:cd08259  170 GAgGGVGIHAIQLAKALGARVIAVTRSPEKLKILKELGADYVID--GSKFSEDVKKLGG---ADVVIELVGS-PTIEESL 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446028188 249 NLIRHGGTVVFVGLFKGELQFSDPEFH-KKETTMMGSRNATPEDFAKVGRLMAEGKI 304
Cdd:cd08259  244 RSLNKGGRLVLIGNVTPDPAPLRPGLLiLKEIRIIGSISATKADVEEALKLVKEGKI 300
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
12-340 1.79e-53

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: 179.01  E-value: 1.79e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKELVWKQREIP-IPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYV 90
Cdd:cd05278    9 PGKIGLEEVPDPkIQGPHDAIVRVTATSICGSDLHIYRGGVPGAKHGMILGHEFVGEVVEVGSDVKRLKPGDRVSVPCIT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  91 ACQQCPACKSGRTNCCEKISVI---GVHQDGGFSEYLSVPVA----NILPADGIDPQAAALIEPFAISAHAVRRAAIAPG 163
Cdd:cd05278   89 FCGRCRFCRRGYHAHCENGLWGwklGNRIDGGQAEYVRVPYAdmnlAKIPDGLPDEDALMLSDILPTGFHGAELAGIKPG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 164 EQVLVVGAGPIGL-GAAAIAKADGAQVVVADTSPARREHVATRLELPVLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQH 242
Cdd:cd05278  169 STVAVIGAGPVGLcAVAGARLLGAARIIAVDSNPERLDLAKEAGATDIINPKNGDIVEQILELTGGRGVDCVIEAVGFEE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 243 AMNNTVNLIRHGGTVVFVGLFKGELQFSDPE--FHKKETTMMGSRNATPeDFAKVGRLMAEGKITADMMLTHRYPFATLA 320
Cdd:cd05278  249 TFEQAVKVVRPGGTIANVGVYGKPDPLPLLGewFGKNLTFKTGLVPVRA-RMPELLDLIEEGKIDPSKLITHRFPLDDIL 327
                        330       340
                 ....*....|....*....|..
gi 446028188 321 ETYerDVINNRE--LIKGVITF 340
Cdd:cd05278  328 KAY--RLFDNKPdgCIKVVIRP 347
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
15-324 3.81e-50

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: 170.11  E-value: 3.81e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  15 LVWKQREIPIPGDNEALIKIKSVGICGTDIH-----AWGgnQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPY 89
Cdd:cd05281   13 AELVEVPVPKPGPGEVLIKVLAASICGTDVHiyewdEWA--QSRIKPPLIFGHEFAGEVVEVGEGVTRVKVGDYVSAETH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  90 VACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANI--LPADgIDPQAAALIEPFAISAHAVRRAAIApGEQVL 167
Cdd:cd05281   91 IVCGKCYQCRTGNYHVCQNTKILGVDTDGCFAEYVVVPEENLwkNDKD-IPPEIASIQEPLGNAVHTVLAGDVS-GKSVL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 168 VVGAGPIGL-GAAAIAKADGAQVVVADTSPARREHV----ATRlelpVLDPSAEDfDAQLRAQFGGSLAQKVIDATGNQH 242
Cdd:cd05281  169 ITGCGPIGLmAIAVAKAAGASLVIASDPNPYRLELAkkmgADV----VINPREED-VVEVKSVTDGTGVDVVLEMSGNPK 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 243 AMNNTVNLIRHGGTVVFVGLFKGELQF---SDPEFhkKETTMMG--SRNATpEDFAKVGRLMAEGKITADMMLTHRYPFA 317
Cdd:cd05281  244 AIEQGLKALTPGGRVSILGLPPGPVDIdlnNLVIF--KGLTVQGitGRKMF-ETWYQVSALLKSGKVDLSPVITHKLPLE 320

                 ....*..
gi 446028188 318 TLAETYE 324
Cdd:cd05281  321 DFEEAFE 327
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
17-325 9.94e-50

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: 169.04  E-value: 9.94e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  17 WKQREIPIP--GDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAViPYV--AC 92
Cdd:cd08245   12 LEPEEVPVPepGPGEVLIKIEACGVCHTDLHAAEGDWGGSKYPLVPGHEIVGEVVEVGAGVEGRKVGDRVGV-GWLvgSC 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  93 QQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILP-ADGIDPQAAALIEPFAISAH-AVRRAAIAPGEQVLVVG 170
Cdd:cd08245   91 GRCEYCRRGLENLCQKAVNTGYTTQGGYAEYMVADAEYTVLlPDGLPLAQAAPLLCAGITVYsALRDAGPRPGERVAVLG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 171 AGPIGLGAAAIAKADGAQVVVADTSPARREhVATRLELPVLDPSAEDFDAQlrAQFGGslAQKVIDATGNQHAMNNTVNL 250
Cdd:cd08245  171 IGGLGHLAVQYARAMGFETVAITRSPDKRE-LARKLGADEVVDSGAELDEQ--AAAGG--ADVILVTVVSGAAAEAALGG 245
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446028188 251 IRHGGTVVFVGLFKGELQFSDP-EFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADmmlTHRYPFATLAETYER 325
Cdd:cd08245  246 LRRGGRIVLVGLPESPPFSPDIfPLIMKRQSIAGSTHGGRADLQEALDFAAEGKVKPM---IETFPLDQANEAYER 318
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
4-324 1.24e-48

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


Pssm-ID: 176218 [Multi-domain]  Cd Length: 350  Bit Score: 166.81  E-value: 1.24e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHA-------WGG--NQPFFSYPRVLGHEICGEIVGLGKN 74
Cdd:cd08256    1 MRAVVCHGPQDYRLEEVPVPRPGPGEILVKVEACGICAGDIKCyhgapsfWGDenQPPYVKPPMIPGHEFVGRVVELGEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  75 IAN--LKNGQQVAVIPYVACQQCPACKSGRTNCCEKISVIGVHQD--GGFSEYLSVPVANI---LPaDGIDPQAAALIEP 147
Cdd:cd08256   81 AEErgVKVGDRVISEQIVPCWNCRFCNRGQYWMCQKHDLYGFQNNvnGGMAEYMRFPKEAIvhkVP-DDIPPEDAILIEP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 148 FAISAHAVRRAAIAPGEQVLVVGAGPIGLGAAAIAKADGAQ-VVVADTSPARREhVATRLELP-VLDPSAEDFDAQLRAQ 225
Cdd:cd08256  160 LACALHAVDRANIKFDDVVVLAGAGPLGLGMIGAARLKNPKkLIVLDLKDERLA-LARKFGADvVLNPPEVDVVEKIKEL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 226 FGGSLAQKVIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQ-----FSDpefhKKETTMMGSrNATPEDFAKVGRLMA 300
Cdd:cd08256  239 TGGYGCDIYIEATGHPSAVEQGLNMIRKLGRFVEFSVFGDPVTvdwsiIGD----RKELDVLGS-HLGPYCYPIAIDLIA 313
                        330       340
                 ....*....|....*....|....
gi 446028188 301 EGKITADMMLTHRYPFATLAETYE 324
Cdd:cd08256  314 SGRLPTDGIVTHQFPLEDFEEAFE 337
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
20-325 3.62e-47

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: 162.34  E-value: 3.62e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  20 REIPIP--GDNEALIKIKSVGICGTDIH----AWGGNQPFfSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYVACQ 93
Cdd:cd05284   16 EDVPVPepGPGQVLVRVGGAGVCHSDLHvidgVWGGILPY-KLPFTLGHENAGWVEEVGSGVDGLKEGDPVVVHPPWGCG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  94 QCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANIL-PADGIDPQAAAliePFA---ISA-HAVRRAA--IAPGEQV 166
Cdd:cd05284   95 TCRYCRRGEENYCENARFPGIGTDGGFAEYLLVPSRRLVkLPRGLDPVEAA---PLAdagLTAyHAVKKALpyLDPGSTV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 167 LVVGAGPIG-LGAAAIAKADGAQVVVADTSPARREHvATRLELPVLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQHAMN 245
Cdd:cd05284  172 VVIGVGGLGhIAVQILRALTPATVIAVDRSEEALKL-AERLGADHVLNASDDVVEEVRELTGGRGADAVIDFVGSDETLA 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 246 NTVNLIRHGGTVVFVGLFkGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITadmMLTHRYPFATLAETYER 325
Cdd:cd05284  251 LAAKLLAKGGRYVIVGYG-GHGRLPTSDLVPTEISVIGSLWGTRAELVEVVALAESGKVK---VEITKFPLEDANEALDR 326
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
4-340 8.79e-47

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: 161.66  E-value: 8.79e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIP-IPGDNEALIKIKSVGICGTDIHAWGGNQPFfSYPRVLGHEICGEIVGLGKNIANLKNGQ 82
Cdd:cd08284    1 MKAVVFKGPGDVRVEEVPIPqIQDPTDAIVKVTAAAICGSDLHIYRGHIPS-TPGFVLGHEFVGEVVEVGPEVRTLKVGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  83 QVAVIPYVACQQCPACKSGRTNCCEKISVIGVHQ----DGGFSEYLSVPVANI----LPADGIDPQAAALIEPFAISAHA 154
Cdd:cd08284   80 RVVSPFTIACGECFYCRRGQSGRCAKGGLFGYAGspnlDGAQAEYVRVPFADGtllkLPDGLSDEAALLLGDILPTGYFG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 155 VRRAAIAPGEQVLVVGAGPIGL-GAAAIAKADGAQVVVADTSPARREhVATRLELPVLDPSAEDFDAQLRAQFGGSLAQK 233
Cdd:cd08284  160 AKRAQVRPGDTVAVIGCGPVGLcAVLSAQVLGAARVFAVDPVPERLE-RAAALGAEPINFEDAEPVERVREATEGRGADV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 234 VIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGE-LQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMMLTH 312
Cdd:cd08284  239 VLEAVGGAAALDLAFDLVRPGGVISSVGVHTAEeFPFPGLDAYNKNLTLRFGRCPVRSLFPELLPLLESGRLDLEFLIDH 318
                        330       340
                 ....*....|....*....|....*...
gi 446028188 313 RYPFATLAETYERdvINNRELIKGVITF 340
Cdd:cd08284  319 RMPLEEAPEAYRL--FDKRKVLKVVLDP 344
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
4-269 2.19e-46

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 160.38  E-value: 2.19e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVW-KQREIPIPGDNEALIKIKSVGICGTDIHAWGGN---QPFFSYPRVLGHEICGEIVGLGKNIANLK 79
Cdd:PRK05396   1 MKALVKLKAEPGLWlTDVPVPEPGPNDVLIKVKKTAICGTDVHIYNWDewaQKTIPVPMVVGHEFVGEVVEVGSEVTGFK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  80 NGQQVAVIPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILP-ADGIDPQAAALIEPFAISAHAVRRA 158
Cdd:PRK05396  81 VGDRVSGEGHIVCGHCRNCRAGRRHLCRNTKGVGVNRPGAFAEYLVIPAFNVWKiPDDIPDDLAAIFDPFGNAVHTALSF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 159 AIApGEQVLVVGAGPIGL-GAAAIAKADGAQVVVADTSPARREHV----ATRlelpVLDPSAEDFDAQLRAQFGGSLAQK 233
Cdd:PRK05396 161 DLV-GEDVLITGAGPIGImAAAVAKHVGARHVVITDVNEYRLELArkmgATR----AVNVAKEDLRDVMAELGMTEGFDV 235
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446028188 234 VIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQF 269
Cdd:PRK05396 236 GLEMSGAPSAFRQMLDNMNHGGRIAMLGIPPGDMAI 271
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
10-313 4.82e-46

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: 159.69  E-value: 4.82e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  10 QQPKELvwKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAViPY 89
Cdd:cd08260   10 GEPLEI--REVPDPEPPPDGVVVEVEACGVCRSDWHGWQGHDPDVTLPHVPGHEFAGVVVEVGEDVSRWRVGDRVTV-PF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  90 V-ACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANI----LPaDGIDPQAAALIE-PFAISAHA-VRRAAIAP 162
Cdd:cd08260   87 VlGCGTCPYCRAGDSNVCEHQVQPGFTHPGSFAEYVAVPRADVnlvrLP-DDVDFVTAAGLGcRFATAFRAlVHQARVKP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 163 GEQVLVVGAGPIGLGAAAIAKADGAQVVVADTSPARREH------VATrlelpvLDPSA-EDFDAQLRAQFGGSlAQKVI 235
Cdd:cd08260  166 GEWVAVHGCGGVGLSAVMIASALGARVIAVDIDDDKLELarelgaVAT------VNASEvEDVAAAVRDLTGGG-AHVSV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 236 DATGNQHAMNNTVNLIRHGGTVVFVGLF-KGELQFSDP--EFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMMLTH 312
Cdd:cd08260  239 DALGIPETCRNSVASLRKRGRHVQVGLTlGEEAGVALPmdRVVARELEIVGSHGMPAHRYDAMLALIASGKLDPEPLVGR 318

                 .
gi 446028188 313 R 313
Cdd:cd08260  319 T 319
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
4-325 6.94e-46

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family, including threonine dehydrogenase. 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: 176204 [Multi-domain]  Cd Length: 319  Bit Score: 158.56  E-value: 6.94e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFfsyPRVLGHEICGEIVGLGKniANLKnGQQ 83
Cdd:cd08242    1 MKALVLDGGLDLRVEDLPKPEPPPGEALVRVLLAGICNTDLEIYKGYYPF---PGVPGHEFVGIVEEGPE--AELV-GKR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  84 VAVIPYVACQQCPACKSGRTNCCEKISVIGVH-QDGGFSEYLSVPVANILP-ADGIDPQAAALIEPFAISAHAVRRAAIA 161
Cdd:cd08242   75 VVGEINIACGRCEYCRRGLYTHCPNRTVLGIVdRDGAFAEYLTLPLENLHVvPDLVPDEQAVFAEPLAAALEILEQVPIT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 162 PGEQVLVVGAGPIGLGAAAIAKADGAQVVVAdTSPARREHVATRLELPVLDPSaedfdaqlRAQFGGSLAQKVIDATGNQ 241
Cdd:cd08242  155 PGDKVAVLGDGKLGLLIAQVLALTGPDVVLV-GRHSEKLALARRLGVETVLPD--------EAESEGGGFDVVVEATGSP 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 242 HAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNAtpeDFAKVGRLMAEGKITADMMLTHRYPFATLAE 321
Cdd:cd08242  226 SGLELALRLVRPRGTVVLKSTYAGPASFDLTKAVVNEITLVGSRCG---PFAPALRLLRKGLVDVDPLITAVYPLEEALE 302

                 ....
gi 446028188 322 TYER 325
Cdd:cd08242  303 AFER 306
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
4-325 1.67e-44

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: 155.38  E-value: 1.67e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIPI--PGDNEALIKIKSVGICGTDIHAWGGNQPFFS-YPRVLGHEICGEIVGLGKNIANLKN 80
Cdd:cd08297    1 MKAAVVEEFGEKPYEVKDVPVpePGPGEVLVKLEASGVCHTDLHAALGDWPVKPkLPLIGGHEGAGVVVAVGPGVSGLKV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  81 GQQVAVIP-YVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPV--ANILPaDGIDPQAAALIEPFAISAH-AVR 156
Cdd:cd08297   81 GDRVGVKWlYDACGKCEYCRTGDETLCPNQKNSGYTVDGTFAEYAIADAryVTPIP-DGLSFEQAAPLLCAGVTVYkALK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 157 RAAIAPGEQVLVVGAGPiGLGAAAI--AKADGAQVVVADTSPARREHVatrLELP---VLDPSAEDFDAQLRAQFGGSLA 231
Cdd:cd08297  160 KAGLKPGDWVVISGAGG-GLGHLGVqyAKAMGLRVIAIDVGDEKLELA---KELGadaFVDFKKSDDVEAVKELTGGGGA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 232 QKVIDATGNQHAMNNTVNLIRHGGTVVFVGL-FKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMml 310
Cdd:cd08297  236 HAVVVTAVSAAAYEQALDYLRPGGTLVCVGLpPGGFIPLDPFDLVLRGITIVGSLVGTRQDLQEALEFAARGKVKPHI-- 313
                        330
                 ....*....|....*
gi 446028188 311 tHRYPFATLAETYER 325
Cdd:cd08297  314 -QVVPLEDLNEVFEK 327
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
13-339 1.94e-44

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: 155.88  E-value: 1.94e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  13 KELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAV------ 86
Cdd:cd08231   11 KPLEIREVPLPDLEPGAVLVRVRLAGVCGSDVHTVAGRRPRVPLPIILGHEGVGRVVALGGGVTTDVAGEPLKVgdrvtw 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  87 IPYVACQQCPACKSGRTNCCEKISVIGV-------HQDGGFSEYLSVPV-ANILPADGIDPQ--AAALIEPFAISAHAVR 156
Cdd:cd08231   91 SVGAPCGRCYRCLVGDPTKCENRKKYGHeascddpHLSGGYAEHIYLPPgTAIVRVPDNVPDevAAPANCALATVLAALD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 157 RAAIAP-GEQVLVVGAGPIGL-GAAAIAKADGAQVVVADTSPARREhVATRLEL-PVLDP---SAEDFDAQLRAQFGGSL 230
Cdd:cd08231  171 RAGPVGaGDTVVVQGAGPLGLyAVAAAKLAGARRVIVIDGSPERLE-LAREFGAdATIDIdelPDPQRRAIVRDITGGRG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 231 AQKVIDATGNQHAMNNTVNLIRHGGTVVFVGLF--KGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAE--GKITA 306
Cdd:cd08231  250 ADVVIEASGHPAAVPEGLELLRRGGTYVLVGSVapAGTVPLDPERIVRKNLTIIGVHNYDPSHLYRAVRFLERtqDRFPF 329
                        330       340       350
                 ....*....|....*....|....*....|...
gi 446028188 307 DMMLTHRYPFATLAETYERdvINNRELIKGVIT 339
Cdd:cd08231  330 AELVTHRYPLEDINEALEL--AESGTALKVVID 360
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
14-325 2.18e-43

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenase and has the catalytic and structural zinc-binding sites characteristic of this group. 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. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176226 [Multi-domain]  Cd Length: 384  Bit Score: 153.82  E-value: 2.18e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  14 ELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFF-------SYPRVLGHEICGEIVGLGKNIANLKNGQQVAV 86
Cdd:cd08265   38 ELRVEDVPVPNLKPDEILIRVKACGICGSDIHLYETDKDGYilypgltEFPVVIGHEFSGVVEKTGKNVKNFEKGDPVTA 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  87 IPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVP------VANILPADGIDP--QAAALIEPFAISAHAV--R 156
Cdd:cd08265  118 EEMMWCGMCRACRSGSPNHCKNLKELGFSADGAFAEYIAVNaryaweINELREIYSEDKafEAGALVEPTSVAYNGLfiR 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 157 RAAIAPGEQVLVVGAGPIGLGAAAIAKAD-GAQVVVADTSPARREhVATRLELP-VLDPSAEDFDAQLRAQF---GGSLA 231
Cdd:cd08265  198 GGGFRPGAYVVVYGAGPIGLAAIALAKAAgASKVIAFEISEERRN-LAKEMGADyVFNPTKMRDCLSGEKVMevtKGWGA 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 232 QKVIDATGN-QHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPE-DFAKVGRLMAEGKITADMM 309
Cdd:cd08265  277 DIQVEAAGApPATIPQMEKSIAINGKIVYIGRAATTVPLHLEVLQVRRAQIVGAQGHSGHgIFPSVIKLMASGKIDMTKI 356
                        330
                 ....*....|....*.
gi 446028188 310 LTHRYPFATLAETYER 325
Cdd:cd08265  357 ITARFPLEGIMEAIKA 372
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
21-339 2.83e-43

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: 152.70  E-value: 2.83e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  21 EIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFfSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYVACQQCPACKS 100
Cdd:cd08279   19 ELDDPGPGEVLVRIAAAGLCHSDLHVVTGDLPA-PLPAVLGHEGAGVVEEVGPGVTGVKPGDHVVLSWIPACGTCRYCSR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 101 GRTNCCEKISVIGV----------HQDGG----------FSEYLSVPVANILP-ADGIDPQAAALIE---PFAISAhAVR 156
Cdd:cd08279   98 GQPNLCDLGAGILGgqlpdgtrrfTADGEpvgamcglgtFAEYTVVPEASVVKiDDDIPLDRAALLGcgvTTGVGA-VVN 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 157 RAAIAPGEQVLVVGAGPIGLGAAAIAKADGAQVVVA-DTSPARREhVATRL-ELPVLDPSAEDFDAQLRAQFGGSLAQKV 234
Cdd:cd08279  177 TARVRPGDTVAVIGCGGVGLNAIQGARIAGASRIIAvDPVPEKLE-LARRFgATHTVNASEDDAVEAVRDLTDGRGADYA 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 235 IDATGNQHAMNNTVNLIRHGGTVVFVGLFKGE--LQFSDPEFHKKETTMMGSR--NATPE-DFAKVGRLMAEGKITADMM 309
Cdd:cd08279  256 FEAVGRAATIRQALAMTRKGGTAVVVGMGPPGetVSLPALELFLSEKRLQGSLygSANPRrDIPRLLDLYRAGRLKLDEL 335
                        330       340       350
                 ....*....|....*....|....*....|
gi 446028188 310 LTHRYPFATLAETYERdvINNRELIKGVIT 339
Cdd:cd08279  336 VTRRYSLDEINEAFAD--MLAGENARGVIV 363
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
12-325 1.48e-42

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: 150.48  E-value: 1.48e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGnQPF--FSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPY 89
Cdd:cd08266   12 PEVLEYGDLPEPEPGPDEVLVRVKAAALNHLDLWVRRG-MPGikLPLPHILGSDGAGVVEAVGPGVTNVKPGQRVVIYPG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  90 VACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILPA-DGID-PQAAALIEPFAISAHA-VRRAAIAPGEQV 166
Cdd:cd08266   91 ISCGRCEYCLAGRENLCAQYGILGEHVDGGYAEYVAVPARNLLPIpDNLSfEEAAAAPLTFLTAWHMlVTRARLRPGETV 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 167 LVVGAGPiGLGAAAIAKADGAQVVVADTspARREHVATRL-EL---PVLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQH 242
Cdd:cd08266  171 LVHGAGS-GVGSAAIQIAKLFGATVIAT--AGSEDKLERAkELgadYVIDYRKEDFVREVRELTGKRGVDVVVEHVGAAT 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 243 aMNNTVNLIRHGGTVVFVGLFKG-ELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITAdmMLTHRYPFATLAE 321
Cdd:cd08266  248 -WEKSLKSLARGGRLVTCGATTGyEAPIDLRHVFWRQLSILGSTMGTKAELDEALRLVFRGKLKP--VIDSVFPLEEAAE 324

                 ....
gi 446028188 322 TYER 325
Cdd:cd08266  325 AHRR 328
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
28-133 1.49e-42

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: 143.13  E-value: 1.49e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   28 NEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYVACQQCPACKSGRTNCCE 107
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYNLCP 80
                          90       100
                  ....*....|....*....|....*.
gi 446028188  108 KISVIGVHQDGGFSEYLSVPVANILP 133
Cdd:pfam08240  81 NGRFLGYDRDGGFAEYVVVPERNLVP 106
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
12-339 1.09e-40

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: 144.81  E-value: 1.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSY---PRVLGHEICGEIVGLGKNIANLKNGQQVAVIP 88
Cdd:cd08269    4 PGRFEVEEHPRPTPGPGQVLVRVEGCGVCGSDLPAFNQGRPWFVYpaePGGPGHEGWGRVVALGPGVRGLAVGDRVAGLS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  89 YvacqqcpacksgrtnccekisvigvhqdGGFSEYLSVPVANI--LPADgIDPQAAALiEPFAISAHAVRRAAIAPGEQV 166
Cdd:cd08269   84 G----------------------------GAFAEYDLADADHAvpLPSL-LDGQAFPG-EPLGCALNVFRRGWIRAGKTV 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 167 LVVGAGPIG-LGAAAIAKADGAQVVVADTSPARREhVATRL--ELPVLDPSAEDFDAqLRAQFGGSLAQKVIDATGNQHA 243
Cdd:cd08269  134 AVIGAGFIGlLFLQLAAAAGARRVIAIDRRPARLA-LARELgaTEVVTDDSEAIVER-VRELTGGAGADVVIEAVGHQWP 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 244 MNNTVNLIRHGGTVVFVGLFKGEL-QFSDPEFHKKETTMMGSRNATP----EDFAKVGRLMAEGKITADMMLTHRYPFAT 318
Cdd:cd08269  212 LDLAGELVAERGRLVIFGYHQDGPrPVPFQTWNWKGIDLINAVERDPriglEGMREAVKLIADGRLDLGSLLTHEFPLEE 291
                        330       340
                 ....*....|....*....|.
gi 446028188 319 LAETYERDVINNRELIKGVIT 339
Cdd:cd08269  292 LGDAFEAARRRPDGFIKGVIV 312
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
21-339 1.16e-40

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 145.61  E-value: 1.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  21 EIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFfSYPRVLGHEICGEIVGLGKNIANLKNGQQVaVIPYV-ACQQCPACK 99
Cdd:COG1062   10 ELDEPRPGEVLVRIVAAGLCHSDLHVRDGDLPV-PLPAVLGHEGAGVVEEVGPGVTGVAPGDHV-VLSFIpSCGHCRYCA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 100 SGRTNCCEKISVI---GVHQDG-------------------GFSEYLSVPVANILP-ADGIDPQAAALIE---PFAISAh 153
Cdd:COG1062   88 SGRPALCEAGAALngkGTLPDGtsrlssadgepvghffgqsSFAEYAVVPERSVVKvDKDVPLELAALLGcgvQTGAGA- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 154 AVRRAAIAPGEQVLVVGAGPIGL---------GaaaiakadGAQVVVADTSPARREhVAtrLEL---PVLDPSAEDFDAQ 221
Cdd:COG1062  167 VLNTAKVRPGDTVAVFGLGGVGLsavqgariaG--------ASRIIAVDPVPEKLE-LA--RELgatHTVNPADEDAVEA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 222 LRAQFGGsLAQKVIDATGNQHAMNNTVNLIRHGGTVVFVGLFKG--ELQFSDPEFHKKETTMMGSR--NATP-EDFAKVG 296
Cdd:COG1062  236 VRELTGG-GVDYAFETTGNPAVIRQALEALRKGGTVVVVGLAPPgaEISLDPFQLLLTGRTIRGSYfgGAVPrRDIPRLV 314
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 446028188 297 RLMAEGKITADMMLTHRYPFATLAETYERdvINNRELIKGVIT 339
Cdd:COG1062  315 DLYRAGRLPLDELITRRYPLDEINEAFDD--LRSGEVIRPVIV 355
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
12-321 7.47e-39

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 140.59  E-value: 7.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKELVWKQREIpIPGDNEALIKIKSVGICGTDIHAW----GGNQpFFSYPRVLGHEICGEIVGlgKNIANLKNGQQVAVI 87
Cdd:PRK09880  13 KKDVAVTEQEI-EWNNNGTLVQITRGGICGSDLHYYqegkVGNF-VIKAPMVLGHEVIGKIVH--SDSSGLKEGQTVAIN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  88 PYVACQQCPACKSGRTNCCEKISVIGV-----HQDGGFSEYLSVPVANILPAD-GIDPQAAALIEPFAISAHAVRRAAIA 161
Cdd:PRK09880  89 PSKPCGHCKYCLSHNENQCTTMRFFGSamyfpHVDGGFTRYKVVDTAQCIPYPeKADEKVMAFAEPLAVAIHAAHQAGDL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 162 PGEQVLVVGAGPIG-LGAAAIAKADGAQVVVADTSPARREHVATRLELPVLDPSAEDFDA--QLRAQFGGSLaqkviDAT 238
Cdd:PRK09880 169 QGKRVFVSGVGPIGcLIVAAVKTLGAAEIVCADVSPRSLSLAREMGADKLVNPQNDDLDHykAEKGYFDVSF-----EVS 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 239 GNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATpEDFAKVGRLMAEGKITADMMLTHRYPFAT 318
Cdd:PRK09880 244 GHPSSINTCLEVTRAKGVMVQVGMGGAPPEFPMMTLIVKEISLKGSFRFT-EEFNTAVSWLANGVINPLPLLSAEYPFTD 322

                 ...
gi 446028188 319 LAE 321
Cdd:PRK09880 323 LEE 325
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
4-305 1.07e-38

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 140.17  E-value: 1.07e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKE-LVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQ 82
Cdd:PRK13771   1 MKAVILPGFKQgYRIEEVPDPKPGKDEVVIKVNYAGLCYRDLLQLQGFYPRMKYPVILGHEVVGTVEEVGENVKGFKPGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  83 QVAVIPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILPADGIDPQAAALIEPFAISA--HAVRRAAI 160
Cdd:PRK13771  81 RVASLLYAPDGTCEYCRSGEEAYCKNRLGYGEELDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVTGMvyRGLRRAGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 161 APGEQVLVVGA-GPIGLGAAAIAKADGAQVVVADTSPARREHVAtRLELPVLDPSAEDFDAQlraQFGGslAQKVIDATG 239
Cdd:PRK13771 161 KKGETVLVTGAgGGVGIHAIQVAKALGAKVIAVTSSESKAKIVS-KYADYVIVGSKFSEEVK---KIGG--ADIVIETVG 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446028188 240 NqHAMNNTVNLIRHGGTVVFVGLFKGELQFSDP--EFHKKETTMMGSRNATPEDFAKVGRLMAEGKIT 305
Cdd:PRK13771 235 T-PTLEESLRSLNMGGKIIQIGNVDPSPTYSLRlgYIILKDIEIIGHISATKRDVEEALKLVAEGKIK 301
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
13-325 1.45e-37

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: 137.89  E-value: 1.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  13 KELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSyPRVLGHEICGEIVGLGKNIAN---LKNGQQVAVIPY 89
Cdd:cd08263   11 PPLTIEEIPVPRPKEGEILIRVAACGVCHSDLHVLKGELPFPP-PFVLGHEISGEVVEVGPNVENpygLSVGDRVVGSFI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  90 VACQQCPACKSGRTNCCEKI----------------------SVIGVHQDGGFSEYLSVPVANILP-ADGIDPQAAALIE 146
Cdd:cd08263   90 MPCGKCRYCARGKENLCEDFfaynrlkgtlydgttrlfrldgGPVYMYSMGGLAEYAVVPATALAPlPESLDYTESAVLG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 147 PFAISAH-AVRRAAIA-PGEQVLVVGAGPIGLGAAAIAKADGAQVVVA-DTSPARREHVATRLELPVLDPSAEDFDAQLR 223
Cdd:cd08263  170 CAGFTAYgALKHAADVrPGETVAVIGVGGVGSSAIQLAKAFGASPIIAvDVRDEKLAKAKELGATHTVNAAKEDAVAAIR 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 224 AQFGGSLAQKVIDATGNQHAMNNTVNLIRHGGTVVFVGL--FKGELQFSDPEFHKKETTMMGSRNATPE-DFAKVGRLMA 300
Cdd:cd08263  250 EITGGRGVDVVVEALGKPETFKLALDVVRDGGRAVVVGLapGGATAEIPITRLVRRGIKIIGSYGARPRqDLPELVGLAA 329
                        330       340
                 ....*....|....*....|....*
gi 446028188 301 EGKITADMMLTHRYPFATLAETYER 325
Cdd:cd08263  330 SGKLDPEALVTHKYKLEEINEAYEN 354
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
12-339 1.07e-36

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: 134.68  E-value: 1.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKELVwkQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAViPYVA 91
Cdd:cd08296   12 PLELV--ERDVPLPGPGEVLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVGEGVSRWKVGDRVGV-GWHG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  92 --CQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVP---VANIlPaDGIDPQAAALIEPFAISA-HAVRRAAIAPGEQ 165
Cdd:cd08296   89 ghCGTCDACRRGDFVHCENGKVTGVTRDGGYAEYMLAPaeaLARI-P-DDLDAAEAAPLLCAGVTTfNALRNSGAKPGDL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 166 VLVVGAGpiGLGaaaiakADGAQ-------VVVADTSPARREHVATRLELPV-LDPSAEDFDAQLRAqFGGSlaqKVIDA 237
Cdd:cd08296  167 VAVQGIG--GLG------HLAVQyaakmgfRTVAISRGSDKADLARKLGAHHyIDTSKEDVAEALQE-LGGA---KLILA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 238 T-GNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPED------FAKVG--RLMAEgkitadm 308
Cdd:cd08296  235 TaPNAKAISALVGGLAPRGKLLILGAAGEPVAVSPLQLIMGRKSIHGWPSGTALDsedtlkFSALHgvRPMVE------- 307
                        330       340       350
                 ....*....|....*....|....*....|.
gi 446028188 309 mlthRYPFATLAETYERdVINNRELIKGVIT 339
Cdd:cd08296  308 ----TFPLEKANEAYDR-MMSGKARFRVVLT 333
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
4-340 5.44e-36

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: 133.14  E-value: 5.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQ 83
Cdd:cd08285    1 MKAFAMLGIGKVGWIEKPIPVCGPNDAIVRPTAVAPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGSEVKDFKPGDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  84 VAVIPYVACQQCPACKSGRTNCCE------KISVIgvhQDGGFSEYLSVPVAN----ILPaDGIDPQAAALIEPFAISA- 152
Cdd:cd08285   81 VIVPAITPDWRSVAAQRGYPSQSGgmlggwKFSNF---KDGVFAEYFHVNDADanlaPLP-DGLTDEQAVMLPDMMSTGf 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 153 HAVRRAAIAPGEQVLVVGAGPIGL-GAAAIAKADGAQVVVADTSPARREhVATRLELP-VLDPSAEDFDAQLRAQFGGSL 230
Cdd:cd08285  157 HGAELANIKLGDTVAVFGIGPVGLmAVAGARLRGAGRIIAVGSRPNRVE-LAKEYGATdIVDYKNGDVVEQILKLTGGKG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 231 AQKVIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDP--EF-----HKKETT--MMGSRnatpEDFAKVGRLMAE 301
Cdd:cd08285  236 VDAVIIAGGGQDTFEQALKVLKPGGTISNVNYYGEDDYLPIPreEWgvgmgHKTINGglCPGGR----LRMERLASLIEY 311
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 446028188 302 GKI-TADMMLTHRYPFATLAETYerDVINNRE--LIKGVITF 340
Cdd:cd08285  312 GRVdPSKLLTHHFFGFDDIEEAL--MLMKDKPddLIKPVIIF 351
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
12-325 3.33e-35

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


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 130.27  E-value: 3.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPF-FSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPyv 90
Cdd:COG0604   12 PEVLELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPLpPGLPFIPGSDAAGVVVAVGEGVTGFKVGDRVAGLG-- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  91 acqqcpacksgrtnccekisvigvhQDGGFSEYLSVPVANILPA-DGIDP-QAAALIEPFAISAHA-VRRAAIAPGEQVL 167
Cdd:COG0604   90 -------------------------RGGGYAEYVVVPADQLVPLpDGLSFeEAAALPLAGLTAWQAlFDRGRLKPGETVL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 168 VVGA-GPIG---------LGaaaiakadgAQVVVADTSPARREHVatrLEL---PVLDPSAEDFDAQLRAQFGGSLAQKV 234
Cdd:COG0604  145 VHGAaGGVGsaavqlakaLG---------ARVIATASSPEKAELL---RALgadHVIDYREEDFAERVRALTGGRGVDVV 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 235 IDATGNQHAMNNtVNLIRHGGTVVFVGLFKGE-LQFSDPEFHKKETTMMGS------RNATPEDFAKVGRLMAEGKITAD 307
Cdd:COG0604  213 LDTVGGDTLARS-LRALAPGGRLVSIGAASGApPPLDLAPLLLKGLTLTGFtlfardPAERRAALAELARLLAAGKLRPV 291
                        330
                 ....*....|....*...
gi 446028188 308 MmlTHRYPFATLAETYER 325
Cdd:COG0604  292 I--DRVFPLEEAAEAHRL 307
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
21-321 6.00e-34

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 127.64  E-value: 6.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  21 EIPIP---GDNEALIKIKSVGICGTDIHAWGGNQPFFsYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYVACQQCPA 97
Cdd:PRK10309  16 ESPIPeikHQDDVLVKVASSGLCGSDIPRIFKNGAHY-YPITLGHEFSGYVEAVGSGVDDLHPGDAVACVPLLPCFTCPE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  98 CKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANI--LPADgIDPQAAALIEPFAISAHAVRRAAIAPGEQVLVVGAGPIG 175
Cdd:PRK10309  95 CLRGFYSLCAKYDFIGSRRDGGNAEYIVVKRKNLfaLPTD-MPIEDGAFIEPITVGLHAFHLAQGCEGKNVIIIGAGTIG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 176 -LGAAAIAKADGAQVVVADTSPARRE--------HVATRLELpvldpSAEDFDAQLRAQfggSLAQKVIDATGNQHAMNN 246
Cdd:PRK10309 174 lLAIQCAVALGAKSVTAIDINSEKLAlakslgamQTFNSREM-----SAPQIQSVLREL---RFDQLILETAGVPQTVEL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 247 TVNLIRHGGTVVFVGLFKGELQFSDPEFHK---KETTMMGS--RNATP---EDFAKVGRLMAEGKITADMMLTHRYPFAT 318
Cdd:PRK10309 246 AIEIAGPRAQLALVGTLHHDLHLTSATFGKilrKELTVIGSwmNYSSPwpgQEWETASRLLTERKLSLEPLIAHRGSFES 325

                 ...
gi 446028188 319 LAE 321
Cdd:PRK10309 326 FAQ 328
PLN02702 PLN02702
L-idonate 5-dehydrogenase
22-317 7.42e-34

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 127.97  E-value: 7.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  22 IPIPGDNEALIKIKSVGICGTDIHAWGGNQP---FFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYVACQQCPAC 98
Cdd:PLN02702  36 LPPLGPHDVRVRMKAVGICGSDVHYLKTMRCadfVVKEPMVIGHECAGIIEEVGSEVKHLVVGDRVALEPGISCWRCNLC 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  99 KSGRTNCCEKISVIG---VHqdGGFSEYLSVPvANI---LPaDGIDPQAAALIEPFAISAHAVRRAAIAPGEQVLVVGAG 172
Cdd:PLN02702 116 KEGRYNLCPEMKFFAtppVH--GSLANQVVHP-ADLcfkLP-ENVSLEEGAMCEPLSVGVHACRRANIGPETNVLVMGAG 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 173 PIGL-GAAAIAKADGAQVVVADTSPaRREHVATRL---ELPVLDPSAEDFDAQLRA--QFGGSLAQKVIDATGNQHAMNN 246
Cdd:PLN02702 192 PIGLvTMLAARAFGAPRIVIVDVDD-ERLSVAKQLgadEIVLVSTNIEDVESEVEEiqKAMGGGIDVSFDCVGFNKTMST 270
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446028188 247 TVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMG---SRNATPEDFakvgRLMAEGKITADMMLTHRYPFA 317
Cdd:PLN02702 271 ALEATRAGGKVCLVGMGHNEMTVPLTPAAAREVDVVGvfrYRNTWPLCL----EFLRSGKIDVKPLITHRFGFS 340
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
13-324 2.41e-32

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: 124.19  E-value: 2.41e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  13 KELVW------KQREIPIPG---DNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQ 83
Cdd:cd08283    2 KALVWhgkgdvRVEEVPDPKiedPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGPEVRNLKVGDR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  84 VAVIPYVACQQCPACKSGRTNCCEKI------------SVIGV----HQDGGFS----EYLSVPVANI----LPADGIDP 139
Cdd:cd08283   82 VVVPFTIACGECFYCKRGLYSQCDNTnpsaemaklyghAGAGIfgysHLTGGYAggqaEYVRVPFADVgpfkIPDDLSDE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 140 QAAALIEPFAISAHAVRRAAIAPGEQVLVVGAGPIGL-GAAAIAKADGAQVVVADTSPARREHVATRLELPVLDPSAEDF 218
Cdd:cd08283  162 KALFLSDILPTGYHAAELAEVKPGDTVAVWGCGPVGLfAARSAKLLGAERVIAIDRVPERLEMARSHLGAETINFEEVDD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 219 DAQ-LRAQFGGSLAQKVIDA---------------------TGNQHAMNNTVNLIRHGGTVVFVGLFKGelqFSDP---- 272
Cdd:cd08283  242 VVEaLRELTGGRGPDVCIDAvgmeahgsplhkaeqallkleTDRPDALREAIQAVRKGGTVSIIGVYGG---TVNKfpig 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446028188 273 EFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMMLTHRYPFATLAETYE 324
Cdd:cd08283  319 AAMNKGLTLRMGQTHVQRYLPRLLELIESGELDPSFIITHRLPLEDAPEAYK 370
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
13-325 1.73e-31

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: 120.68  E-value: 1.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  13 KELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYV-A 91
Cdd:cd05283   10 GKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDRVGVGCQVdS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  92 CQQCPACKSGRTNCCEKISV--IGVHQD-----GGFSEYLSVP---VANIlPaDGIDPQAAAliePF---AISAHA-VRR 157
Cdd:cd05283   90 CGTCEQCKSGEEQYCPKGVVtyNGKYPDgtitqGGYADHIVVDerfVFKI-P-EGLDSAAAA---PLlcaGITVYSpLKR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 158 AAIAPGEQVLVVGAGPIG---------LGaaaiakadgAQVVVADTSPARRE---------HVATRlELPVLDPSAEDFD 219
Cdd:cd05283  165 NGVGPGKRVGVVGIGGLGhlavkfakaLG---------AEVTAFSRSPSKKEdalklgadeFIATK-DPEAMKKAAGSLD 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 220 AqlraqfggslaqkVIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETT----MMGSRNATPE--DFA 293
Cdd:cd05283  235 L-------------IIDTVSASHDLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGRKSvagsLIGGRKETQEmlDFA 301
                        330       340       350
                 ....*....|....*....|....*....|..
gi 446028188 294 kvgrlmAEGKITADMMLthrYPFATLAETYER 325
Cdd:cd05283  302 ------AEHGIKPWVEV---IPMDGINEALER 324
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
15-317 3.00e-31

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: 119.98  E-value: 3.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  15 LVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIP-YVACQ 93
Cdd:cd08298   17 LRLTEVPVPEPGPGEVLIKVEACGVCRTDLHIVEGDLPPPKLPLIPGHEIVGRVEAVGPGVTRFSVGDRVGVPWlGSTCG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  94 QCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVP--VANILPADGIDPQAAALIEPFAISAHAVRRAAIAPGEQVLVVGA 171
Cdd:cd08298   97 ECRYCRSGRENLCDNARFTGYTVDGGYAEYMVADerFAYPIPEDYDDEEAAPLLCAGIIGYRALKLAGLKPGQRLGLYGF 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 172 GPIGlgaaaiakADGAQVVVADtspARREHVATRlelpvlDPSAEDFDAQLRAQFGGSLAQK-------VIDATGNQHAM 244
Cdd:cd08298  177 GASA--------HLALQIARYQ---GAEVFAFTR------SGEHQELARELGADWAGDSDDLppepldaAIIFAPVGALV 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446028188 245 NNTVNLIRHGGTVVFVGLFKGELqfsdPEFHKK----ETTMMGSRNATPEDFAKVGRLMAEGKITADmmlTHRYPFA 317
Cdd:cd08298  240 PAALRAVKKGGRVVLAGIHMSDI----PAFDYEllwgEKTIRSVANLTRQDGEEFLKLAAEIPIKPE---VETYPLE 309
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
4-324 6.55e-31

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: 119.28  E-value: 6.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKELVWKQREIPI---PGDneALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKN 80
Cdd:cd08286    1 MKALVYHGPGKISWEDRPKPTiqePTD--AIVKMLKTTICGTDLHILKGDVPTVTPGRILGHEGVGVVEEVGSAVTNFKV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  81 GQQVAVIPYVACQQCPACKSGRTNCCEKISVI-GVHQDGGFSEYLSVPVANI----LPaDGIDPQAAALIEPFAISAH-- 153
Cdd:cd08286   79 GDRVLISCISSCGTCGYCRKGLYSHCESGGWIlGNLIDGTQAEYVRIPHADNslykLP-EGVDEEAAVMLSDILPTGYec 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 154 AVRRAAIAPGEQVLVVGAGPIGLGAAAIAKA-DGAQVVVADTSPARREH----VATRlelpVLDPSAEDFDAQLRAQFGG 228
Cdd:cd08286  158 GVLNGKVKPGDTVAIVGAGPVGLAALLTAQLySPSKIIMVDLDDNRLEVakklGATH----TVNSAKGDAIEQVLELTDG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 229 SLAQKVIDATGNQHAMNNTVNLIRHGGTVVFVGLFkGELQfsdpEFHKKE--------TTMMGSRNATPEdfakVGRLMA 300
Cdd:cd08286  234 RGVDVVIEAVGIPATFELCQELVAPGGHIANVGVH-GKPV----DLHLEKlwiknitiTTGLVDTNTTPM----LLKLVS 304
                        330       340
                 ....*....|....*....|....
gi 446028188 301 EGKITADMMLTHRYPFATLAETYE 324
Cdd:cd08286  305 SGKLDPSKLVTHRFKLSEIEKAYD 328
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
57-325 2.33e-30

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: 116.22  E-value: 2.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  57 PRVLGHEICGEIVGLGKNIANLKNGQQVAVIpyvacqqcpacksgrtnccekisviGVHQdggfsEYLSVPVANILPA-D 135
Cdd:cd08255   21 PLPPGYSSVGRVVEVGSGVTGFKPGDRVFCF-------------------------GPHA-----ERVVVPANLLVPLpD 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 136 GIDPQAAALIEPFAISAHAVRRAAIAPGEQVLVVGAGPIGL---------GaaaiakadGAQVVVADTSPARREHVAtrl 206
Cdd:cd08255   71 GLPPERAALTALAATALNGVRDAEPRLGERVAVVGLGLVGLlaaqlakaaG--------AREVVGVDPDAARRELAE--- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 207 ELPVLDPsAEDFDAQLRAQFGGSLaqkVIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRN 286
Cdd:cd08255  140 ALGPADP-VAADTADEIGGRGADV---VIEASGSPSALETALRLLRDRGRVVLVGWYGLKPLLLGEEFHFKRLPIRSSQV 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446028188 287 ATP------------EDFAKVGRLMAEGKITAdmMLTHRYPFATLAETYER 325
Cdd:cd08255  216 YGIgrydrprrwteaRNLEEALDLLAEGRLEA--LITHRVPFEDAPEAYRL 264
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
11-325 1.34e-26

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: 108.23  E-value: 1.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  11 QPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFfSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYV 90
Cdd:cd08281   17 DSRPLVIEEVELDPPGPGEVLVKIAAAGLCHSDLSVINGDRPR-PLPMALGHEAAGVVVEVGEGVTDLEVGDHVVLVFVP 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  91 ACQQCPACKSGRTNCCE---KISVIGVHQDGG------------------FSEYLSVPVANILPAD-GIDPQAAALIEPF 148
Cdd:cd08281   96 SCGHCRPCAEGRPALCEpgaAANGAGTLLSGGrrlrlrggeinhhlgvsaFAEYAVVSRRSVVKIDkDVPLEIAALFGCA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 149 AIS--AHAVRRAAIAPGEQVLVVGAGPIGLGAAAIAKAD-GAQVVVADTSPARREHVATRLELPVLDPSAEDFDAQLRAQ 225
Cdd:cd08281  176 VLTgvGAVVNTAGVRPGQSVAVVGLGGVGLSALLGAVAAgASQVVAVDLNEDKLALARELGATATVNAGDPNAVEQVREL 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 226 FGGSlAQKVIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFH--KKETTMMGSR--NATPE-DFAKVGRLMA 300
Cdd:cd08281  256 TGGG-VDYAFEMAGSVPALETAYEITRRGGTTVTAGLPDPEARLSVPALSlvAEERTLKGSYmgSCVPRrDIPRYLALYL 334
                        330       340
                 ....*....|....*....|....*
gi 446028188 301 EGKITADMMLTHRYPFATLAETYER 325
Cdd:cd08281  335 SGRLPVDKLLTHRLPLDEINEGFDR 359
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
21-340 1.77e-26

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: 108.06  E-value: 1.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  21 EIPIPGDneALIKIKSVGICGTDIHAWGGNQPFfSYPRVLGHEICGEIVGLGKNIANLKNGQQVaVIPY-VACQQCPACK 99
Cdd:cd08282   21 KIEHPTD--AIVRITTTAICGSDLHMYRGRTGA-EPGLVLGHEAMGEVEEVGSAVESLKVGDRV-VVPFnVACGRCRNCK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 100 SGRTNCCE----------KISVIGVHQDGGFSEYLSVPVA--NILPADGiDPQAAA------LIEPFAISAHAVRRAAIA 161
Cdd:cd08282   97 RGLTGVCLtvnpgraggaYGYVDMGPYGGGQAEYLRVPYAdfNLLKLPD-RDGAKEkddylmLSDIFPTGWHGLELAGVQ 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 162 PGEQVLVVGAGPIGL-GAAAIAKADGAQVVVADTSPARREHVATRLELPVlDPSAEDFDAQLRAQFGGSlAQKVIDATGN 240
Cdd:cd08282  176 PGDTVAVFGAGPVGLmAAYSAILRGASRVYVVDHVPERLDLAESIGAIPI-DFSDGDPVEQILGLEPGG-VDRAVDCVGY 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 241 Q-----------HAMNNTVNLIRHGGTVVFVGLF-------------KGELQFSDPEFHKKETTmMGSRNATPEDFAKVG 296
Cdd:cd08282  254 EardrggeaqpnLVLNQLIRVTRPGGGIGIVGVYvaedpgagdaaakQGELSFDFGLLWAKGLS-FGTGQAPVKKYNRQL 332
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 446028188 297 R-LMAEGKITADMMLTHRYPFATLAETYERdvINNRELIKGVITF 340
Cdd:cd08282  333 RdLILAGRAKPSFVVSHVISLEDAPEAYAR--FDKRLETKVVIKP 375
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
20-340 9.15e-26

formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol dehydrogenases and glutathione-dependant formaldehyde dehydrogenases (FDH) of the zinc-dependent/medium chain alcohol dehydrogenase family. The MDR family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. 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. 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: 176247 [Multi-domain]  Cd Length: 345  Bit Score: 105.47  E-value: 9.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  20 REIPIP---GDNEALIKIKSVGICGTDIHAWGGNQPFfSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYVACQQCP 96
Cdd:cd08287   15 EEVPDPvieEPTDAVIRVVATCVCGSDLWPYRGVSPT-RAPAPIGHEFVGVVEEVGSEVTSVKPGDFVIAPFAISDGTCP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  97 ACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVAN--ILPADGIDPQAAALIEPF-AISA------HAVRRAAIAPGEQVL 167
Cdd:cd08287   94 FCRAGFTTSCVHGGFWGAFVDGGQGEYVRVPLADgtLVKVPGSPSDDEDLLPSLlALSDvmgtghHAAVSAGVRPGSTVV 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 168 VVGAGPIGLgaaaiakadgAQVVVADTSPARR----EHVATRLELP-------VLDPSAEDFDAQLRAQFGGSLAQKVID 236
Cdd:cd08287  174 VVGDGAVGL----------CAVLAAKRLGAERiiamSRHEDRQALArefgatdIVAERGEEAVARVRELTGGVGADAVLE 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 237 ATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSrnatpedFAKVGRLMAE-------GKITADMM 309
Cdd:cd08287  244 CVGTQESMEQAIAIARPGGRVGYVGVPHGGVELDVRELFFRNVGLAGG-------PAPVRRYLPEllddvlaGRINPGRV 316
                        330       340       350
                 ....*....|....*....|....*....|.
gi 446028188 310 LTHRYPFATLAETYErdVINNRELIKGVITF 340
Cdd:cd08287  317 FDLTLPLDEVAEGYR--AMDERRAIKVLLRP 345
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
6-305 1.19e-25

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 105.12  E-value: 1.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   6 VLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNqpFFSYP-RVLGHEICGEIVGLGKNIANLKNGQQV 84
Cdd:PRK09422   4 AVVNKDHTGDVVVEKTLRPLKHGEALVKMEYCGVCHTDLHVANGD--FGDKTgRILGHEGIGIVKEVGPGVTSLKVGDRV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  85 AVI-PYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPV--ANILPaDGIDPQAAALIEPFAISAH-AVRRAAI 160
Cdd:PRK09422  82 SIAwFFEGCGHCEYCTTGRETLCRSVKNAGYTVDGGMAEQCIVTAdyAVKVP-EGLDPAQASSITCAGVTTYkAIKVSGI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 161 APGEQVLVVGAGPIG-LGAAAIAKADGAQVVVADTSPARREhVATRL--ELPVLDPSAEDFDAQLRAQFGGSLAqKVIDA 237
Cdd:PRK09422 161 KPGQWIAIYGAGGLGnLALQYAKNVFNAKVIAVDINDDKLA-LAKEVgaDLTINSKRVEDVAKIIQEKTGGAHA-AVVTA 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446028188 238 TgNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKIT 305
Cdd:PRK09422 239 V-AKAAFNQAVDAVRAGGRVVAVGLPPESMDLSIPRLVLDGIEVVGSLVGTRQDLEEAFQFGAEGKVV 305
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
25-262 8.55e-25

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: 102.96  E-value: 8.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  25 PGDNEALIKIKSVGICGTDIHAWGGNQPfFSYPRVLGHEICGEIVGLGKNIANLKNGQQVaVIPYVACQQCPACKSGRTN 104
Cdd:cd08278   25 PRPDEVLVRIVATGICHTDLVVRDGGLP-TPLPAVLGHEGAGVVEAVGSAVTGLKPGDHV-VLSFASCGECANCLSGHPA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 105 CCEKISVI-----------GVHQDGG------------FSEYLSVPVANILPADGIDPqaAALIEPFAIS----AHAV-R 156
Cdd:cd08278  103 YCENFFPLnfsgrrpdgstPLSLDDGtpvhghffgqssFATYAVVHERNVVKVDKDVP--LELLAPLGCGiqtgAGAVlN 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 157 RAAIAPGEQVLVVGAGPIGLGAAAIAKADGAQVVVA-DTSPARREhVAtrLEL---PVLDPSAEDFDAQLRAQFGGSlAQ 232
Cdd:cd08278  181 VLKPRPGSSIAVFGAGAVGLAAVMAAKIAGCTTIIAvDIVDSRLE-LA--KELgatHVINPKEEDLVAAIREITGGG-VD 256
                        250       260       270
                 ....*....|....*....|....*....|
gi 446028188 233 KVIDATGNQHAMNNTVNLIRHGGTVVFVGL 262
Cdd:cd08278  257 YALDTTGVPAVIEQAVDALAPRGTLALVGA 286
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
21-339 6.13e-24

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: 100.59  E-value: 6.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  21 EIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFfSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYVACQQCPACKS 100
Cdd:cd05279   19 EVAPPKAGEVRIKVVATGVCHTDLHVIDGKLPT-PLPVILGHEGAGIVESIGPGVTTLKPGDKVIPLFGPQCGKCKQCLN 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 101 GRTNCCEKISVI---GVHQDG------------------GFSEYLSVPVANILPAD-GIDPQAAALIePFAIS---AHAV 155
Cdd:cd05279   98 PRPNLCSKSRGTngrGLMSDGtsrftckgkpihhflgtsTFAEYTVVSEISLAKIDpDAPLEKVCLI-GCGFStgyGAAV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 156 RRAAIAPGEQVLVVGAGPIGLGAAAIAKADGAQVVVA-DTSPARREHVATRLELPVLDPSAEDFDAQ--LRAQFGGSlAQ 232
Cdd:cd05279  177 NTAKVTPGSTCAVFGLGGVGLSVIMGCKAAGASRIIAvDINKDKFEKAKQLGATECINPRDQDKPIVevLTEMTDGG-VD 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 233 KVIDATGNQHAMNNTVNLIRH-GGTVVFVGL--FKGELQFsDPEFHKKETTMMGSRNAT---PEDFAKVGRLMAEGKITA 306
Cdd:cd05279  256 YAFEVIGSADTLKQALDATRLgGGTSVVVGVppSGTEATL-DPNDLLTGRTIKGTVFGGwksKDSVPKLVALYRQKKFPL 334
                        330       340       350
                 ....*....|....*....|....*....|...
gi 446028188 307 DMMLTHRYPFATLAETYERdvINNRELIKGVIT 339
Cdd:cd05279  335 DELITHVLPFEEINDGFDL--MRSGESIRTILT 365
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
189-301 2.06e-23

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 93.44  E-value: 2.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  189 VVVADTSPARREHVatrLEL---PVLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQHAMNNTVNLIRHGGTVVFVGLFKG 265
Cdd:pfam00107  17 VIAVDGSEEKLELA---KELgadHVINPKETDLVEEIKELTGGKGVDVVFDCVGSPATLEQALKLLRPGGRVVVVGLPGG 93
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 446028188  266 ELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAE 301
Cdd:pfam00107  94 PLPLPLAPLLLKELTILGSFLGSPEEFPEALDLLAS 129
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
18-340 3.26e-23

Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain dehydrogenase/zinc-dependent alcohol dehydrogenase-like family, catalyzes the NADP(+)-dependent oxidation of glucose to gluconate, the first step in the Entner-Doudoroff pathway, an alternative to or substitute for glycolysis or the pentose phosphate pathway. 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-Rossman 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: 176192 [Multi-domain]  Cd Length: 355  Bit Score: 98.45  E-value: 3.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  18 KQREIPIPGDNEALIKIKSVGICGTD--IHAWGGNQPFFSYPR-VLGHEICGEIVGLGKNIaNLKNGQQVAVIPYVACQQ 94
Cdd:cd08230   16 VDIPEPEPTPGEVLVRTLEVGVCGTDreIVAGEYGTAPPGEDFlVLGHEALGVVEEVGDGS-GLSPGDLVVPTVRRPPGK 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  95 CPACKSGRTNCCE--KISVIGVHQDGGF-SEYLSVPVANILPadgIDP---QAAALIEPFAISAHAV-------RRAAIA 161
Cdd:cd08230   95 CLNCRIGRPDFCEtgEYTERGIKGLHGFmREYFVDDPEYLVK---VPPslaDVGVLLEPLSVVEKAIeqaeavqKRLPTW 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 162 PGEQVLVVGAGPIGLGAAAIAKADGAQVVVADtspaRREHVATRLELpVLDPSAEDFDAQLRAQFGGSLAQK---VIDAT 238
Cdd:cd08230  172 NPRRALVLGAGPIGLLAALLLRLRGFEVYVLN----RRDPPDPKADI-VEELGATYVNSSKTPVAEVKLVGEfdlIIEAT 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 239 GNQHAMNNTVNLIRHGGTVVFVGL--FKGELQFSDPEFHK----KETTMMGSRNATPEDFAKVGRLMAEGKI----TADM 308
Cdd:cd08230  247 GVPPLAFEALPALAPNGVVILFGVpgGGREFEVDGGELNRdlvlGNKALVGSVNANKRHFEQAVEDLAQWKYrwpgVLER 326
                        330       340       350
                 ....*....|....*....|....*....|..
gi 446028188 309 MLTHRYPFATLAETYERDVinnRELIKGVITF 340
Cdd:cd08230  327 LITRRVPLEEFAEALTEKP---DGEIKVVIEW 355
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
8-339 6.26e-23

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: 97.79  E-value: 6.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   8 ICQQPKE-LVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGnQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVav 86
Cdd:cd08277    7 VAWEAGKpLVIEEIEVAPPKANEVRIKMLATSVCHTDILAIEG-FKATLFPVILGHEGAGIVESVGEGVTNLKPGDKV-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  87 IPYVA--CQQCPACKSGRTNCCEK--ISVIGVHQDG------------------GFSEYLSVPVANILPADGIDPQAAAL 144
Cdd:cd08277   84 IPLFIgqCGECSNCRSGKTNLCQKyrANESGLMPDGtsrftckgkkiyhflgtsTFSQYTVVDENYVAKIDPAAPLEHVC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 145 IEPFAIS---AHAVRRAAIAPGEQVLVVGAGPIGLGAAAIAKAD-GAQVVVADTSPARREHvATRLELP-VLDP--SAED 217
Cdd:cd08277  164 LLGCGFStgyGAAWNTAKVEPGSTVAVFGLGAVGLSAIMGAKIAgASRIIGVDINEDKFEK-AKEFGATdFINPkdSDKP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 218 FDAQLRAQFGGSLaQKVIDATGNQHAMNNTVNLIRHG-GTVVFVGLFKGELQFSDP-----EFHKKETTMMGSRNAtpED 291
Cdd:cd08277  243 VSEVIREMTGGGV-DYSFECTGNADLMNEALESTKLGwGVSVVVGVPPGAELSIRPfqlilGRTWKGSFFGGFKSR--SD 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 446028188 292 FAKVGRLMAEGKITADMMLTHRYPFATLAETYerDVINNRELIKGVIT 339
Cdd:cd08277  320 VPKLVSKYMNKKFDLDELITHVLPFEEINKGF--DLMKSGECIRTVIT 365
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
23-332 2.36e-20

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: 90.10  E-value: 2.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  23 PIPGDNEALIKIKSVGICGTD---IHAWggnqPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYVACQQCPACK 99
Cdd:cd08264   22 PKPGPGEVLIRVKMAGVNPVDynvINAV----KVKPMPHIPGAEFAGVVEEVGDHVKGVKKGDRVVVYNRVFDGTCDMCL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 100 SGRTNCCEKISVIGVHQDGGFSEYLSVPVANI--LPADGIDPQAAALiePFAI--SAHAVRRAAIAPGEQVLVVGA-GPI 174
Cdd:cd08264   98 SGNEMLCRNGGIIGVVSNGGYAEYIVVPEKNLfkIPDSISDELAASL--PVAAltAYHALKTAGLGPGETVVVFGAsGNT 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 175 GLGAAAIAKADGAQVVVAdtspARREHVATRLELPVLDPSaedfDAQLRAQFGGSLAQKVIDATGNQHAMNNTVNLIRHG 254
Cdd:cd08264  176 GIFAVQLAKMMGAEVIAV----SRKDWLKEFGADEVVDYD----EVEEKVKEITKMADVVINSLGSSFWDLSLSVLGRGG 247
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446028188 255 GTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITadmmlTHR-YPFATLAETYERDVINNRE 332
Cdd:cd08264  248 RLVTFGTLTGGEVKLDLSDLYSKQISIIGSTGGTRKELLELVKIAKDLKVK-----VWKtFKLEEAKEALKELFSKERD 321
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
12-304 2.25e-19

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: 87.74  E-value: 2.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKELVWKQ-REIPIPGDNEALIKIKSVGICGTDI--------------------HAWGGNQPFFSYPRVLGHEICGEIVG 70
Cdd:cd08274   12 LDKLVYRDdVPVPTPAPGEVLIRVGACGVNNTDIntregwystevdgatdstgaGEAGWWGGTLSFPRIQGADIVGRVVA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  71 LGKNIANLKNGQQVAVIPYVacqqcpacKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILP--ADGIDPQAAALIEPF 148
Cdd:cd08274   92 VGEGVDTARIGERVLVDPSI--------RDPPEDDPADIDYIGSERDGGFAEYTVVPAENAYPvnSPLSDVELATFPCSY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 149 AISAHAVRRAAIAPGEQVLVVGA-GPIGLGAAAIAKADGAQvVVADTSPARREHVATRLELPVLDPSAEDFDAQLRAqfG 227
Cdd:cd08274  164 STAENMLERAGVGAGETVLVTGAsGGVGSALVQLAKRRGAI-VIAVAGAAKEEAVRALGADTVILRDAPLLADAKAL--G 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 228 GSLAQKVIDATGNQhAMNNTVNLIRHGGTVVFVGLFKG---ELQFSDpeFHKKETTMMGSRNATPEDFAKVGRLMAEGKI 304
Cdd:cd08274  241 GEPVDVVADVVGGP-LFPDLLRLLRPGGRYVTAGAIAGpvvELDLRT--LYLKDLTLFGSTLGTREVFRRLVRYIEEGEI 317
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
4-325 1.82e-18

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: 84.47  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQ---PKELVWkqREI-PIPG-DNEALIKIKSVGICGTDI-HAWGGNQ-----PFfsyprVLGHEICGEIVGLG 72
Cdd:cd08241    1 MKAVVCKElggPEDLVL--EEVpPEPGaPGEVRIRVEAAGVNFPDLlMIQGKYQvkpplPF-----VPGSEVAGVVEAVG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  73 KNIANLKNGQQVavipyvacqqcpacksgrtnccekisvIGVHQDGGFSEYLSVPVANILPA-DGIDP-QAAALIEPFAI 150
Cdd:cd08241   74 EGVTGFKVGDRV---------------------------VALTGQGGFAEEVVVPAAAVFPLpDGLSFeEAAALPVTYGT 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 151 SAHA-VRRAAIAPGEQVLVVGA-GPIGLGAAAIAKADGAQVVVADTSPARREHVATRLELPVLDPSAEDFDAQLRAQFGG 228
Cdd:cd08241  127 AYHAlVRRARLQPGETVLVLGAaGGVGLAAVQLAKALGARVIAAASSEEKLALARALGADHVIDYRDPDLRERVKALTGG 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 229 SLAQKVIDATGNQHAmNNTVNLIRHGGTVVFVG--------------LFK---------GELQFSDPEfhkkettmmgsr 285
Cdd:cd08241  207 RGVDVVYDPVGGDVF-EASLRSLAWGGRLLVIGfasgeipqipanllLLKnisvvgvywGAYARREPE------------ 273
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 446028188 286 nATPEDFAKVGRLMAEGKITadMMLTHRYPFATLAETYER 325
Cdd:cd08241  274 -LLRANLAELFDLLAEGKIR--PHVSAVFPLEQAAEALRA 310
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
12-325 3.91e-18

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: 83.42  E-value: 3.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKELVWKQREIPIP--GDNEALIKIKSVGICGTDIHAWGGNQP---FFSYPRVLGHEICGEIVGLGKNIANLKNGQQVav 86
Cdd:cd08267    9 PEVLLLLEVEVPIPtpKPGEVLVKVHAASVNPVDWKLRRGPPKlllGRPFPPIPGMDFAGEVVAVGSGVTRFKVGDEV-- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  87 ipyvacqqcpacksgrtnccekISVIGVHQDGGFSEYLSVPVANILP-ADGIDP-QAAALiePFA-ISA-HAVRRAA-IA 161
Cdd:cd08267   87 ----------------------FGRLPPKGGGALAEYVVAPESGLAKkPEGVSFeEAAAL--PVAgLTAlQALRDAGkVK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 162 PGEQVLVVGA-GPIG---------LGAaaiakadgaqVVVADTSPARREHV----ATRlelpVLDPSAEDFDAQLRaqfg 227
Cdd:cd08267  143 PGQRVLINGAsGGVGtfavqiakaLGA----------HVTGVCSTRNAELVrslgADE----VIDYTTEDFVALTA---- 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 228 gsLAQK---VIDATGNQH-AMNNTVNLIRHGGTVVFVGLFKGELQFSDPE-------FHKKETTMMGSrnATPEDFAKVG 296
Cdd:cd08267  205 --GGEKydvIFDAVGNSPfSLYRASLALKPGGRYVSVGGGPSGLLLVLLLlpltlggGGRRLKFFLAK--PNAEDLEQLA 280
                        330       340       350
                 ....*....|....*....|....*....|.
gi 446028188 297 RLMAEGKITA--DmmltHRYPFATLAETYER 325
Cdd:cd08267  281 ELVEEGKLKPviD----SVYPLEDAPEAYRR 307
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
26-262 9.52e-18

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 83.00  E-value: 9.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  26 GDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYV-ACQQCPACKSGRTN 104
Cdd:PLN02586  36 GDEDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGKNVKKFKEGDRVGVGVIVgSCKSCESCDQDLEN 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 105 CCEKISVI-------GVHQDGGFSEYLSVP------VANILPADGIDPQAAALIEPFAISAHavrRAAIAPGEQVLVVGA 171
Cdd:PLN02586 116 YCPKMIFTynsighdGTKNYGGYSDMIVVDqhfvlrFPDNLPLDAGAPLLCAGITVYSPMKY---YGMTEPGKHLGVAGL 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 172 GPIGLGAAAIAKADGAQVVVADTSPARREHVATRLE----LPVLDPSaedfdaQLRAQFGgsLAQKVIDATGNQHAMNNT 247
Cdd:PLN02586 193 GGLGHVAVKIGKAFGLKVTVISSSSNKEDEAINRLGadsfLVSTDPE------KMKAAIG--TMDYIIDTVSAVHALGPL 264
                        250
                 ....*....|....*
gi 446028188 248 VNLIRHGGTVVFVGL 262
Cdd:PLN02586 265 LGLLKVNGKLITLGL 279
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
13-176 1.11e-16

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: 79.97  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  13 KELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVavIP-YVA 91
Cdd:cd08300   13 KPLSIEEVEVAPPKAGEVRIKILATGVCHTDAYTLSGADPEGLFPVILGHEGAGIVESVGEGVTSVKPGDHV--IPlYTP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  92 -CQQCPACKSGRTNCCEKISVI---GVHQDG------------------GFSEYLSVP---VANIlpadgiDPQAaalie 146
Cdd:cd08300   91 eCGECKFCKSGKTNLCQKIRATqgkGLMPDGtsrfsckgkpiyhfmgtsTFSEYTVVAeisVAKI------NPEA----- 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446028188 147 PF--------AIS---AHAVRRAAIAPGEQVLVVGAGPIGL 176
Cdd:cd08300  160 PLdkvcllgcGVTtgyGAVLNTAKVEPGSTVAVFGLGAVGL 200
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
20-325 1.12e-16

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: 79.14  E-value: 1.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  20 REIPIP--GDNEALIKIKSVGICGTDIHAW-GGNQPFFSY--PRVLGHEICGEIVGLGKNIANLKNGQQVavipyvacqq 94
Cdd:cd05289   18 ADVPTPepGPGEVLVKVHAAGVNPVDLKIReGLLKAAFPLtlPLIPGHDVAGVVVAVGPGVTGFKVGDEV---------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  95 cpacksgrtnccekISVIGVHQDGGFSEYLSVPVANILPA-DGID-PQAAALiepfAISA----HAVRRAA-IAPGEQVL 167
Cdd:cd05289   88 --------------FGMTPFTRGGAYAEYVVVPADELALKpANLSfEEAAAL----PLAGltawQALFELGgLKAGQTVL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 168 VVGA-GPIGLGAAAIAKADGAQvVVADTSPARREHVATRLELPVLDPSAEDFDAQLraqfGGSLAQKVIDATGNQHAMnN 246
Cdd:cd05289  150 IHGAaGGVGSFAVQLAKARGAR-VIATASAANADFLRSLGADEVIDYTKGDFERAA----APGGVDAVLDTVGGETLA-R 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 247 TVNLIRHGGTVV-FVGLFKGELQFSDPEFHKKETTMMGSRnatpEDFAKVGRLMAEGKITADmmLTHRYPFATLAETYER 325
Cdd:cd05289  224 SLALVKPGGRLVsIAGPPPAEQAAKRRGVRAGFVFVEPDG----EQLAELAELVEAGKLRPV--VDRVFPLEDAAEAHER 297
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
26-288 9.75e-16

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 77.14  E-value: 9.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  26 GDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYV-ACQQCPACKSGRTN 104
Cdd:PLN02514  33 GPEDVVIKVIYCGICHTDLHQIKNDLGMSNYPMVPGHEVVGEVVEVGSDVSKFTVGDIVGVGVIVgCCGECSPCKSDLEQ 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 105 CCEKI--SVIGVHQD-----GGFSEYLSVP---VANIlpADGIDPQAAALIEPFAISAHAVRR--AAIAPGEQVLVVGAG 172
Cdd:PLN02514 113 YCNKRiwSYNDVYTDgkptqGGFASAMVVDqkfVVKI--PEGMAPEQAAPLLCAGVTVYSPLShfGLKQSGLRGGILGLG 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 173 PIGLGAAAIAKADGAQVVVADTSPARREHVATRLelpvldpSAEDF----DAQLRAQFGGSLaQKVIDATGNQHAMNNTV 248
Cdd:PLN02514 191 GVGHMGVKIAKAMGHHVTVISSSDKKREEALEHL-------GADDYlvssDAAEMQEAADSL-DYIIDTVPVFHPLEPYL 262
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446028188 249 NLIRHGGTVVFVGLFKGELQFSDPEFhkkettMMGSRNAT 288
Cdd:PLN02514 263 SLLKLDGKLILMGVINTPLQFVTPML------MLGRKVIT 296
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
4-263 3.92e-15

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: 75.00  E-value: 3.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   4 MNVLICQQPKE---LVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKN 80
Cdd:cd08271    1 MKAWVLPKPGAalqLTLEEIEIPGPGAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTGWKV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  81 GQQVAvipyvacqqcpacksgrtnccekisvigVHQD----GGFSEYLSVPVANILPA-DGIDPQAAALIEPFAISA-HA 154
Cdd:cd08271   81 GDRVA----------------------------YHASlargGSFAEYTVVDARAVLPLpDSLSFEEAAALPCAGLTAyQA 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 155 V-RRAAIAPGEQVLVVGA-GPIGlGAAAIAKADGAQVVVADTSPARREHVATRLELPVLDPSAEDFDAQLRAQFGGSLAQ 232
Cdd:cd08271  133 LfKKLRIEAGRTILITGGaGGVG-SFAVQLAKRAGLRVITTCSKRNFEYVKSLGADHVIDYNDEDVCERIKEITGGRGVD 211
                        250       260       270
                 ....*....|....*....|....*....|.
gi 446028188 233 KVIDATGNQHAMNNTVNLIRHGGTVVFVGLF 263
Cdd:cd08271  212 AVLDTVGGETAAALAPTLAFNGHLVCIQGRP 242
PLN02740 PLN02740
Alcohol dehydrogenase-like
3-176 7.22e-15

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 74.83  E-value: 7.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   3 TMNVLICQQPKE-LVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGG-NQPFFSYPRVLGHEICGEIVGLGKNIANLKN 80
Cdd:PLN02740  10 TCKAAVAWGPGEpLVMEEIRVDPPQKMEVRIKILYTSICHTDLSAWKGeNEAQRAYPRILGHEAAGIVESVGEGVEDLKA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  81 GQQVAVIPYVACQQCPACKSGRTNCCEKISV-----IGVHqDGG--------------------FSEYLSVPVANILPAD 135
Cdd:PLN02740  90 GDHVIPIFNGECGDCRYCKRDKTNLCETYRVdpfksVMVN-DGKtrfstkgdgqpiyhflntstFTEYTVLDSACVVKID 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446028188 136 GIDPQAAALIEPFAIS---AHAVRRAAIAPGEQVLVVGAGPIGL 176
Cdd:PLN02740 169 PNAPLKKMSLLSCGVStgvGAAWNTANVQAGSSVAIFGLGAVGL 212
sorbose_phosphate_red cd08238
L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, ...
21-312 8.28e-15

L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, catalyzes the NADPH-dependent conversion of l-sorbose 1-phosphate to d-glucitol 6-phosphate in the metabolism of L-sorbose to (also converts d-fructose 1-phosphate to d-mannitol 6-phosphate). 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.


Pssm-ID: 176200 [Multi-domain]  Cd Length: 410  Bit Score: 74.78  E-value: 8.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  21 EIPIPGDNEALIKIKSVGICGTDIHA--WGGNQP-----FFSYPRVLGHEICGEIVGLGKNIAN-LKNGQQVAVIPYVAC 92
Cdd:cd08238   20 ELPEIADDEILVRVISDSLCFSTWKLalQGSDHKkvpndLAKEPVILGHEFAGTILKVGKKWQGkYKPGQRFVIQPALIL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  93 QQCPACKS-GRTNCcekisvigvhqdGGFSEYLSVP--VAN---ILPADGIDPQAAALIEPFA--ISAHAVRRAAIaPGE 164
Cdd:cd08238  100 PDGPSCPGySYTYP------------GGLATYHIIPneVMEqdcLLIYEGDGYAEASLVEPLScvIGAYTANYHLQ-PGE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 165 Q------------VLVVGAGPIGLGAAAIAKADGAQ---VVVADTSPARREHVATRL---------ELPVLDPSAED-FD 219
Cdd:cd08238  167 YrhrmgikpggntAILGGAGPMGLMAIDYAIHGPIGpslLVVTDVNDERLARAQRLFppeaasrgiELLYVNPATIDdLH 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 220 AQLRAQFGGSLAQKVIDATGNQHAMNNTVNLI-RHGGTVVFVGL----FKGELQFSDpeFHKKETTMMGSRNATPEDFAK 294
Cdd:cd08238  247 ATLMELTGGQGFDDVFVFVPVPELVEEADTLLaPDGCLNFFAGPvdknFSAPLNFYN--VHYNNTHYVGTSGGNTDDMKE 324
                        330
                 ....*....|....*...
gi 446028188 295 VGRLMAEGKITADMMLTH 312
Cdd:cd08238  325 AIDLMAAGKLNPARMVTH 342
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
20-261 8.38e-15

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: 74.22  E-value: 8.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  20 REIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSY-PRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYVacqqcpac 98
Cdd:cd08273   20 ADLPEPAAGEVVVKVEASGVSFADVQMRRGLYPDQPPlPFTPGYDLVGRVDALGSGVTGFEVGDRVAALTRV-------- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  99 ksgrtnccekisvigvhqdGGFSEYLSVPVANILPA-DGIDP-QAAALIEPFAISAHAVRRAA-IAPGEQVLVVGA-GPI 174
Cdd:cd08273   92 -------------------GGNAEYINLDAKYLVPVpEGVDAaEAVCLVLNYVTAYQMLHRAAkVLTGQRVLIHGAsGGV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 175 GLGAAAIAKADGAQVVVadTSPARREHVATRLELPVLDPSAEDFDAQLRAQfGGSLAqkVIDATGNQHaMNNTVNLIRHG 254
Cdd:cd08273  153 GQALLELALLAGAEVYG--TASERNHAALRELGATPIDYRTKDWLPAMLTP-GGVDV--VFDGVGGES-YEESYAALAPG 226

                 ....*..
gi 446028188 255 GTVVFVG 261
Cdd:cd08273  227 GTLVCYG 233
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
13-176 9.41e-15

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: 74.27  E-value: 9.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  13 KELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFsYPRVLGHEICGEIVGLGKNIANLKNGQQvaVIPYVA- 91
Cdd:cd08299   18 KPFSIEEIEVAPPKAHEVRIKIVATGICRSDDHVVSGKLVTP-FPVILGHEAAGIVESVGEGVTTVKPGDK--VIPLFVp 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  92 -CQQCPACKSGRTNCCEKISVI---GVHQDG------------------GFSEYLSVPVANILPADGidpqAAALIEPFA 149
Cdd:cd08299   95 qCGKCRACLNPESNLCLKNDLGkpqGLMQDGtsrftckgkpihhflgtsTFSEYTVVDEIAVAKIDA----AAPLEKVCL 170
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446028188 150 IS-------AHAVRRAAIAPGEQVLVVGAGPIGL 176
Cdd:cd08299  171 IGcgfstgyGAAVNTAKVTPGSTCAVFGLGGVGL 204
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
21-266 1.77e-14

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: 73.02  E-value: 1.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  21 EIPIPGDNEALIKIKSVGICGTDIhAW--GGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPyvacqQCPAc 98
Cdd:cd08268   21 PVPAPGAGEVLIRVEAIGLNRADA-MFrrGAYIEPPPLPARLGYEAAGVVEAVGAGVTGFAVGDRVSVIP-----AADL- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  99 ksgrtnccekisvigvHQDGGFSEYLSVPVANILPA-DGIDP-QAAALIEPFaISAHA--VRRAAIAPGEQVLVVGA-GP 173
Cdd:cd08268   94 ----------------GQYGTYAEYALVPAAAVVKLpDGLSFvEAAALWMQY-LTAYGalVELAGLRPGDSVLITAAsSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 174 IGLGAAAIAKADGAQVVVADTSPARRE--------HVATRLElpvldpsaEDFDAQLRAQFGGSLAQKVIDATGNQHaMN 245
Cdd:cd08268  157 VGLAAIQIANAAGATVIATTRTSEKRDallalgaaHVIVTDE--------EDLVAEVLRITGGKGVDVVFDPVGGPQ-FA 227
                        250       260
                 ....*....|....*....|.
gi 446028188 246 NTVNLIRHGGTVVFVGLFKGE 266
Cdd:cd08268  228 KLADALAPGGTLVVYGALSGE 248
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
13-176 2.14e-14

Plant 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: 176261 [Multi-domain]  Cd Length: 369  Bit Score: 73.10  E-value: 2.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  13 KELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYVAC 92
Cdd:cd08301   13 KPLVIEEVEVAPPQAMEVRIKILHTSLCHTDVYFWEAKGQTPLFPRILGHEAAGIVESVGEGVTDLKPGDHVLPVFTGEC 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  93 QQCPACKSGRTNCCEKISVI----GVHQDGG------------------FSEYLSVPVANILPadgIDPQA----AALIE 146
Cdd:cd08301   93 KECRHCKSEKSNMCDLLRINtdrgVMINDGKsrfsingkpiyhfvgtstFSEYTVVHVGCVAK---INPEApldkVCLLS 169
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446028188 147 ---PFAISAhAVRRAAIAPGEQVLVVGAGPIGL 176
Cdd:cd08301  170 cgvSTGLGA-AWNVAKVKKGSTVAIFGLGAVGL 201
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
26-262 1.29e-13

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 70.82  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  26 GDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAV-IPYVACQQCPACKSGRTN 104
Cdd:PLN02178  30 GENDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVGKNVTKFKEGDRVGVgVIIGSCQSCESCNQDLEN 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 105 CCEKI-------SVIGVHQDGGFSEYLSV------PVANILPADGIDPQAAALIEPFaiSAHAVRRAAIAPGEQVLVVGA 171
Cdd:PLN02178 110 YCPKVvftynsrSSDGTRNQGGYSDVIVVdhrfvlSIPDGLPSDSGAPLLCAGITVY--SPMKYYGMTKESGKRLGVNGL 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 172 GPIGLGAAAIAKADGAQVVVADTSPARREHVATRLelpvldpSAEDF----DAQLRAQFGGSLaQKVIDATGNQHAMNNT 247
Cdd:PLN02178 188 GGLGHIAVKIGKAFGLRVTVISRSSEKEREAIDRL-------GADSFlvttDSQKMKEAVGTM-DFIIDTVSAEHALLPL 259
                        250
                 ....*....|....*
gi 446028188 248 VNLIRHGGTVVFVGL 262
Cdd:PLN02178 260 FSLLKVSGKLVALGL 274
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
12-271 2.88e-13

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: 69.56  E-value: 2.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNiaNLKNGQQVAVIpyva 91
Cdd:cd08243   12 PEVLKLREIPIPEPKPGWVLIRVKAFGLNRSEIFTRQGHSPSVKFPRVLGIEAVGEVEEAPGG--TFTPGQRVATA---- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  92 cqqcpacksgrtnccekISVIGVHQDGGFSEYLSVPVANILPadgIDP-----QAAALIEPFAISAHAVRRA-AIAPGEQ 165
Cdd:cd08243   86 -----------------MGGMGRTFDGSYAEYTLVPNEQVYA---IDSdlswaELAALPETYYTAWGSLFRSlGLQPGDT 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 166 VLVVGaGPIGLGAAAIAKADGAQVVVADTSpaRREHVATRLELP-----VLDPsaEDFDAQLRAQFGGSlaQKVIDATGN 240
Cdd:cd08243  146 LLIRG-GTSSVGLAALKLAKALGATVTATT--RSPERAALLKELgadevVIDD--GAIAEQLRAAPGGF--DKVLELVGT 218
                        250       260       270
                 ....*....|....*....|....*....|.
gi 446028188 241 QhAMNNTVNLIRHGGTVVFVGLFKGELQFSD 271
Cdd:cd08243  219 A-TLKDSLRHLRPGGIVCMTGLLGGQWTLED 248
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
11-321 5.67e-13

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: 68.46  E-value: 5.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  11 QPKELVWKQREIPIP--GDNEALIKIKSVGICGTDIHAWGGNQPFF-SYPRVLGHEICGEIVGLGKNIANLKNGQQVAVI 87
Cdd:cd05282    8 EPLPLVLELVSLPIPppGPGEVLVRMLAAPINPSDLITISGAYGSRpPLPAVPGNEGVGVVVEVGSGVSGLLVGQRVLPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  88 PYVacqqcpacksgrtnccekisvigvhqdGGFSEYLSVPVANILP-ADGIDPQAAA--LIEPFAISAHAVRRAAIAPGE 164
Cdd:cd05282   88 GGE---------------------------GTWQEYVVAPADDLIPvPDSISDEQAAmlYINPLTAWLMLTEYLKLPPGD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 165 QVLVVGAGP------IGLGAAAIAkadgaqVVVADTSpaRREHVATRLEL---PVLDPSAEDFDAQLRAQFGGSLAQKVI 235
Cdd:cd05282  141 WVIQNAANSavgrmlIQLAKLLGF------KTINVVR--RDEQVEELKALgadEVIDSSPEDLAQRVKEATGGAGARLAL 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 236 DATGNQHAmNNTVNLIRHGGTVVFVGLFKGELQ-FSDPEFHKKETTMMG----------SRNATPEDFAKVGRLMAEGKI 304
Cdd:cd05282  213 DAVGGESA-TRLARSLRPGGTLVNYGLLSGEPVpFPRSVFIFKDITVRGfwlrqwlhsaTKEAKQETFAEVIKLVEAGVL 291
                        330
                 ....*....|....*..
gi 446028188 305 TAdmMLTHRYPFATLAE 321
Cdd:cd05282  292 TT--PVGAKFPLEDFEE 306
PLN02827 PLN02827
Alcohol dehydrogenase-like
1-200 8.46e-13

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 68.39  E-value: 8.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188   1 MSTMNVLICQQ-----PKE-LVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGgNQPFFsyPRVLGHEICGEIVGLGKN 74
Cdd:PLN02827   5 ISQPNVITCRAavawgAGEaLVMEEVEVSPPQPLEIRIKVVSTSLCRSDLSAWE-SQALF--PRIFGHEASGIVESIGEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  75 IANLKNGQQVAVIPYVACQQCPACKSGRTNCCEKISV--IGV-HQDGG------------------FSEYLSVPVANILP 133
Cdd:PLN02827  82 VTEFEKGDHVLTVFTGECGSCRHCISGKSNMCQVLGLerKGVmHSDQKtrfsikgkpvyhycavssFSEYTVVHSGCAVK 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446028188 134 ADGIDPQAAALIEPFAISA---HAVRRAAIAPGEQVLVVGAGPIGLGAAA-IAKADGAQVVVADTSPARRE 200
Cdd:PLN02827 162 VDPLAPLHKICLLSCGVAAglgAAWNVADVSKGSSVVIFGLGTVGLSVAQgAKLRGASQIIGVDINPEKAE 232
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
12-265 1.70e-12

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: 67.08  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNqpffsYP------RVLGHEICGEIVGLGKNIANLKNGQQVA 85
Cdd:cd05276   12 PEVLELGEVPKPAPGPGEVLIRVAAAGVNRADLLQRQGL-----YPpppgasDILGLEVAGVVVAVGPGVTGWKVGDRVC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  86 VIpyvacqqcpacksgrtnccekisVIGvhqdGGFSEYLSVPVANILPA-DGIDP-QAAALIEPFAISAHAVR-RAAIAP 162
Cdd:cd05276   87 AL-----------------------LAG----GGYAEYVVVPAGQLLPVpEGLSLvEAAALPEVFFTAWQNLFqLGGLKA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 163 GEQVLV-VGAGPIGLGAAAIAKADGAQVVVADTSPARREHV----ATRlelpVLDPSAEDFDAQLRAQFGGSLAQKVIDA 237
Cdd:cd05276  140 GETVLIhGGASGVGTAAIQLAKALGARVIATAGSEEKLEACralgADV----AINYRTEDFAEEVKEATGGRGVDVILDM 215
                        250       260
                 ....*....|....*....|....*...
gi 446028188 238 TGNQHaMNNTVNLIRHGGTVVFVGLFKG 265
Cdd:cd05276  216 VGGDY-LARNLRALAPDGRLVLIGLLGG 242
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
16-329 2.02e-12

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: 66.84  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  16 VWKQREIPIP--GDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGH-EICGEIVGLGKNIANLKNGQQVAVipyvac 92
Cdd:cd08253   14 VLRLGDLPVPtpGPGEVLVRVHASGVNPVDTYIRAGAYPGLPPLPYVPGsDGAGVVEAVGEGVDGLKVGDRVWL------ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  93 qqCPACKSGRTnccekisvigvhqdGGFSEYLSVPVANILP-ADGIDP-QAAALIEPFAISAHAV-RRAAIAPGEQVLVV 169
Cdd:cd08253   88 --TNLGWGRRQ--------------GTAAEYVVVPADQLVPlPDGVSFeQGAALGIPALTAYRALfHRAGAKAGETVLVH 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 170 G-AGPIGLGAAAIAKADGAQVVVADTSPARREHVATRLELPVLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQHaMNNTV 248
Cdd:cd08253  152 GgSGAVGHAAVQLARWAGARVIATASSAEGAELVRQAGADAVFNYRAEDLADRILAATAGQGVDVIIEVLANVN-LAKDL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 249 NLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSR--NATPEDFAK----VGRLMAEGKITADMmlTHRYPFATLAET 322
Cdd:cd08253  231 DVLAPGGRIVVYGSGGLRGTIPINPLMAKEASIRGVLlyTATPEERAAaaeaIAAGLADGALRPVI--AREYPLEEAAAA 308

                 ....*..
gi 446028188 323 YErDVIN 329
Cdd:cd08253  309 HE-AVES 314
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
21-172 4.80e-11

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: 63.04  E-value: 4.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  21 EIPIPGDNEALIKIKSVGICGTDI-HAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYvacqqcpack 99
Cdd:cd08250   24 PVPLPGPGEVLVKNRFVGINASDInFTAGRYDPGVKPPFDCGFEGVGEVVAVGEGVTDFKVGDAVATMSF---------- 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446028188 100 sgrtnccekisvigvhqdGGFSEYLSVPVANILPADGIDPQAAALIEPFAISAHAVRRAA-IAPGEQVLVVGAG 172
Cdd:cd08250   94 ------------------GAFAEYQVVPARHAVPVPELKPEVLPLLVSGLTASIALEEVGeMKSGETVLVTAAA 149
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
12-306 5.03e-11

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: 62.99  E-value: 5.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKELVWKQREIPIPGDNEALIKIKSVGICGTD-IHAWGGNQPffSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVipyv 90
Cdd:cd08249   11 GGLLVVVDVPVPKPGPDEVLVKVKAVALNPVDwKHQDYGFIP--SYPAILGCDFAGTVVEVGSGVTRFKVGDRVAG---- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  91 acqqcpACKSGRTNCcekisvigvHQDGGFSEYLSVPVANILP-ADGIDPQAAALIePFAISAhavrrAAIA-------- 161
Cdd:cd08249   85 ------FVHGGNPND---------PRNGAFQEYVVADADLTAKiPDNISFEEAATL-PVGLVT-----AALAlfqklglp 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 162 ----------PGEQVLV------VGAGPIglgaaaiakadgaQV-------VVADTSPARREHV----ATRlelpVLDPS 214
Cdd:cd08249  144 lpppkpspasKGKPVLIwggsssVGTLAI-------------QLaklagykVITTASPKNFDLVkslgADA----VFDYH 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 215 AEDFDAQLRAQFGGSLAqKVIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGS--------RN 286
Cdd:cd08249  207 DPDVVEDIRAATGGKLR-YALDCISTPESAQLCAEALGRSGGGKLVSLLPVPEETEPRKGVKVKFVLGYTvfgeipedRE 285
                        330       340
                 ....*....|....*....|
gi 446028188 287 ATPEDFAKVGRLMAEGKITA 306
Cdd:cd08249  286 FGEVFWKYLPELLEEGKLKP 305
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
15-317 9.81e-11

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: 62.07  E-value: 9.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  15 LVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFfSYPRVLGHEICGEIVGLGKNIANLKNGQQVAvipYVACQq 94
Cdd:cd05286   14 LEYEDVPVPEPGPGEVLVRNTAIGVNFIDTYFRSGLYPL-PLPFVLGVEGAGVVEAVGPGVTGFKVGDRVA---YAGPP- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  95 cpacksgrtnccekisvigvhqdGGFSEYLSVPVANILP-ADGIDP-QAAALIEPfAISAHA-VRRA-AIAPGEQVLVVG 170
Cdd:cd05286   89 -----------------------GAYAEYRVVPASRLVKlPDGISDeTAAALLLQ-GLTAHYlLRETyPVKPGDTVLVHA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 171 -AGPIGLGAAAIAKADGAQVVVADTSPAR----REHVATRlelpVLDPSAEDFDAQLRAQFGGSLAQKVIDATGnQHAMN 245
Cdd:cd05286  145 aAGGVGLLLTQWAKALGATVIGTVSSEEKaelaRAAGADH----VINYRDEDFVERVREITGGRGVDVVYDGVG-KDTFE 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 246 NTVNLIRHGGTVVFVG-------------LFKGELQFSDPefhkkettMMGSRNATPEDFAK----VGRLMAEGKITADm 308
Cdd:cd05286  220 GSLDSLRPRGTLVSFGnasgpvppfdllrLSKGSLFLTRP--------SLFHYIATREELLAraaeLFDAVASGKLKVE- 290

                 ....*....
gi 446028188 309 mLTHRYPFA 317
Cdd:cd05286  291 -IGKRYPLA 298
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
21-255 2.05e-10

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: 60.90  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  21 EIPIPGDNEALIKIKSVGICGTDIHAWGGNQP-FFSYPRVLGHEICGEIVGLGKNIANLKNGQQVavipyvacqqcpack 99
Cdd:cd08251    1 EVAPPGPGEVRIQVRAFSLNFGDLLCVRGLYPtMPPYPFTPGFEASGVVRAVGPHVTRLAVGDEV--------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 100 sgrtnccekISVIGVHQdGGFSEYLSVPVANIL--PADGIDPQAAALIEPFAISAHAVRRAAIAPGEQVLVVGA-GPIGL 176
Cdd:cd08251   66 ---------IAGTGESM-GGHATLVTVPEDQVVrkPASLSFEEACALPVVFLTVIDAFARAGLAKGEHILIQTAtGGTGL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 177 GAAAIAKADGAQVVVADTSPARREHVaTRLELP-VLDPSAEDFDAQLRAQFGGSLAQKVIDaTGNQHAMNNTVNLIRHGG 255
Cdd:cd08251  136 MAVQLARLKGAEIYATASSDDKLEYL-KQLGVPhVINYVEEDFEEEIMRLTGGRGVDVVIN-TLSGEAIQKGLNCLAPGG 213
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
12-273 2.33e-08

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: 54.68  E-value: 2.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFF---SYPRVLGHEICGEIVGLGKNIANLKNGQQVAVip 88
Cdd:cd08244   12 PEVLVPEDVPDPVPGPGQVRIAVAAAGVHFVDTQLRSGWGPGPfppELPYVPGGEVAGVVDAVGPGVDPAWLGRRVVA-- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  89 yvacqqcpacKSGRTNccekisvigvhqdGGFSEYLSVPVANILPA-DGIDPQAAALIepFAISAHAV---RRAAIAPGE 164
Cdd:cd08244   90 ----------HTGRAG-------------GGYAELAVADVDSLHPVpDGLDLEAAVAV--VHDGRTALgllDLATLTPGD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 165 QVLVVGA-GPIGLGAAAIAKADGAQVVVADTSPARREhVATRL--ELPVlDPSAEDFDAQLRAQFGGSLAQKVIDATGNQ 241
Cdd:cd08244  145 VVLVTAAaGGLGSLLVQLAKAAGATVVGAAGGPAKTA-LVRALgaDVAV-DYTRPDWPDQVREALGGGGVTVVLDGVGGA 222
                        250       260       270
                 ....*....|....*....|....*....|..
gi 446028188 242 HAmNNTVNLIRHGGTVVFVGLFKGELQFSDPE 273
Cdd:cd08244  223 IG-RAALALLAPGGRFLTYGWASGEWTALDED 253
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
18-239 3.69e-08

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: 54.13  E-value: 3.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  18 KQREIPIPGDNEALIKIKSVGICGTDIHA-WGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIpyvacqqcp 96
Cdd:cd08275   17 EKEALPEPSSGEVRVRVEACGLNFADLMArQGLYDSAPKPPFVPGFECAGTVEAVGEGVKDFKVGDRVMGL--------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  97 acksgrTNCcekisvigvhqdGGFSEYLSVPVANILP-ADGID-PQAAALIEPFAISAHAVRR-AAIAPGEQVLV-VGAG 172
Cdd:cd08275   88 ------TRF------------GGYAEVVNVPADQVFPlPDGMSfEEAAAFPVNYLTAYYALFElGNLRPGQSVLVhSAAG 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446028188 173 PIGLGAAAIAKADGAQVVVADTSPARREHVATRLELPVLDPSAEDFDAQLRAQFGGSLAQkVIDATG 239
Cdd:cd08275  150 GVGLAAGQLCKTVPNVTVVGTASASKHEALKENGVTHVIDYRTQDYVEEVKKISPEGVDI-VLDALG 215
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
18-265 2.32e-07

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 51.57  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  18 KQREIPIPGDNEALIKIKSVGICGTDIHAWGGNqpffsYP------RVLGHEICGEIVGLGKNIANLKNGQQVavipyva 91
Cdd:PTZ00354  19 GESPKPAPKRNDVLIKVSAAGVNRADTLQRQGK-----YPpppgssEILGLEVAGYVEDVGSDVKRFKEGDRV------- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  92 cqqcpacksgrtnccekisvIGVHQDGGFSEYLSVPVANILP-ADGID-PQAAALIEPFAISAHAVRR-AAIAPGEQVLV 168
Cdd:PTZ00354  87 --------------------MALLPGGGYAEYAVAHKGHVMHiPQGYTfEEAAAIPEAFLTAWQLLKKhGDVKKGQSVLI 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 169 -VGAGPIGLGAAAIAKADGAQVVVADTSPAR----REHVATRLelpVLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQHa 243
Cdd:PTZ00354 147 hAGASGVGTAAAQLAEKYGAATIITTSSEEKvdfcKKLAAIIL---IRYPDEEGFAPKVKKLTGEKGVNLVLDCVGGSY- 222
                        250       260
                 ....*....|....*....|..
gi 446028188 244 MNNTVNLIRHGGTVVFVGLFKG 265
Cdd:PTZ00354 223 LSETAEVLAVDGKWIVYGFMGG 244
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
28-177 1.07e-06

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: 49.49  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  28 NEALIKIKSVGICGTDIHAWGGNQPffSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIpyvacqqcpacksgrtncce 107
Cdd:cd05195    1 DEVEVEVKAAGLNFRDVLVALGLLP--GDETPLGLECSGIVTRVGSGVTGLKVGDRVMGL-------------------- 58
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446028188 108 kisvigvhQDGGFSEYLSVPVANI--LPADGIDPQAAALIEPFAISAHA-VRRAAIAPGEQVLVV-GAGPIGLG 177
Cdd:cd05195   59 --------APGAFATHVRVDARLVvkIPDSLSFEEAATLPVAYLTAYYAlVDLARLQKGESVLIHaAAGGVGQA 124
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
11-311 1.24e-06

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: 49.29  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  11 QPKELVWKQREIPIPGDNEALIKIKSVGICGTDIH---AWGGNqpffsypRVLGHEICGEIVGLGKNIANLKNGQQVavi 87
Cdd:cd08270   10 APLRLRLGEVPDPQPAPHEALVRVAAISLNRGELKfaaERPDG-------AVPGWDAAGVVERAAADGSGPAVGARV--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  88 pyvacqqcpacksgrtnccekisvIGVHQDGGFSEYLSVPVANILPA-DGIDPQAAALIEPFAISA-HAVRRAAIAPGEQ 165
Cdd:cd08270   80 ------------------------VGLGAMGAWAELVAVPTGWLAVLpDGVSFAQAATLPVAGVTAlRALRRGGPLLGRR 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 166 VLVVGA-GPIGLGAAAIAKADGAQVVVADTSPAR----REHVATRLELPVLDPSAEDFDAqlraqfggslaqkVIDATGN 240
Cdd:cd08270  136 VLVTGAsGGVGRFAVQLAALAGAHVVAVVGSPARaeglRELGAAEVVVGGSELSGAPVDL-------------VVDSVGG 202
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446028188 241 QhAMNNTVNLIRHGGTVVFVGLFKGELQ-------FSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMMLT 311
Cdd:cd08270  203 P-QLARALELLAPGGTVVSVGSSSGEPAvfnpaafVGGGGGRRLYTFFLYDGEPLAADLARLLGLVAAGRLDPRIGWR 279
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
11-143 6.51e-06

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: 47.21  E-value: 6.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  11 QPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGnqPFFS---YPRVLGHEICGEIVGLG-KNIANLKNGQQVAV 86
Cdd:cd08291   14 EVKELSLPEPEVPEPGPGEVLIKVEAAPINPSDLGFLKG--QYGStkaLPVPPGFEGSGTVVAAGgGPLAQSLIGKRVAF 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446028188  87 IpyvacqqcpacksgrtnccekisvigVHQDGGFSEYLSVPVANILP-ADGIDPQAAA 143
Cdd:cd08291   92 L--------------------------AGSYGTYAEYAVADAQQCLPlPDGVSFEQGA 123
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
17-272 7.94e-06

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: 47.15  E-value: 7.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  17 WKQREIPIP--GDNEALIKIKSVGICGTD-IHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPYvacq 93
Cdd:cd08276   15 LKLVEEPVPepGPGEVLVRVHAVSLNYRDlLILNGRYPPPVKDPLIPLSDGAGEVVAVGEGVTRFKVGDRVVPTFF---- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  94 qcPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILPA-DGIDPQAAALIEPFAISA-HAVR-RAAIAPGEQVLVVG 170
Cdd:cd08276   91 --PNWLDGPPTAEDEASALGGPIDGVLAEYVVLPEEGLVRApDHLSFEEAATLPCAGLTAwNALFgLGPLKPGDTVLVQG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 171 AGPIGLGAAAIAKADGAQVVVADTSPARRE--------HVATRLELPvldpsaeDFDAQLRAQFGGSLAQKVIDATGNQH 242
Cdd:cd08276  169 TGGVSLFALQFAKAAGARVIATSSSDEKLErakalgadHVINYRTTP-------DWGEEVLKLTGGRGVDHVVEVGGPGT 241
                        250       260       270
                 ....*....|....*....|....*....|
gi 446028188 243 aMNNTVNLIRHGGTVVFVGLFKGELQFSDP 272
Cdd:cd08276  242 -LAQSIKAVAPGGVISLIGFLSGFEAPVLL 270
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
112-262 4.29e-05

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


Pssm-ID: 274315 [Multi-domain]  Cd Length: 323  Bit Score: 44.86  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  112 IGVHQDGGFSEYLSVPVANILP-ADGIDP-QAAAL-IEPF--AISAHAVRRAAIAPGE-QVLVVGA-GPIG--------- 175
Cdd:TIGR02823  89 LGVSHDGGYSQYARVPADWLVPlPEGLSLrEAMALgTAGFtaALSVMALERNGLTPEDgPVLVTGAtGGVGslavailsk 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  176 LGAAaiakadgaqvVVADTspARREHVATRLEL---PVLDPsaEDFDAQLR----AQFGGslaqkVIDATGNqHAMNNTV 248
Cdd:TIGR02823 169 LGYE----------VVAST--GKAEEEDYLKELgasEVIDR--EDLSPPGKplekERWAG-----AVDTVGG-HTLANVL 228
                         170
                  ....*....|....
gi 446028188  249 NLIRHGGTVVFVGL 262
Cdd:TIGR02823 229 AQLKYGGAVAACGL 242
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
112-325 4.37e-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: 44.84  E-value: 4.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 112 IGVHQDGGFSEYLSVPVANILP-ADGIDPQAAALI--EPF--AISAHAVRRAAIAP--GEqVLVVGA-GPIG-------- 175
Cdd:cd05280   90 LGMNTDGGFAEYVRVPADWVVPlPEGLSLREAMILgtAGFtaALSVHRLEDNGQTPedGP-VLVTGAtGGVGsiavaila 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 176 -LGAAaiakadgaqvVVADTSpaRREHVATRLEL---PVLDPsaEDFDAQ-----LRAQFGGslaqkVIDATGNQHamnn 246
Cdd:cd05280  169 kLGYT----------VVALTG--KEEQADYLKSLgasEVLDR--EDLLDEskkplLKARWAG-----AIDTVGGDV---- 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 247 TVNLIRH---GGTVVFVGLFKGelqfsdPEFHkkeTTMM----------G--SRNATPEDFAKV-GRLMAEGKITADMML 310
Cdd:cd05280  226 LANLLKQtkyGGVVASCGNAAG------PELT---TTVLpfilrgvsllGidSVNCPMELRKQVwQKLATEWKPDLLEIV 296
                        250
                 ....*....|....*
gi 446028188 311 THRYPFATLAETYER 325
Cdd:cd05280  297 VREISLEELPEAIDR 311
ribitol-5-phosphate_DH cd08237
ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of ...
28-300 5.02e-05

ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of the MDR/zinc-dependent alcohol dehydrogenase-like family, oxidizes the phosphate ester of ribitol-5-phosphate to xylulose-5-phosphate of the pentose phosphate pathway. 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: 176199 [Multi-domain]  Cd Length: 341  Bit Score: 44.66  E-value: 5.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  28 NEALIKIKSVGICGTDIHAWGGNQPffsyPRVLG--------HEICGEIVGlgKNIANLKNGQQVAVIPYVACQQ----- 94
Cdd:cd08237   26 DWVIVRPTYLSICHADQRYYQGNRS----PEALKkklpmaliHEGIGVVVS--DPTGTYKVGTKVVMVPNTPVEKdeiip 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  95 ---CPA---CKSGrtnccekisvigvhQDGGFSEYLSVPVANI--LPADgIDPQAAALIEPFAISAHAVRR---AAIAPG 163
Cdd:cd08237  100 enyLPSsrfRSSG--------------YDGFMQDYVFLPPDRLvkLPDN-VDPEVAAFTELVSVGVHAISRfeqIAHKDR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 164 EQVLVVGAGPIG--LGAAAIAKADGAQVVVADTSPARREHVATRLELPVLDPSAED--FDAQLRAqFGGSlaqkvidatG 239
Cdd:cd08237  165 NVIGVWGDGNLGyiTALLLKQIYPESKLVVFGKHQEKLDLFSFADETYLIDDIPEDlaVDHAFEC-VGGR---------G 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446028188 240 NQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMA 300
Cdd:cd08237  235 SQSAINQIIDYIRPQGTIGLMGVSEYPVPINTRMVLEKGLTLVGSSRSTREDFERAVELLS 295
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
20-301 7.47e-05

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: 43.86  E-value: 7.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  20 REIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFF-SYPRVLGHEICGEIVGLGKNIANLKNGQQVAVIPyvacqqcpac 98
Cdd:cd08292   21 VPKPTPGAGEVLVRTTLSPIHNHDLWTIRGTYGYKpELPAIGGSEAVGVVDAVGEGVKGLQVGQRVAVAP---------- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  99 ksgrtnccekisvigVHqdGGFSEYLSVPVANILP-ADGIDPQAAALIEPFAISAHAVRRAAIAPGEQVLVVGAGPIGLG 177
Cdd:cd08292   91 ---------------VH--GTWAEYFVAPADGLVPlPDGISDEVAAQLIAMPLSALMLLDFLGVKPGQWLIQNAAGGAVG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188 178 AAAIAKADGAQVVVadTSPARREHVATRLE----LPVLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQhAMNNTVNLIRH 253
Cdd:cd08292  154 KLVAMLAAARGINV--INLVRRDAGVAELRalgiGPVVSTEQPGWQDKVREAAGGAPISVALDSVGGK-LAGELLSLLGE 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446028188 254 GGTVVFVGLFKGE-LQFSDPEFHKKETTMMG------SRNATPEDFAkvgRLMAE 301
Cdd:cd08292  231 GGTLVSFGSMSGEpMQISSGDLIFKQATVRGfwggrwSQEMSVEYRK---RMIAE 282
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
21-175 3.70e-04

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: 41.83  E-value: 3.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  21 EIPIP---GDNEALIKIKS-------VGICG----TDIHAWGGNQPFFSY----PRVLGHEICGEIVGLGKNIANLKNGQ 82
Cdd:cd08248   20 NARIPvirKPNQVLIKVHAasvnpidVLMRSgygrTLLNKKRKPQSCKYSgiefPLTLGRDCSGVVVDIGSGVKSFEIGD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  83 QVAVipyvacqqcpacksgrtnccekisVIGVHQDGGFSEYLSVPVANI--LPADGIDPQAAALiePF-------AISAH 153
Cdd:cd08248  100 EVWG------------------------AVPPWSQGTHAEYVVVPENEVskKPKNLSHEEAASL--PYagltawsALVNV 153
                        170       180
                 ....*....|....*....|...
gi 446028188 154 AVRRAAIAPGEQVLVVGA-GPIG 175
Cdd:cd08248  154 GGLNPKNAAGKRVLILGGsGGVG 176
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
13-84 5.51e-04

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: 41.48  E-value: 5.51e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446028188  13 KELVWKQREIPIP---GDNEALIKIKSVGICGTDIHAWGG-NQPFFSYPRVLGHEICGEIVGLGKNIAN-LKNGQQV 84
Cdd:cd08247   11 SPLTITTIKLPLPncyKDNEIVVKVHAAALNPVDLKLYNSyTFHFKVKEKGLGRDYSGVIVKVGSNVASeWKVGDEV 87
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
20-175 7.17e-03

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: 37.92  E-value: 7.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  20 REIPIP--GDNEALIKIKSVGICGTDIHAWGGNQPFF-SYPRVLGHEICGEIVGLGKNIANLKNGQQVavipYvacqqcp 96
Cdd:cd08272   18 REVPRPqpGPGQVLVRVHASGVNPLDTKIRRGGAAARpPLPAILGCDVAGVVEAVGEGVTRFRVGDEV----Y------- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  97 ACKSGrtnccekisvIGVHQdGGFSEYLSVPvANIL---PADGIDPQAAALiePFA-ISAHA--VRRAAIAPGEQVLVV- 169
Cdd:cd08272   87 GCAGG----------LGGLQ-GSLAEYAVVD-ARLLalkPANLSMREAAAL--PLVgITAWEglVDRAAVQAGQTVLIHg 152

                 ....*.
gi 446028188 170 GAGPIG 175
Cdd:cd08272  153 GAGGVG 158
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
12-88 8.84e-03

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: 37.58  E-value: 8.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  12 PKElVWKQREIPIP---GDNEALIKIKSVGICGTDIHAWGGNQPFF-----SYPRVLGHEICGEIVGLGKNIANLKNGQQ 83
Cdd:cd08290   12 PKE-VLQLESYEIPppgPPNEVLVKMLAAPINPADINQIQGVYPIKppttpEPPAVGGNEGVGEVVKVGSGVKSLKPGDW 90

                 ....*
gi 446028188  84 vaVIP 88
Cdd:cd08290   91 --VIP 93
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
55-171 8.88e-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: 37.69  E-value: 8.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446028188  55 SYPRVLGHEICGEIVGlgKNIANLKNGQQVAVIPYVacqqcpacksgrtnccekisvIGVHQDGGFSEYLSVPVANILP- 133
Cdd:cd08289   56 RYPFIPGIDLAGTVVE--SNDPRFKPGDEVIVTSYD---------------------LGVSHHGGYSEYARVPAEWVVPl 112
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446028188 134 ADGIDPQAAALIE----PFAISAHAVRRAAIAP-GEQVLVVGA 171
Cdd:cd08289  113 PKGLTLKEAMILGtagfTAALSIHRLEENGLTPeQGPVLVTGA 155
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH