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Conserved domains on  [gi|488471907|ref|WP_002515577|]
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MULTISPECIES: zinc-dependent dehydrogenase [Cutibacterium]

Protein Classification

zinc-dependent dehydrogenase( domain architecture ID 10169514)

zinc-dependent dehydrogenase from the medium-chain dehydrogenase/reductase (MDR) may catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 1-347 7.36e-172

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: 481.32  E-value: 7.36e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVGD 80
Cdd:cd08235    1 MKAAVLHGPNDVRLEEVPVPEPGPGEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGDGVTG-FKVGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  81 WVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPQVLKVDGLNRIPDDVDFDEASAAEPFACAINAQE 160
Cdd:cd08235   80 RVFVAPHVPCGECHYCLRGNENMCPNYKKFGNLYDGGFAEYVRVPAWAVKRGGVLKLPDNVSFEEAALVEPLACCINAQR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 161 QLGIEKGDFLVIFGAGPIGCMHTRIARGVHKvGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMELTNGRGADV 240
Cdd:cd08235  160 KAGIKPGDTVLVIGAGPIGLLHAMLAKASGA-RKVIVSDLNEFRLEF-AKKLGADYTIDAAEEDLVEKVRELTDGRGADV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 241 IITATPANITQEQALSMAARNGRISFFGGLPKTNpTITCDSNLIHYRQLHIHGANGSAPEHNKRALQYIASGQVPVKDLI 320
Cdd:cd08235  238 VIVATGSPEAQAQALELVRKGGRILFFGGLPKGS-TVNIDPNLIHYREITITGSYAASPEDYKEALELIASGKIDVKDLI 316

                        330       340
                 ....*....|....*....|....*..
gi 488471907 321 TRHVKLDDVMTVFDIVAKGEAIKVTVE 347
Cdd:cd08235  317 THRFPLEDIEEAFELAADGKSLKIVIT 343
 
Name Accession Description Interval E-value
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 1-347 7.36e-172

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: 481.32  E-value: 7.36e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVGD 80
Cdd:cd08235    1 MKAAVLHGPNDVRLEEVPVPEPGPGEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGDGVTG-FKVGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  81 WVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPQVLKVDGLNRIPDDVDFDEASAAEPFACAINAQE 160
Cdd:cd08235   80 RVFVAPHVPCGECHYCLRGNENMCPNYKKFGNLYDGGFAEYVRVPAWAVKRGGVLKLPDNVSFEEAALVEPLACCINAQR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 161 QLGIEKGDFLVIFGAGPIGCMHTRIARGVHKvGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMELTNGRGADV 240
Cdd:cd08235  160 KAGIKPGDTVLVIGAGPIGLLHAMLAKASGA-RKVIVSDLNEFRLEF-AKKLGADYTIDAAEEDLVEKVRELTDGRGADV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 241 IITATPANITQEQALSMAARNGRISFFGGLPKTNpTITCDSNLIHYRQLHIHGANGSAPEHNKRALQYIASGQVPVKDLI 320
Cdd:cd08235  238 VIVATGSPEAQAQALELVRKGGRILFFGGLPKGS-TVNIDPNLIHYREITITGSYAASPEDYKEALELIASGKIDVKDLI 316

                        330       340
                 ....*....|....*....|....*..
gi 488471907 321 TRHVKLDDVMTVFDIVAKGEAIKVTVE 347
Cdd:cd08235  317 THRFPLEDIEEAFELAADGKSLKIVIT 343
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 1-348 6.05e-125

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: 362.15  E-value: 6.05e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVGD 80
Cdd:COG1063    1 MKALVLHGPGDLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTG-LKVGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  81 WVQSIAAVPCGQCHECRKGWMQVCQNQTSVGY-QYDGGFAEYMIVPPqvlkvDGLNRIPDDVDFDEASAAEPFACAINAQ 159
Cdd:COG1063   80 RVVVEPNIPCGECRYCRRGRYNLCENLQFLGIaGRDGGFAEYVRVPA-----ANLVKVPDGLSDEAAALVEPLAVALHAV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 160 EQLGIEKGDFLVIFGAGPIGCMHTRIARgVHKVGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMELTNGRGAD 239
Cdd:COG1063  155 ERAGVKPGDTVLVIGAGPIGLLAALAAR-LAGAARVIVVDRNPERLEL-ARELGADAVVNPREEDLVEAVRELTGGRGAD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 240 VIITATPANITQEQALSMAARNGRISFFGGLPktnPTITCDSNLIHYRQLHIHGANGSAPEHNKRALQYIASGQVPVKDL 319
Cdd:COG1063  233 VVIEAVGAPAALEQALDLVRPGGTVVLVGVPG---GPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPL 309

                        330       340       350
                 ....*....|....*....|....*....|.
gi 488471907 320 ITRHVKLDDVMTVFDIVAKG--EAIKVTVEP 348
Cdd:COG1063  310 ITHRFPLDDAPEAFEAAADRadGAIKVVLDP 340
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 1-344 4.26e-61

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 198.90  E-value: 4.26e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPED-VRLEDVPEPECKPDEIKIKVRNCSTCGTDVKIlHN----GHQNITGVTTMGHEVAGEIVEIGSEVAGd 75
Cdd:PRK05396   1 MKALVKLKAEPgLWLTDVPVPEPGPNDVLIKVKKTAICGTDVHI-YNwdewAQKTIPVPMVVGHEFVGEVVEVGSEVTG- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  76 WKVGDWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPQvlkvdglN--RIPDDVDFDEASAAEPFA 153
Cdd:PRK05396  79 FKVGDRVSGEGHIVCGHCRNCRAGRRHLCRNTKGVGVNRPGAFAEYLVIPAF-------NvwKIPDDIPDDLAAIFDPFG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 154 CAINAQEQLGIEKGDFLvIFGAGPIGCMHTRIAR--GVHKVgtiVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVME 231
Cdd:PRK05396 152 NAVHTALSFDLVGEDVL-ITGAGPIGIMAAAVAKhvGARHV---VITDVNEYRLEL-ARKMGATRAVNVAKEDLRDVMAE 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 232 LTNGRGADVIITATPANITQEQALSMAARNGRISFFGGLPKtnpTITCDSNLIHYRQLHIHGANGsapehnkRAL----- 306
Cdd:PRK05396 227 LGMTEGFDVGLEMSGAPSAFRQMLDNMNHGGRIAMLGIPPG---DMAIDWNKVIFKGLTIKGIYG-------REMfetwy 296

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 488471907 307 ---QYIASGqVPVKDLITRHVKLDDVMTVFDIVAKGEAIKV 344
Cdd:PRK05396 297 kmsALLQSG-LDLSPIITHRFPIDDFQKGFEAMRSGQSGKV 336
tdh TIGR00692
L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme ...
 8-348 9.91e-53

L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme of threonine catabolism. Closely related proteins include sorbitol dehydrogenase, xylitol dehydrogenase, and benzyl alcohol dehydrogenase. Eukaryotic examples of this enzyme have been demonstrated experimentally but do not appear in database search results.E. coli His-90 modulates substrate specificity and is believed part of the active site. [Energy metabolism, Amino acids and amines]


Pssm-ID: 129775 [Multi-domain]  Cd Length: 340  Bit Score: 177.36  E-value: 9.91e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907    8 APEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHN---GHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVGDWVQS 84
Cdd:TIGR00692   7 PGYGAELTEVPVPEPGPGEVLIKVLATSICGTDVHIYNWdewAQSRIKPPQVVGHEVAGEVVGIGPGVEG-IKVGDYVSV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   85 IAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEASAAEPFACAINAQEQLGI 164
Cdd:TIGR00692  86 ETHIVCGKCYACRRGQYHVCQNTKIFGVDTDGCFAEYAVVP-----AQNIWKNPKSIPPEYATIQEPLGNAVHTVLAGPI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  165 EKGDFLVIfGAGPIGCMHTRIARGVhKVGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMELTNGRGADVIITA 244
Cdd:TIGR00692 161 SGKSVLVT-GAGPIGLMAIAVAKAS-GAYPVIVSDPNEYRLEL-AKKMGATYVVNPFKEDVVKEVADLTDGEGVDVFLEM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  245 TPANITQEQALSMAARNGRISFFgGLPKTNPTITCdSNLIHYRQLHIHGANGSAP-EHNKRALQYIASGQVPVKDLITRH 323
Cdd:TIGR00692 238 SGAPKALEQGLQAVTPGGRVSLL-GLPPGKVTIDF-TNKVIFKGLTIYGITGRHMfETWYTVSRLIQSGKLDLDPIITHK 315

                         330       340
                  ....*....|....*....|....*
gi 488471907  324 VKLDDVMTVFDIVAKGEAIKVTVEP 348
Cdd:TIGR00692 316 FKFDKFEKGFELMRSGQTGKVILSL 340
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 25-127 1.63e-29

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: 109.24  E-value: 1.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   25 DEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVGDWVQSIAAVPCGQCHECRKGWMQVC 104
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTG-LKVGDRVVVEPLIPCGKCEYCREGRYNLC 79

                          90       100
                  ....*....|....*....|...
gi 488471907  105 QNQTSVGYQYDGGFAEYMIVPPQ 127
Cdd:pfam08240  80 PNGRFLGYDRDGGFAEYVVVPER 102
 
Name Accession Description Interval E-value
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 1-347 7.36e-172

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: 481.32  E-value: 7.36e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVGD 80
Cdd:cd08235    1 MKAAVLHGPNDVRLEEVPVPEPGPGEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGDGVTG-FKVGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  81 WVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPQVLKVDGLNRIPDDVDFDEASAAEPFACAINAQE 160
Cdd:cd08235   80 RVFVAPHVPCGECHYCLRGNENMCPNYKKFGNLYDGGFAEYVRVPAWAVKRGGVLKLPDNVSFEEAALVEPLACCINAQR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 161 QLGIEKGDFLVIFGAGPIGCMHTRIARGVHKvGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMELTNGRGADV 240
Cdd:cd08235  160 KAGIKPGDTVLVIGAGPIGLLHAMLAKASGA-RKVIVSDLNEFRLEF-AKKLGADYTIDAAEEDLVEKVRELTDGRGADV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 241 IITATPANITQEQALSMAARNGRISFFGGLPKTNpTITCDSNLIHYRQLHIHGANGSAPEHNKRALQYIASGQVPVKDLI 320
Cdd:cd08235  238 VIVATGSPEAQAQALELVRKGGRILFFGGLPKGS-TVNIDPNLIHYREITITGSYAASPEDYKEALELIASGKIDVKDLI 316

                        330       340
                 ....*....|....*....|....*..
gi 488471907 321 TRHVKLDDVMTVFDIVAKGEAIKVTVE 347
Cdd:cd08235  317 THRFPLEDIEEAFELAADGKSLKIVIT 343
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 1-348 6.05e-125

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: 362.15  E-value: 6.05e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVGD 80
Cdd:COG1063    1 MKALVLHGPGDLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTG-LKVGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  81 WVQSIAAVPCGQCHECRKGWMQVCQNQTSVGY-QYDGGFAEYMIVPPqvlkvDGLNRIPDDVDFDEASAAEPFACAINAQ 159
Cdd:COG1063   80 RVVVEPNIPCGECRYCRRGRYNLCENLQFLGIaGRDGGFAEYVRVPA-----ANLVKVPDGLSDEAAALVEPLAVALHAV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 160 EQLGIEKGDFLVIFGAGPIGCMHTRIARgVHKVGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMELTNGRGAD 239
Cdd:COG1063  155 ERAGVKPGDTVLVIGAGPIGLLAALAAR-LAGAARVIVVDRNPERLEL-ARELGADAVVNPREEDLVEAVRELTGGRGAD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 240 VIITATPANITQEQALSMAARNGRISFFGGLPktnPTITCDSNLIHYRQLHIHGANGSAPEHNKRALQYIASGQVPVKDL 319
Cdd:COG1063  233 VVIEAVGAPAALEQALDLVRPGGTVVLVGVPG---GPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPL 309

                        330       340       350
                 ....*....|....*....|....*....|.
gi 488471907 320 ITRHVKLDDVMTVFDIVAKG--EAIKVTVEP 348
Cdd:COG1063  310 ITHRFPLDDAPEAFEAAADRadGAIKVVLDP 340
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 1-346 1.46e-86

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: 264.00  E-value: 1.46e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHnGHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVGD 80
Cdd:cd08234    1 MKALVYEGPGELEVEEVPVPEPGPDEVLIKVAACGICGTDLHIYE-GEFGAAPPLVPGHEFAGVVVAVGSKVTG-FKVGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  81 WVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEASAAEPFACAINAQE 160
Cdd:cd08234   79 RVAVDPNIYCGECFYCRRGRPNLCENLTAVGVTRNGGFAEYVVVP-----AKQVYKIPDNLSFEEAALAEPLSCAVHGLD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 161 QLGIEKGDFLVIFGAGPIGCMHTRIAR--GVHKVgtiVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKvmELTNGRGA 238
Cdd:cd08234  154 LLGIKPGDSVLVFGAGPIGLLLAQLLKlnGASRV---TVAEPNEEKLEL-AKKLGATETVDPSREDPEAQ--KEDNPYGF 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 239 DVIITATPANITQEQALSMAARNGRISFFgGLPKTNPTITCDSNLIHYRQLHIHGANgSAPEHNKRALQYIASGQVPVKD 318
Cdd:cd08234  228 DVVIEATGVPKTLEQAIEYARRGGTVLVF-GVYAPDARVSISPFEIFQKELTIIGSF-INPYTFPRAIALLESGKIDVKG 305

                        330       340
                 ....*....|....*....|....*...
gi 488471907 319 LITRHVKLDDVMTVFDIVAKGEAIKVTV 346
Cdd:cd08234  306 LVSHRLPLEEVPEALEGMRSGGALKVVV 333
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 1-344 7.40e-85

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: 260.24  E-value: 7.40e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGvTTMGHEVAGEIVEIGSEVAgDWKVGD 80
Cdd:cd08236    1 MKALVLTGPGDLRYEDIPKPEPGPGEVLVKVKACGICGSDIPRYLGTGAYHPP-LVLGHEFSGTVEEVGSGVD-DLAVGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  81 WVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEASAAEPFACAINAQE 160
Cdd:cd08236   79 RVAVNPLLPCGKCEYCKKGEYSLCSNYDYIGSRRDGAFAEYVSVP-----ARNLIKIPDHVDYEEAAMIEPAAVALHAVR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 161 QLGIEKGDFLVIFGAGPIGCMHTRIARgVHKVGTIVMIDINAERLAMsAAAVKPDITIDGSQEDvVAKVMELTNGRGADV 240
Cdd:cd08236  154 LAGITLGDTVVVIGAGTIGLLAIQWLK-ILGAKRVIAVDIDDEKLAV-ARELGADDTINPKEED-VEKVRELTEGRGADL 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 241 IITATPANITQEQALSMAARNGRISFFgGLPKTNPTITCDS-NLIHYRQLHIHG--ANGSAPEHNK---RALQYIASGQV 314
Cdd:cd08236  231 VIEAAGSPATIEQALALARPGGKVVLV-GIPYGDVTLSEEAfEKILRKELTIQGswNSYSAPFPGDewrTALDLLASGKI 309

                        330       340       350
                 ....*....|....*....|....*....|..
gi 488471907 315 PVKDLITRHVKLDDVMTVFDIVAKGE--AIKV 344
Cdd:cd08236  310 KVEPLITHRLPLEDGPAAFERLADREefSGKV 341
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 1-347 3.15e-78

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: 242.86  E-value: 3.15e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHnGHQ------NItgvttMGHEVAGEIVEIGSEVAG 74
Cdd:cd08261    1 MKALVCEKPGRLEVVDIPEPVPGAGEVLVRVKRVGICGSDLHIYH-GRNpfasypRI-----LGHELSGEVVEVGEGVAG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  75 dWKVGDWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPQVLKVdglnriPDDVDFDEASAAEPFAC 154
Cdd:cd08261   75 -LKVGDRVVVDPYISCGECYACRKGRPNCCENLQVLGVHRDGGFAEYIVVPADALLV------PEGLSLDQAALVEPLAI 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 155 AINAQEQLGIEKGDFLVIFGAGPIGCMHTRIARGVHkvGTIVMIDINAERLAmSAAAVKPDITIDGSQEDVVAKVMELTN 234
Cdd:cd08261  148 GAHAVRRAGVTAGDTVLVVGAGPIGLGVIQVAKARG--ARVIVVDIDDERLE-FARELGADDTINVGDEDVAARLRELTD 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 235 GRGADVIITATPANITQEQALSMAARNGRISFFgGLPKTNPTItcDSNLIHYRQLHIHGANGSAPEHNKRALQYIASGQV 314
Cdd:cd08261  225 GEGADVVIDATGNPASMEEAVELVAHGGRVVLV-GLSKGPVTF--PDPEFHKKELTILGSRNATREDFPDVIDLLESGKV 301

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 488471907 315 PVKDLITRHVKLDDVMTVFDIVAKGEA--IKVTVE 347
Cdd:cd08261  302 DPEALITHRFPFEDVPEAFDLWEAPPGgvIKVLIE 336
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 1-346 2.79e-77

(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: 240.91  E-value: 2.79e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVK--------ILHNGHQNITGVT---TMGHEVAGEIVEIG 69
Cdd:cd08233    1 MKAARYHGRKDIRVEEVPEPPVKPGEVKIKVAWCGICGSDLHeyldgpifIPTEGHPHLTGETapvTLGHEFSGVVVEVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  70 SEVAGdWKVGDWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQ-YDGGFAEYMIVPPQVLKvdglnRIPDDVDFDEASA 148
Cdd:cd08233   81 SGVTG-FKVGDRVVVEPTIKCGTCGACKRGLYNLCDSLGFIGLGgGGGGFAEYVVVPAYHVH-----KLPDNVPLEEAAL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 149 AEPFACAINAQEQLGIEKGDFLVIFGAGPIGcMHTRIARGVHKVGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAK 228
Cdd:cd08233  155 VEPLAVAWHAVRRSGFKPGDTALVLGAGPIG-LLTILALKAAGASKIIVSEPSEARREL-AEELGATIVLDPTEVDVVAE 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 229 VMELTNGRGADVIITATPANITQEQALSMAARNGR---ISFFGGLPKTNPtitcdsNLIHYRQLHIHGANGSAPEHNKRA 305
Cdd:cd08233  233 VRKLTGGGGVDVSFDCAGVQATLDTAIDALRPRGTavnVAIWEKPISFNP------NDLVLKEKTLTGSICYTREDFEEV 306

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 488471907 306 LQYIASGQVPVKDLITRHVKLDDVMTV-FD--IVAKGEAIKVTV 346
Cdd:cd08233  307 IDLLASGKIDAEPLITSRIPLEDIVEKgFEelINDKEQHVKILV 350
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 1-346 8.32e-76

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 236.55  E-value: 8.32e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAP-EDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVG 79
Cdd:COG1064    1 MKAAVLTEPgGPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGVTG-FKVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  80 DWVqsiaAVP----CGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPqvlkvDGLNRIPDDVDFDEASA-AEPFAC 154
Cdd:COG1064   80 DRV----GVGwvdsCGTCEYCRSGRENLCENGRFTGYTTDGGYAEYVVVPA-----RFLVKLPDGLDPAEAAPlLCAGIT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 155 AINAQEQLGIEKGDFLVIFGAGPIGCMHTRIAR--GVHkvgtIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMEL 232
Cdd:COG1064  151 AYRALRRAGVGPGDRVAVIGAGGLGHLAVQIAKalGAE----VIAVDRSPEKLEL-ARELGADHVVNSSDEDPVEAVREL 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 233 TngrGADVIITATPANITQEQALSMAARNGRISfFGGLPKTNPTItcDSNLIHYRQLHIHGANGSAPEHNKRALQYIASG 312
Cdd:COG1064  226 T---GADVVIDTVGAPATVNAALALLRRGGRLV-LVGLPGGPIPL--PPFDLILKERSIRGSLIGTRADLQEMLDLAAEG 299

                        330       340       350
                 ....*....|....*....|....*....|....
gi 488471907 313 QVpvkDLITRHVKLDDVMTVFDIVAKGEAIKVTV 346
Cdd:COG1064  300 KI---KPEVETIPLEEANEALERLRAGKVRGRAV 330
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
 1-344 1.33e-69

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: 221.13  E-value: 1.33e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHN-----GHQN----ITGVTTMGHEVAGEIVEIGSE 71
Cdd:cd08256    1 MRAVVCHGPQDYRLEEVPVPRPGPGEILVKVEACGICAGDIKCYHGapsfwGDENqppyVKPPMIPGHEFVGRVVELGEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  72 VA-GDWKVGDWVQSIAAVPCGQCHECRKG--WMqvCQNQTSVGYQ--YDGGFAEYMIVPPQVLkvdgLNRIPDDVDFDEA 146
Cdd:cd08256   81 AEeRGVKVGDRVISEQIVPCWNCRFCNRGqyWM--CQKHDLYGFQnnVNGGMAEYMRFPKEAI----VHKVPDDIPPEDA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 147 SAAEPFACAINAQEQLGIEKGDFLVIFGAGPIGCMHTRIARGVHKvGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVV 226
Cdd:cd08256  155 ILIEPLACALHAVDRANIKFDDVVVLAGAGPLGLGMIGAARLKNP-KKLIVLDLKDERLAL-ARKFGADVVLNPPEVDVV 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 227 AKVMELTNGRGADVIITATPANITQEQALSMAARNGRI---SFFGGLPKTNPTITCDSnlihyRQLHIHGANgSAPEHNK 303
Cdd:cd08256  233 EKIKELTGGYGCDIYIEATGHPSAVEQGLNMIRKLGRFvefSVFGDPVTVDWSIIGDR-----KELDVLGSH-LGPYCYP 306

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 488471907 304 RALQYIASGQVPVKDLITRHVKLDDVMTVFDIVAKGE-AIKV 344
Cdd:cd08256  307 IAIDLIASGRLPTDGIVTHQFPLEDFEEAFELMARGDdSIKV 348
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 1-312 1.16e-68

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: 217.57  E-value: 1.16e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPE--DVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAgDWKV 78
Cdd:cd08258    1 MKALVKTGPGpgNVELREVPEPEPGPGEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEVGPDVE-GWKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  79 GDWVQSIA-AVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEASAAEPFACAIN 157
Cdd:cd08258   80 GDRVVSETtFSTCGRCPYCRRGDYNLCPHRKGIGTQADGGFAEYVLVP-----EESLHELPENLSLEAAALTEPLAVAVH 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 158 A-QEQLGIEKGDFLVIFGAGPIGCMHTRIARgvHKVGTIVM--IDINAERLAMsAAAVKPDiTIDGSQEDVVAKVMELTN 234
Cdd:cd08258  155 AvAERSGIRPGDTVVVFGPGPIGLLAAQVAK--LQGATVVVvgTEKDEVRLDV-AKELGAD-AVNGGEEDLAELVNEITD 230

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488471907 235 GRGADVIITATPANITQEQALSMAARNGRISFFGGLPKTNPTItcDSNLIHYRQLHIHGANGSAPEHNKRALQYIASG 312
Cdd:cd08258  231 GDGADVVIECSGAVPALEQALELLRKGGRIVQVGIFGPLAASI--DVERIIQKELSVIGSRSSTPASWETALRLLASG 306
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 1-348 4.72e-66

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: 211.73  E-value: 4.72e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECK-PDEIKIKVRNCSTCGTDVKILHnGHQNITGVTTMGHEVAGEIVEIGSEVaGDWKVG 79
Cdd:cd08284    1 MKAVVFKGPGDVRVEEVPIPQIQdPTDAIVKVTAAAICGSDLHIYR-GHIPSTPGFVLGHEFVGEVVEVGPEV-RTLKVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  80 DWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQ----YDGGFAEYMIVPpqvlKVDG-LNRIPDDVDFDEA-----SAA 149
Cdd:cd08284   79 DRVVSPFTIACGECFYCRRGQSGRCAKGGLFGYAgspnLDGAQAEYVRVP----FADGtLLKLPDGLSDEAAlllgdILP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 150 EPFACAINAQEQlgieKGDFLVIFGAGPIGCMHTRIARgVHKVGTIVMIDINAERLAmsAAAVKPDITIDGSQEDVVAKV 229
Cdd:cd08284  155 TGYFGAKRAQVR----PGDTVAVIGCGPVGLCAVLSAQ-VLGAARVFAVDPVPERLE--RAAALGAEPINFEDAEPVERV 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 230 MELTNGRGADVIITATPANITQEQALSMAARNGRISFFGglPKTNPTITCDSNLIHYRQLHIHGANGSAPEHNKRALQYI 309
Cdd:cd08284  228 REATEGRGADVVLEAVGGAAALDLAFDLVRPGGVISSVG--VHTAEEFPFPGLDAYNKNLTLRFGRCPVRSLFPELLPLL 305

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 488471907 310 ASGQVPVKDLITRHVKLDDVMTVFDIVAKGEAIKVTVEP 348
Cdd:cd08284  306 ESGRLDLEFLIDHRMPLEEAPEAYRLFDKRKVLKVVLDP 344
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 1-348 2.28e-63

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: 204.78  E-value: 2.28e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPED-VRLEDVPEPECKPDEIKIKVRNCSTCGTDVKIlHN----GHQNITGVTTMGHEVAGEIVEIGSEVaGD 75
Cdd:cd05281    1 MKAIVKTKAGPgAELVEVPVPKPGPGEVLIKVLAASICGTDVHI-YEwdewAQSRIKPPLIFGHEFAGEVVEVGEGV-TR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  76 WKVGDWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPQVLKVDglnriPDDVDFDEASAAEPFACA 155
Cdd:cd05281   79 VKVGDYVSAETHIVCGKCYQCRTGNYHVCQNTKILGVDTDGCFAEYVVVPEENLWKN-----DKDIPPEIASIQEPLGNA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 156 INAQEQLGIeKGDFLVIFGAGPIGCMHTRIARgVHKVGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVaKVMELTNG 235
Cdd:cd05281  154 VHTVLAGDV-SGKSVLITGCGPIGLMAIAVAK-AAGASLVIASDPNPYRLEL-AKKMGADVVINPREEDVV-EVKSVTDG 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 236 RGADVIITATPANITQEQALSMAARNGRISFFgGLPKTNPTITCDsNLIHYRQLHIHGANGSAP-EHNKRALQYIASGQV 314
Cdd:cd05281  230 TGVDVVLEMSGNPKAIEQGLKALTPGGRVSIL-GLPPGPVDIDLN-NLVIFKGLTVQGITGRKMfETWYQVSALLKSGKV 307

                        330       340       350
                 ....*....|....*....|....*....|....
gi 488471907 315 PVKDLITRHVKLDDVMTVFDIVAKGEAIKVTVEP 348
Cdd:cd05281  308 DLSPVITHKLPLEDFEEAFELMRSGKCGKVVLYP 341
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 1-348 2.08e-62

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: 202.50  E-value: 2.08e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECK-PDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVaGDWKVG 79
Cdd:cd05278    1 MKALVYLGPGKIGLEEVPDPKIQgPHDAIVRVTATSICGSDLHIYRGGVPGAKHGMILGHEFVGEVVEVGSDV-KRLKPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  80 DWVQSIAAVPCGQCHECRKGWMQVCQNqTSV----GYQYDGGFAEYMIVPpqvlKVD-GLNRIPDDVDFDEASA-AEPFA 153
Cdd:cd05278   80 DRVSVPCITFCGRCRFCRRGYHAHCEN-GLWgwklGNRIDGGQAEYVRVP----YADmNLAKIPDGLPDEDALMlSDILP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 154 CAINAQEQLGIEKGDFLVIFGAGPIGCMHTRIARgVHKVGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMELT 233
Cdd:cd05278  155 TGFHGAELAGIKPGSTVAVIGAGPVGLCAVAGAR-LLGAARIIAVDSNPERLDL-AKEAGATDIINPKNGDIVEQILELT 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 234 NGRGADVIITATPANITQEQALSMAARNGRIS----FFGGLPKTNPTITCDSNlihyrqLHIHGANGSAPEHNKRALQYI 309
Cdd:cd05278  233 GGRGVDCVIEAVGFEETFEQAVKVVRPGGTIAnvgvYGKPDPLPLLGEWFGKN------LTFKTGLVPVRARMPELLDLI 306

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 488471907 310 ASGQVPVKDLITRHVKLDDVMTVFDIVAKGE--AIKVTVEP 348
Cdd:cd05278  307 EEGKIDPSKLITHRFPLDDILKAYRLFDNKPdgCIKVVIRP 347
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 1-344 4.26e-61

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 198.90  E-value: 4.26e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPED-VRLEDVPEPECKPDEIKIKVRNCSTCGTDVKIlHN----GHQNITGVTTMGHEVAGEIVEIGSEVAGd 75
Cdd:PRK05396   1 MKALVKLKAEPgLWLTDVPVPEPGPNDVLIKVKKTAICGTDVHI-YNwdewAQKTIPVPMVVGHEFVGEVVEVGSEVTG- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  76 WKVGDWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPQvlkvdglN--RIPDDVDFDEASAAEPFA 153
Cdd:PRK05396  79 FKVGDRVSGEGHIVCGHCRNCRAGRRHLCRNTKGVGVNRPGAFAEYLVIPAF-------NvwKIPDDIPDDLAAIFDPFG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 154 CAINAQEQLGIEKGDFLvIFGAGPIGCMHTRIAR--GVHKVgtiVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVME 231
Cdd:PRK05396 152 NAVHTALSFDLVGEDVL-ITGAGPIGIMAAAVAKhvGARHV---VITDVNEYRLEL-ARKMGATRAVNVAKEDLRDVMAE 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 232 LTNGRGADVIITATPANITQEQALSMAARNGRISFFGGLPKtnpTITCDSNLIHYRQLHIHGANGsapehnkRAL----- 306
Cdd:PRK05396 227 LGMTEGFDVGLEMSGAPSAFRQMLDNMNHGGRIAMLGIPPG---DMAIDWNKVIFKGLTIKGIYG-------REMfetwy 296

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 488471907 307 ---QYIASGqVPVKDLITRHVKLDDVMTVFDIVAKGEAIKV 344
Cdd:PRK05396 297 kmsALLQSG-LDLSPIITHRFPIDDFQKGFEAMRSGQSGKV 336
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 26-309 5.18e-61

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: 196.39  E-value: 5.18e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  26 EIKIKVRNCSTCGTDVKILHNGH-QNITGVTTMGHEVAGEIVEIGSEVAGdWKVGDWVQSIAAVPCGQCHECRKGwmqvC 104
Cdd:cd05188    1 EVLVRVEAAGLCGTDLHIRRGGYpPPPKLPLILGHEGAGVVVEVGPGVTG-VKVGDRVVVLPNLGCGTCELCREL----C 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 105 QNQTSVGYQYDGGFAEYMIVPPqvlkvDGLNRIPDDVDFDEASAA-EPFACAINAQEQLG-IEKGDFLVIFGAGPIGCMH 182
Cdd:cd05188   76 PGGGILGEGLDGGFAEYVVVPA-----DNLVPLPDGLSLEEAALLpEPLATAYHALRRAGvLKPGDTVLVLGAGGVGLLA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 183 TRIARgvHKVGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMeLTNGRGADVIITATPANITQEQALSMAARNG 262
Cdd:cd05188  151 AQLAK--AAGARVIVTDRSDEKLEL-AKELGADHVIDYKEEDLEEELR-LTGGGGADVVIDAVGGPETLAQALRLLRPGG 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 488471907 263 RISFFGGLPKTNPTItcDSNLIHYRQLHIHGANGSAPEHNKRALQYI 309
Cdd:cd05188  227 RIVVVGGTSGGPPLD--DLRRLLFKELTIIGSTGGTREDFEEALDLL 271
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 7-348 8.89e-61

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: 198.10  E-value: 8.89e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   7 HAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVT---TMGHEVAGEIVEIGSEVAgDWKVGDWVQ 83
Cdd:cd05285    5 HGPGDLRLEERPIPEPGPGEVLVRVRAVGICGSDVHYYKHGRIGDFVVKepmVLGHESAGTVVAVGSGVT-HLKVGDRVA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  84 SIAAVPCGQCHECRKGWMQVCQNQTSVGYQ-YDGGFAEYMIVPPqvlkvDGLNRIPDDVDFDEASAAEPFACAINAQEQL 162
Cdd:cd05285   84 IEPGVPCRTCEFCKSGRYNLCPDMRFAATPpVDGTLCRYVNHPA-----DFCHKLPDNVSLEEGALVEPLSVGVHACRRA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 163 GIEKGDFLVIFGAGPIGCMHTRIARGVHkVGTIVMIDINAERLAMsAAAVKPDITIDGSQED---VVAKVMELTNGRGAD 239
Cdd:cd05285  159 GVRPGDTVLVFGAGPIGLLTAAVAKAFG-ATKVVVTDIDPSRLEF-AKELGATHTVNVRTEDtpeSAEKIAELLGGKGPD 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 240 VIITATPANITQEQALSMAARNGRIsFFGGLPKTNPTItcDSNLIHYRQLHIHGANGSApehN--KRALQYIASGQVPVK 317
Cdd:cd05285  237 VVIECTGAESCIQTAIYATRPGGTV-VLVGMGKPEVTL--PLSAASLREIDIRGVFRYA---NtyPTAIELLASGKVDVK 310

                        330       340       350
                 ....*....|....*....|....*....|...
gi 488471907 318 DLITRHVKLDDVMTVFDIVAKG--EAIKVTVEP 348
Cdd:cd05285  311 PLITHRFPLEDAVEAFETAAKGkkGVIKVVIEG 343
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 1-348 9.01e-61

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: 198.24  E-value: 9.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPED--VRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVT-TMGHEVAGEIVEIGSEVAGdWK 77
Cdd:cd08254    1 MKAWRFHKGSKglLVLEEVPVPEPGPGEVLVKVKAAGVCHSDLHILDGGVPTLTKLPlTLGHEIAGTVVEVGAGVTN-FK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  78 VGDWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEASAA-----EPF 152
Cdd:cd08254   80 VGDRVAVPAVIPCGACALCRRGRGNLCLNQGMPGLGIDGGFAEYIVVP-----ARALVPVPDGVPFAQAAVAtdavlTPY 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 153 ACAINAQEqlgIEKGDFLVIFGAGPIGCMHTRIARGVHkvGTIVMIDINAERLAMSAA--AVKPDITIDGSQEDVVAKvm 230
Cdd:cd08254  155 HAVVRAGE---VKPGETVLVIGLGGLGLNAVQIAKAMG--AAVIAVDIKEEKLELAKElgADEVLNSLDDSPKDKKAA-- 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 231 elTNGRGADVIITATPANITQEQALSMAARNGRISFFGglpKTNPTITCDSNLIHYRQLHIHGANGSAPEHNKRALQYIA 310
Cdd:cd08254  228 --GLGGGFDVIFDFVGTQPTFEDAQKAVKPGGRIVVVG---LGRDKLTVDLSDLIARELRIIGSFGGTPEDLPEVLDLIA 302

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 488471907 311 SGQVpvkDLITRHVKLDDVMTVFDIVAKGEA-IKVTVEP 348
Cdd:cd08254  303 KGKL---DPQVETRPLDEIPEVLERLHKGKVkGRVVLVP 338
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 1-340 3.54e-56

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: 186.20  E-value: 3.54e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPED--VRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHN--GHQNITGVTTmGHEVAGEIVEIGSEVAGdW 76
Cdd:cd08297    1 MKAAVVEEFGEkpYEVKDVPVPEPGPGEVLVKLEASGVCHTDLHAALGdwPVKPKLPLIG-GHEGAGVVVAVGPGVSG-L 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  77 KVGD-----WVQSiaavPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPqvlkvDGLNRIPDDVDFDEASaaeP 151
Cdd:cd08297   79 KVGDrvgvkWLYD----ACGKCEYCRTGDETLCPNQKNSGYTVDGTFAEYAIADA-----RYVTPIPDGLSFEQAA---P 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 152 FACA----INAQEQLGIEKGDFLVIFGA-GPIGCMHTRIARGV-HKVgtiVMIDINAERLAMsAAAVKPDITIDGSQEDV 225
Cdd:cd08297  147 LLCAgvtvYKALKKAGLKPGDWVVISGAgGGLGHLGVQYAKAMgLRV---IAIDVGDEKLEL-AKELGADAFVDFKKSDD 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 226 VAKVMELTNGRGADVIITATPANITQEQALSMAARNGRISFFgGLPKtNPTITCDSNLIHYRQLHIHG-ANGSAPEHNKr 304
Cdd:cd08297  223 VEAVKELTGGGGAHAVVVTAVSAAAYEQALDYLRPGGTLVCV-GLPP-GGFIPLDPFDLVLRGITIVGsLVGTRQDLQE- 299

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 488471907 305 ALQYIASGQvpVKDLITRhVKLDDVMTVFDIVAKGE 340
Cdd:cd08297  300 ALEFAARGK--VKPHIQV-VPLEDLNEVFEKMEEGK 332
tdh TIGR00692
L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme ...
 8-348 9.91e-53

L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme of threonine catabolism. Closely related proteins include sorbitol dehydrogenase, xylitol dehydrogenase, and benzyl alcohol dehydrogenase. Eukaryotic examples of this enzyme have been demonstrated experimentally but do not appear in database search results.E. coli His-90 modulates substrate specificity and is believed part of the active site. [Energy metabolism, Amino acids and amines]


Pssm-ID: 129775 [Multi-domain]  Cd Length: 340  Bit Score: 177.36  E-value: 9.91e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907    8 APEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHN---GHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVGDWVQS 84
Cdd:TIGR00692   7 PGYGAELTEVPVPEPGPGEVLIKVLATSICGTDVHIYNWdewAQSRIKPPQVVGHEVAGEVVGIGPGVEG-IKVGDYVSV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   85 IAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEASAAEPFACAINAQEQLGI 164
Cdd:TIGR00692  86 ETHIVCGKCYACRRGQYHVCQNTKIFGVDTDGCFAEYAVVP-----AQNIWKNPKSIPPEYATIQEPLGNAVHTVLAGPI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  165 EKGDFLVIfGAGPIGCMHTRIARGVhKVGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMELTNGRGADVIITA 244
Cdd:TIGR00692 161 SGKSVLVT-GAGPIGLMAIAVAKAS-GAYPVIVSDPNEYRLEL-AKKMGATYVVNPFKEDVVKEVADLTDGEGVDVFLEM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  245 TPANITQEQALSMAARNGRISFFgGLPKTNPTITCdSNLIHYRQLHIHGANGSAP-EHNKRALQYIASGQVPVKDLITRH 323
Cdd:TIGR00692 238 SGAPKALEQGLQAVTPGGRVSLL-GLPPGKVTIDF-TNKVIFKGLTIYGITGRHMfETWYTVSRLIQSGKLDLDPIITHK 315

                         330       340
                  ....*....|....*....|....*
gi 488471907  324 VKLDDVMTVFDIVAKGEAIKVTVEP 348
Cdd:TIGR00692 316 FKFDKFEKGFELMRSGQTGKVILSL 340
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 1-348 1.16e-52

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: 177.13  E-value: 1.16e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNIT-GVTTMGHEVAGEIVEIGSEVAgDWKVG 79
Cdd:cd08239    1 MRGAVFPGDRTVELREFPVPVPGPGEVLLRVKASGLCGSDLHYYYHGHRAPAyQGVIPGHEPAGVVVAVGPGVT-HFRVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  80 DWVQSIAAVPCGQCHECRKGWMQVCQN-QTSVGYQYDGGFAEYMIVPPQVLKVdglnrIPDDVDFDEASA-AEPFACAIN 157
Cdd:cd08239   80 DRVMVYHYVGCGACRNCRRGWMQLCTSkRAAYGWNRDGGHAEYMLVPEKTLIP-----LPDDLSFADGALlLCGIGTAYH 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 158 AQEQLGIEKGDFLVIFGAGPIGCMHTRIAR--GVHKVgtIVMiDINAERLAMsAAAVKPDITIDgSQEDVVAKVMELTNG 235
Cdd:cd08239  155 ALRRVGVSGRDTVLVVGAGPVGLGALMLARalGAEDV--IGV-DPSPERLEL-AKALGADFVIN-SGQDDVQEIRELTSG 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 236 RGADVIITATPANITQEQALSMAARNGRISFFGGLPKtnPTITCDSNLIHyRQLHIHGANGSAPEHNKRALQYIASGQVP 315
Cdd:cd08239  230 AGADVAIECSGNTAARRLALEAVRPWGRLVLVGEGGE--LTIEVSNDLIR-KQRTLIGSWYFSVPDMEECAEFLARHKLE 306

                        330       340       350
                 ....*....|....*....|....*....|...
gi 488471907 316 VKDLITRHVKLDDVMTVFDIVAKGEAIKVTVEP 348
Cdd:cd08239  307 VDRLVTHRFGLDQAPEAYALFAQGESGKVVFVF 339
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 1-268 1.94e-52

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: 176.60  E-value: 1.94e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAP-EDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVT---TMGHEVAGEIVEIGSEVAGdW 76
Cdd:cd05284    1 MKAARLYEYgKPLRLEDVPVPEPGPGQVLVRVGGAGVCHSDLHVIDGVWGGILPYKlpfTLGHENAGWVEEVGSGVDG-L 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  77 KVGDWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVP-PQVLKVdglnriPDDVDFDEASaaePFACA 155
Cdd:cd05284   80 KEGDPVVVHPPWGCGTCRYCRRGEENYCENARFPGIGTDGGFAEYLLVPsRRLVKL------PRGLDPVEAA---PLADA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 156 -INA-----QEQLGIEKGDFLVIFGAGPIGCMHTRIARGVHKVgTIVMIDINAERLAMsAAAVKPDITIDGSqEDVVAKV 229
Cdd:cd05284  151 gLTAyhavkKALPYLDPGSTVVVIGVGGLGHIAVQILRALTPA-TVIAVDRSEEALKL-AERLGADHVLNAS-DDVVEEV 227

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 488471907 230 MELTNGRGADVIITATPANITQEQALSMAARNGRISFFG 268
Cdd:cd05284  228 RELTGGRGADAVIDFVGSDETLALAAKLLAKGGRYVIVG 266
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 2-348 1.01e-51

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: 175.14  E-value: 1.01e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   2 KALRFHAP-EDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHnGHQNITGV-TTMGHEVAGEIVEIGSEVAGDW--- 76
Cdd:cd08231    2 RAAVLTGPgKPLEIREVPLPDLEPGAVLVRVRLAGVCGSDVHTVA-GRRPRVPLpIILGHEGVGRVVALGGGVTTDVage 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  77 --KVGDWVQSIAAVPCGQCHECRKGWMQVCQNQTSVG----YQYD---GGFAEYMIVPPQVLKVdglnRIPDDVDFDEAS 147
Cdd:cd08231   81 plKVGDRVTWSVGAPCGRCYRCLVGDPTKCENRKKYGheasCDDPhlsGGYAEHIYLPPGTAIV----RVPDNVPDEVAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 148 AA-EPFACAINAQEQLG-IEKGDFLVIFGAGPIGCMHTRIA--RGVHKVgtiVMIDINAERLAMsAAAVKPDITIDG--- 220
Cdd:cd08231  157 PAnCALATVLAALDRAGpVGAGDTVVVQGAGPLGLYAVAAAklAGARRV---IVIDGSPERLEL-AREFGADATIDIdel 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 221 SQEDVVAKVMELTNGRGADVIITATPANITQEQALSMAARNGRISfFGGLPKTNPTITCDSNLIHYRQLHIHGANGSAPE 300
Cdd:cd08231  233 PDPQRRAIVRDITGGRGADVVIEASGHPAAVPEGLELLRRGGTYV-LVGSVAPAGTVPLDPERIVRKNLTIIGVHNYDPS 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 488471907 301 HNKRALQYIA--SGQVPVKDLITRHVKLDDVMTVFDIVAKGEAIKVTVEP 348
Cdd:cd08231  312 HLYRAVRFLErtQDRFPFAELVTHRYPLEDINEALELAESGTALKVVIDP 361
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-340 3.67e-47

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: 163.31  E-value: 3.67e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPE-DVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILhNGHQNITGVTTMGHEVAGEIVEIGSEVAGDW--K 77
Cdd:cd08263    1 MKAAVLKGPNpPLTIEEIPVPRPKEGEILIRVAACGVCHSDLHVL-KGELPFPPPFVLGHEISGEVVEVGPNVENPYglS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  78 VGDWVQSIAAVPCGQCHECRKGWMQVCQ----NQTSVGYQYD------------------GGFAEYMIVPpqvlkVDGLN 135
Cdd:cd08263   80 VGDRVVGSFIMPCGKCRYCARGKENLCEdffaYNRLKGTLYDgttrlfrldggpvymysmGGLAEYAVVP-----ATALA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 136 RIPDDVDFDEASaaePFACAI----NAQEQLG-IEKGDFLVIFGAGPIGCMHTRIARGVhKVGTIVMIDINAERLAMsAA 210
Cdd:cd08263  155 PLPESLDYTESA---VLGCAGftayGALKHAAdVRPGETVAVIGVGGVGSSAIQLAKAF-GASPIIAVDVRDEKLAK-AK 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 211 AVKPDITIDGSQEDVVAKVMELTNGRGADVIITATPANITQEQALSMAARNGRISFFgGLPKTNPTITCDSNLIHYRQLH 290
Cdd:cd08263  230 ELGATHTVNAAKEDAVAAIREITGGRGVDVVVEALGKPETFKLALDVVRDGGRAVVV-GLAPGGATAEIPITRLVRRGIK 308

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488471907 291 IHGANGSAPEHN-KRALQYIASGQVPVKDLITRHVKLDDVMTVFDIVAKGE 340
Cdd:cd08263  309 IIGSYGARPRQDlPELVGLAASGKLDPEALVTHKYKLEEINEAYENLRKGL 359
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 11-346 6.02e-47

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: 163.45  E-value: 6.02e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  11 DVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILH---NGHQNITGVT----TMGHEVAGEIVEIGSEVAgDWKVGDWVQ 83
Cdd:cd08265   38 ELRVEDVPVPNLKPDEILIRVKACGICGSDIHLYEtdkDGYILYPGLTefpvVIGHEFSGVVEKTGKNVK-NFEKGDPVT 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  84 SIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPQVL-KVDGL-NRIPDDVDFDEASAAEPFACAINA--Q 159
Cdd:cd08265  117 AEEMMWCGMCRACRSGSPNHCKNLKELGFSADGAFAEYIAVNARYAwEINELrEIYSEDKAFEAGALVEPTSVAYNGlfI 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 160 EQLGIEKGDFLVIFGAGPIGCMHTRIARgVHKVGTIVMIDINAERLAMsAAAVKPDITIDGSQE---DVVAKVMELTNGR 236
Cdd:cd08265  197 RGGGFRPGAYVVVYGAGPIGLAAIALAK-AAGASKVIAFEISEERRNL-AKEMGADYVFNPTKMrdcLSGEKVMEVTKGW 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 237 GADVIITAT---PANITQEQAlSMAArNGRISFFGglpKTNPTITCDSNLIHYRQLHIHGANGSAPEHN-KRALQYIASG 312
Cdd:cd08265  275 GADIQVEAAgapPATIPQMEK-SIAI-NGKIVYIG---RAATTVPLHLEVLQVRRAQIVGAQGHSGHGIfPSVIKLMASG 349

                        330       340       350
                 ....*....|....*....|....*....|....
gi 488471907 313 QVPVKDLITRHVKLDDVMTVFDIVAKGEAIKVTV 346
Cdd:cd08265  350 KIDMTKIITARFPLEGIMEAIKAASERTDGKITI 383
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 1-348 6.10e-47

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: 163.48  E-value: 6.10e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPEC-KPDEIKIKVRNCSTCGTDvkiLHNGHQNITGV---TTMGHEVAGEIVEIGSEVaGDW 76
Cdd:cd08283    1 MKALVWHGKGDVRVEEVPDPKIeDPTDAIVRVTATAICGSD---LHLYHGYIPGMkkgDILGHEFMGVVEEVGPEV-RNL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  77 KVGDWVQSIAAVPCGQCHECRKGWMQVCQN-----------QTSV----GYQ-----YDGGFAEYMIVPpqvlKVD-GLN 135
Cdd:cd08283   77 KVGDRVVVPFTIACGECFYCKRGLYSQCDNtnpsaemaklyGHAGagifGYShltggYAGGQAEYVRVP----FADvGPF 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 136 RIPDDVDFDEAS-AAEPFACAINAQEQLGIEKGDFLVIFGAGPIGCMHTRIARgVHKVGTIVMIDINAERLAMsAAAVKP 214
Cdd:cd08283  153 KIPDDLSDEKALfLSDILPTGYHAAELAEVKPGDTVAVWGCGPVGLFAARSAK-LLGAERVIAIDRVPERLEM-ARSHLG 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 215 DITIDGSQED-VVAKVMELTNGRGADVIITA---------------------TPANITQEQALSMAARNGRISF---FGG 269
Cdd:cd08283  231 AETINFEEVDdVVEALRELTGGRGPDVCIDAvgmeahgsplhkaeqallkleTDRPDALREAIQAVRKGGTVSIigvYGG 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 270 LPKTNPTitcdsNLIHYRQLHIHGANGSAPEHNKRALQYIASGQVPVKDLITRHVKLDDVMTVFDIVAKGE--AIKVTVE 347
Cdd:cd08283  311 TVNKFPI-----GAAMNKGLTLRMGQTHVQRYLPRLLELIESGELDPSFIITHRLPLEDAPEAYKIFDKKEdgCIKVVLK 385


                 .
gi 488471907 348 P 348
Cdd:cd08283  386 P 386
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-329 1.11e-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: 161.62  E-value: 1.11e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHA-PEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVG 79
Cdd:cd08260    1 MRAAVYEEfGEPLEIREVPDPEPPPDGVVVEVEACGVCRSDWHGWQGHDPDVTLPHVPGHEFAGVVVEVGEDVSR-WRVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  80 DWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPQVLKvdgLNRIPDDVDFDEASAAE-PFACAINA 158
Cdd:cd08260   80 DRVTVPFVLGCGTCPYCRAGDSNVCEHQVQPGFTHPGSFAEYVAVPRADVN---LVRLPDDVDFVTAAGLGcRFATAFRA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 159 -QEQLGIEKGDFLVIFGAGPIG--CMHTRIARGvhkvGTIVMIDINAERLAMsAAAVKPDITIDGSQ-EDVVAKVMELTN 234
Cdd:cd08260  157 lVHQARVKPGEWVAVHGCGGVGlsAVMIASALG----ARVIAVDIDDDKLEL-ARELGAVATVNASEvEDVAAAVRDLTG 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 235 GrGADVIITATPANITQEQALSMAARNGRISFFGGLPKTNPTITCDSNLIHYRQLHIHGANGSAPEHNKRALQYIASGQV 314
Cdd:cd08260  232 G-GAHVSVDALGIPETCRNSVASLRKRGRHVQVGLTLGEEAGVALPMDRVVARELEIVGSHGMPAHRYDAMLALIASGKL 310

                        330
                 ....*....|....*
gi 488471907 315 PVKDLITRHVKLDDV 329
Cdd:cd08260  311 DPEPLVGRTISLDEA 325
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 4-344 9.60e-45

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: 156.24  E-value: 9.60e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   4 LRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDvkiLHNGHQNITGVTTM------GHEVAGEIVEIGSEVAGdWK 77
Cdd:cd08232    1 CVIHAAGDLRVEERPAPEPGPGEVRVRVAAGGICGSD---LHYYQHGGFGTVRLrepmvlGHEVSGVVEAVGPGVTG-LA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  78 VGDWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGY-----QYDGGFAEYMIVPPqvlkvDGLNRIPDDVDFDEASAAEPF 152
Cdd:cd08232   77 PGQRVAVNPSRPCGTCDYCRAGRPNLCLNMRFLGSamrfpHVQGGFREYLVVDA-----SQCVPLPDGLSLRRAALAEPL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 153 ACAINAQEQLGIEKGDFLVIFGAGPIGCMHTRIARgVHKVGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAkvmeL 232
Cdd:cd08232  152 AVALHAVNRAGDLAGKRVLVTGAGPIGALVVAAAR-RAGAAEIVATDLADAPLAV-ARAMGADETVNLARDPLAA----Y 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 233 TNGRGA-DVIITATPANITQEQALSMAARNGRISFFGGLPktnPTITCDSNLIHYRQLHIHGANGSAPEHNKrALQYIAS 311
Cdd:cd08232  226 AADKGDfDVVFEASGAPAALASALRVVRPGGTVVQVGMLG---GPVPLPLNALVAKELDLRGSFRFDDEFAE-AVRLLAA 301

                        330       340       350
                 ....*....|....*....|....*....|....
gi 488471907 312 GQVPVKDLITRHVKLDDVMTVFDIVA-KGEAIKV 344
Cdd:cd08232  302 GRIDVRPLITAVFPLEEAAEAFALAAdRTRSVKV 335
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 1-347 2.55e-44

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: 155.16  E-value: 2.55e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHApEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGV-----------TTMGHEVAGEIVEIG 69
Cdd:cd08262    1 MRAAVFRD-GPLVVRDVPDPEPGPGQVLVKVLACGICGSDLHATAHPEAMVDDAggpslmdlgadIVLGHEFCGEVVDYG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  70 SEVAGDWKVGDWVQSIAAVPCGQCHECRKGWMqvcqNQTSvgyqydGGFAEYMIVPPQVLKvdglnRIPDDVDFDEASAA 149
Cdd:cd08262   80 PGTERKLKVGTRVTSLPLLLCGQGASCGIGLS----PEAP------GGYAEYMLLSEALLL-----RVPDGLSMEDAALT 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 150 EPFACAINAQEQLGIEKGDFLVIFGAGPIG----CMHTRiaRGVHkvgTIVMIDINAERLAMsAAAVKPDITIDGSQEDV 225
Cdd:cd08262  145 EPLAVGLHAVRRARLTPGEVALVIGCGPIGlaviAALKA--RGVG---PIVASDFSPERRAL-ALAMGADIVVDPAADSP 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 226 VAKVMELTNGRG---ADVIITATPANITQEQALSMAARNGRISFFGGLPKTNPTITCDSNLihyRQLHIHGANGSAPEHN 302
Cdd:cd08262  219 FAAWAAELARAGgpkPAVIFECVGAPGLIQQIIEGAPPGGRIVVVGVCMESDNIEPALAIR---KELTLQFSLGYTPEEF 295

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 488471907 303 KRALQYIASGQVPVKDLITRHVKLDDVMTVFDIVAKGEA-IKVTVE 347
Cdd:cd08262  296 ADALDALAEGKVDVAPMVTGTVGLDGVPDAFEALRDPEHhCKILVD 341
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 2-341 5.31e-44

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: 154.02  E-value: 5.31e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   2 KALRFHAPED-VRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVGD 80
Cdd:cd08245    1 KAAVVHAAGGpLEPEEVPVPEPGPGEVLIKIEACGVCHTDLHAAEGDWGGSKYPLVPGHEIVGEVVEVGAGVEG-RKVGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  81 -----WVQSiaavPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPQvlkvdGLNRIPDDVDFDEASaaePFACA 155
Cdd:cd08245   80 rvgvgWLVG----SCGRCEYCRRGLENLCQKAVNTGYTTQGGYAEYMVADAE-----YTVLLPDGLPLAQAA---PLLCA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 156 ----INAQEQLGIEKGDFLVIFGAGPIGCMHTRIARGVHKVGTIVMIDINAERLAMSAAAvkpDITIDGSQEDvvakVME 231
Cdd:cd08245  148 gitvYSALRDAGPRPGERVAVLGIGGLGHLAVQYARAMGFETVAITRSPDKRELARKLGA---DEVVDSGAEL----DEQ 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 232 LTNGrGADVIITATPANITQEQALSMAARNGRISFFgGLPKTNPTITCDSNLIHYRQlHIHGANGSAPEHNKRALQYIAS 311
Cdd:cd08245  221 AAAG-GADVILVTVVSGAAAEAALGGLRRGGRIVLV-GLPESPPFSPDIFPLIMKRQ-SIAGSTHGGRADLQEALDFAAE 297

                        330       340       350
                 ....*....|....*....|....*....|
gi 488471907 312 GQVPVkdlITRHVKLDDVMTVFDIVAKGEA 341
Cdd:cd08245  298 GKVKP---MIETFPLDQANEAYERMEKGDV 324
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 1-348 2.36e-43

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: 153.17  E-value: 2.36e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAgDWKVGD 80
Cdd:cd08285    1 MKAFAMLGIGKVGWIEKPIPVCGPNDAIVRPTAVAPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGSEVK-DFKPGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  81 WVQSIAAVPCGQCHECRKGWMQVCQNQTSvGYQY----DGGFAEYMIVPpqvlKVDG-LNRIPDDVDFDEAS-AAEPFAC 154
Cdd:cd08285   80 RVIVPAITPDWRSVAAQRGYPSQSGGMLG-GWKFsnfkDGVFAEYFHVN----DADAnLAPLPDGLTDEQAVmLPDMMST 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 155 AINAQEQLGIEKGDFLVIFGAGPIGCMHTRIARgVHKVGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMELTN 234
Cdd:cd08285  155 GFHGAELANIKLGDTVAVFGIGPVGLMAVAGAR-LRGAGRIIAVGSRPNRVEL-AKEYGATDIVDYKNGDVVEQILKLTG 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 235 GRGADVIITATPANITQEQALSMAARNGRIS----FFGGLPKTNPTITCDSNLIHYRqlhIHGA---NGSapEHNKRALQ 307
Cdd:cd08285  233 GKGVDAVIIAGGGQDTFEQALKVLKPGGTISnvnyYGEDDYLPIPREEWGVGMGHKT---INGGlcpGGR--LRMERLAS 307

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 488471907 308 YIASGQV-PVKDLITRHVKLDDVMTVFDIVAKGEA--IKVTVEP 348
Cdd:cd08285  308 LIEYGRVdPSKLLTHHFFGFDDIEEALMLMKDKPDdlIKPVIIF 351
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-342 1.54e-41

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: 147.85  E-value: 1.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAP-EDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAgDWKVG 79
Cdd:cd08259    1 MKAAILHKPnKPLQIEEVPDPEPGPGEVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVGEGVE-RFKPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  80 DWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEASAAE-PFACAINA 158
Cdd:cd08259   80 DRVILYYYIPCGKCEYCLSGEENLCRNRAEYGEEVDGGFAEYVKVP-----ERSLVKLPDNVSDESAALAAcVVGTAVHA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 159 QEQLGIEKGDFLVIFGAGPigcmhtriARGVHKV-------GTIVMIDINAERLAMsAAAVKPDITIDGSQ--EDVVAKV 229
Cdd:cd08259  155 LKRAGVKKGDTVLVTGAGG--------GVGIHAIqlakalgARVIAVTRSPEKLKI-LKELGADYVIDGSKfsEDVKKLG 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 230 meltngrGADVIITATPANiTQEQALSMAARNGRISFFGglpKTNPT-ITCDSNLIHYRQLHIHGANGSAPEHNKRALQY 308
Cdd:cd08259  226 -------GADVVIELVGSP-TIEESLRSLNKGGRLVLIG---NVTPDpAPLRPGLLILKEIRIIGSISATKADVEEALKL 294

                        330       340       350
                 ....*....|....*....|....*....|....
gi 488471907 309 IASGQvpVKDLITRHVKLDDVMTVFDIVAKGEAI 342
Cdd:cd08259  295 VKEGK--IKPVIDRVVSLEDINEALEDLKSGKVV 326
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 1-348 3.23e-41

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: 147.02  E-value: 3.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHA---PEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKilhnGHQNITGVT-----TMGHEVAGEIVEIGSEV 72
Cdd:cd08266    1 MKAVVIRGhggPEVLEYGDLPEPEPGPDEVLVRVKAAALNHLDLW----VRRGMPGIKlplphILGSDGAGVVEAVGPGV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  73 AgDWKVGDWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEASAAeP- 151
Cdd:cd08266   77 T-NVKPGQRVVIYPGISCGRCEYCLAGRENLCAQYGILGEHVDGGYAEYVAVP-----ARNLLPIPDNLSFEEAAAA-Pl 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 152 -FACAINA-QEQLGIEKGDFLVIFGAGP-IGCMHTRIARgvHKVGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAK 228
Cdd:cd08266  150 tFLTAWHMlVTRARLRPGETVLVHGAGSgVGSAAIQIAK--LFGATVIATAGSEDKLER-AKELGADYVIDYRKEDFVRE 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 229 VMELTNGRGADVIITATPANiTQEQALSMAARNGRISFFGGlpKTNPTITCDSNLIHYRQLHIHGANGSAPEHNKRALQY 308
Cdd:cd08266  227 VRELTGKRGVDVVVEHVGAA-TWEKSLKSLARGGRLVTCGA--TTGYEAPIDLRHVFWRQLSILGSTMGTKAELDEALRL 303

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 488471907 309 IASGQvpVKDLITRHVKLDDVMTVFDIVAKGEAI-KVTVEP 348
Cdd:cd08266  304 VFRGK--LKPVIDSVFPLEEAAEAHRRLESREQFgKIVLTP 342
sorbose_phosphate_red cd08238
L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, ...
 2-324 5.40e-41

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: 148.36  E-value: 5.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   2 KALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNG--HQNI-----TGVTTMGHEVAGEIVEIGSEVAG 74
Cdd:cd08238    4 KAWRMYGKGDLRLEKFELPEIADDEILVRVISDSLCFSTWKLALQGsdHKKVpndlaKEPVILGHEFAGTILKVGKKWQG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  75 DWKVGdwvQSIAAVPCGQchecrkgwMQVCQNQTSVGYQYDGGFAEYMIVPPQVLKVDGLnRIPDDVDFDEASAAEPFAC 154
Cdd:cd08238   84 KYKPG---QRFVIQPALI--------LPDGPSCPGYSYTYPGGLATYHIIPNEVMEQDCL-LIYEGDGYAEASLVEPLSC 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 155 AINAQEQ------------LGIEKGDFLVIFG-AGPIGCMHTRIA-RGVHKVGTIVMIDINAERLAMSAAAVKPD----- 215
Cdd:cd08238  152 VIGAYTAnyhlqpgeyrhrMGIKPGGNTAILGgAGPMGLMAIDYAiHGPIGPSLLVVTDVNDERLARAQRLFPPEaasrg 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 216 ---ITIDGSQED-VVAKVMELTNGRGADVIITATPANITQEQALSMAARNGRISFFGGlpKTNPTITCDSNL--IHYRQL 289
Cdd:cd08238  232 ielLYVNPATIDdLHATLMELTGGQGFDDVFVFVPVPELVEEADTLLAPDGCLNFFAG--PVDKNFSAPLNFynVHYNNT 309

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 488471907 290 HIHGANGSAPEHNKRALQYIASGQVPVKDLITrHV 324
Cdd:cd08238  310 HYVGTSGGNTDDMKEAIDLMAAGKLNPARMVT-HI 343
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 1-348 2.19e-39

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: 141.82  E-value: 2.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHA---PEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGV-TTMGHEVAGEIVEIGSEVAGdW 76
Cdd:COG0604    1 MKAIVITEfggPEVLELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPLPPGLpFIPGSDAAGVVVAVGEGVTG-F 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  77 KVGDWVqsiaavpcgqchecrkgwmqvcqnqtsVGYQYDGGFAEYMIVPPqvlkvDGLNRIPDDVDFDEASAA-EPFACA 155
Cdd:COG0604   80 KVGDRV---------------------------AGLGRGGGYAEYVVVPA-----DQLVPLPDGLSFEEAAALpLAGLTA 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 156 INA-QEQLGIEKGDFLVIFGA-GPIGCMHTRIAR--GVHKVGTiVMIDINAERL-AMSAAAVkpditIDGSQEDVVAKVM 230
Cdd:COG0604  128 WQAlFDRGRLKPGETVLVHGAaGGVGSAAVQLAKalGARVIAT-ASSPEKAELLrALGADHV-----IDYREEDFAERVR 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 231 ELTNGRGADVIITATPANiTQEQALSMAARNGRISFFGGLPKTNPTItcDSNLIHYRQLHIHGANGSA--PEHNKRALQ- 307
Cdd:COG0604  202 ALTGGRGVDVVLDTVGGD-TLARSLRALAPGGRLVSIGAASGAPPPL--DLAPLLLKGLTLTGFTLFArdPAERRAALAe 278

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 488471907 308 ---YIASGQVPVkdLITRHVKLDDVMTVFDIVAKGEAI-KVTVEP 348
Cdd:COG0604  279 larLLAAGKLRP--VIDRVFPLEEAAEAHRLLESGKHRgKVVLTV 321
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 1-347 6.36e-39

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: 141.52  E-value: 6.36e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAP-EDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHnGHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVG 79
Cdd:cd08279    1 MRAAVLHEVgKPLEIEEVELDDPGPGEVLVRIAAAGLCHSDLHVVT-GDLPAPLPAVLGHEGAGVVEEVGPGVTG-VKPG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  80 DWVQSIAAVPCGQCHECRKGWMQVCQN--QTSVGYQYD------------------GGFAEYMIVPP-QVLKvdglnrIP 138
Cdd:cd08279   79 DHVVLSWIPACGTCRYCSRGQPNLCDLgaGILGGQLPDgtrrftadgepvgamcglGTFAEYTVVPEaSVVK------ID 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 139 DDVDFDEASAaepFAC--------AINAQeqlGIEKGDFLVIFGAGPIGcMHT----RIARGvhkvGTIVMIDINAERLA 206
Cdd:cd08279  153 DDIPLDRAAL---LGCgvttgvgaVVNTA---RVRPGDTVAVIGCGGVG-LNAiqgaRIAGA----SRIIAVDPVPEKLE 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 207 MsAAAVKPDITIDGSQEDVVAKVMELTNGRGADVIITATPANITQEQALSMAARNGRISFFgGLPKTNPTITCDSNLIHY 286
Cdd:cd08279  222 L-ARRFGATHTVNASEDDAVEAVRDLTDGRGADYAFEAVGRAATIRQALAMTRKGGTAVVV-GMGPPGETVSLPALELFL 299

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488471907 287 RQLHIHGAN-GSA-PEHN-KRALQYIASGQVPVKDLITRHVKLDDVMTVFDIVAKGEAIKVTVE 347
Cdd:cd08279  300 SEKRLQGSLyGSAnPRRDiPRLLDLYRAGRLKLDELVTRRYSLDEINEAFADMLAGENARGVIV 363
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 1-347 1.84e-38

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: 140.08  E-value: 1.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECK-PDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVG 79
Cdd:cd08286    1 MKALVYHGPGKISWEDRPKPTIQePTDAIVKMLKTTICGTDLHILKGDVPTVTPGRILGHEGVGVVEEVGSAVTN-FKVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  80 DWVqSIAAV-PCGQCHECRKGWMQVCQNQTSV-GYQYDGGFAEYMIVPpqvLKVDGLNRIPDDVDFDEA---SAAEP--F 152
Cdd:cd08286   80 DRV-LISCIsSCGTCGYCRKGLYSHCESGGWIlGNLIDGTQAEYVRIP---HADNSLYKLPEGVDEEAAvmlSDILPtgY 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 153 ACAI-NAQeqlgIEKGDFLVIFGAGPIGCMHTRIARgVHKVGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVME 231
Cdd:cd08286  156 ECGVlNGK----VKPGDTVAIVGAGPVGLAALLTAQ-LYSPSKIIMVDLDDNRLEV-AKKLGATHTVNSAKGDAIEQVLE 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 232 LTNGRGADVIITA--TPAniTQEQALSMAARNGRISFFG--GLPKT---------NPTIT---CDSNLIhyrqlhihgan 295
Cdd:cd08286  230 LTDGRGVDVVIEAvgIPA--TFELCQELVAPGGHIANVGvhGKPVDlhleklwikNITITtglVDTNTT----------- 296

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488471907 296 gsapehnKRALQYIASGQVPVKDLITRHVKLDDVMTVFDI---VAKGEAIKVTVE 347
Cdd:cd08286  297 -------PMLLKLVSSGKLDPSKLVTHRFKLSEIEKAYDTfsaAAKHKALKVIID 344
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 1-245 1.87e-38

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: 139.69  E-value: 1.87e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRF---HAPEDVRLEDVPEPEckPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGdWK 77
Cdd:cd08296    1 YKAVQVtepGGPLELVERDVPLPG--PGEVLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVGEGVSR-WK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  78 VGDWVqsiaAVP-----CGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEASaaePF 152
Cdd:cd08296   78 VGDRV----GVGwhgghCGTCDACRRGDFVHCENGKVTGVTRDGGYAEYMLAP-----AEALARIPDDLDAAEAA---PL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 153 ACA----INAQEQLGIEKGDFLVIFGAGPIGCMHTR-----------IARGVHKvgtivmidinaERLAMSAAAvkpDIT 217
Cdd:cd08296  146 LCAgvttFNALRNSGAKPGDLVAVQGIGGLGHLAVQyaakmgfrtvaISRGSDK-----------ADLARKLGA---HHY 211

                        250       260
                 ....*....|....*....|....*....
gi 488471907 218 IDGSQEDVVAKVMELTngrGADVII-TAT 245
Cdd:cd08296  212 IDTSKEDVAEALQELG---GAKLILaTAP 237
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 1-339 1.23e-37

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: 137.75  E-value: 1.23e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALR---FHAPEDVRLEDVPEPEckPDEIKIKVRNCSTCGTDVKILHNG-------HQNIT--GVT---TMGHEVAGEI 65
Cdd:cd08240    1 MKAAAvvePGKPLEEVEIDTPKPP--GTEVLVKVTACGVCHSDLHIWDGGydlgggkTMSLDdrGVKlplVLGHEIVGEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  66 VEIGSEVAGDwKVGDWVqsiAAVP---CGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPQVLKVDglnriPDDVD 142
Cdd:cd08240   79 VAVGPDAADV-KVGDKV---LVYPwigCGECPVCLAGDENLCAKGRALGIFQDGGYAEYVIVPHSRYLVD-----PGGLD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 143 FDEASaaePFAC----AINAQEQLGIEKGD-FLVIFGAGPIGCMHTRIARGVHKVGtIVMIDINAERLAmSAAAVKPDIT 217
Cdd:cd08240  150 PALAA---TLACsgltAYSAVKKLMPLVADePVVIIGAGGLGLMALALLKALGPAN-IIVVDIDEAKLE-AAKAAGADVV 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 218 IDGSQEDVVAKVMELTNGrGADVIITATPANITQEQALSMAARNGRIS----FFGGLPKTNPTITcdsnlihYRQLHIHG 293
Cdd:cd08240  225 VNGSDPDAAKRIIKAAGG-GVDAVIDFVNNSATASLAFDILAKGGKLVlvglFGGEATLPLPLLP-------LRALTIQG 296

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 488471907 294 ANGSAPEHNKRALQYIASG---QVPVKdlitrHVKLDDVMTVFDIVAKG 339
Cdd:cd08240  297 SYVGSLEELRELVALAKAGklkPIPLT-----ERPLSDVNDALDDLKAG 340
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-348 2.14e-37

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: 136.61  E-value: 2.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILhNGHQNITGVttMGHEVAGEIVEIGSevaGDWkVGD 80
Cdd:cd08242    1 MKALVLDGGLDLRVEDLPKPEPPPGEALVRVLLAGICNTDLEIY-KGYYPFPGV--PGHEFVGIVEEGPE---AEL-VGK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  81 WVQSIAAVPCGQCHECRKGWMQVCQNQTSVG-YQYDGGFAEYMIVPPQVLKVdglnrIPDDVDFDEASAAEPFACAINAQ 159
Cdd:cd08242   74 RVVGEINIACGRCEYCRRGLYTHCPNRTVLGiVDRDGAFAEYLTLPLENLHV-----VPDLVPDEQAVFAEPLAAALEIL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 160 EQLGIEKGDFLVIFGAGPIGCMhtrIARGVHKVG-TIVMIDINAERLAMSAAAVKPDITIDGSQEDvvakvmeltnGRGA 238
Cdd:cd08242  149 EQVPITPGDKVAVLGDGKLGLL---IAQVLALTGpDVVLVGRHSEKLALARRLGVETVLPDEAESE----------GGGF 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 239 DVIITATPANITQEQALSMAARNGRI---SFFGGLPKTNPTitcdsnLIHYRQLHIHGAN-GSAPEhnkrALQYIASGQV 314
Cdd:cd08242  216 DVVVEATGSPSGLELALRLVRPRGTVvlkSTYAGPASFDLT------KAVVNEITLVGSRcGPFAP----ALRLLRKGLV 285

                        330       340       350
                 ....*....|....*....|....*....|....
gi 488471907 315 PVKDLITRHVKLDDVMTVFDIVAKGEAIKVTVEP 348
Cdd:cd08242  286 DVDPLITAVYPLEEALEAFERAAEPGALKVLLRP 319
PRK10083 PRK10083
putative oxidoreductase; Provisional
 1-268 1.47e-36

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 134.87  E-value: 1.47e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGDwKVGD 80
Cdd:PRK10083   1 MKSIVIEKPNSLAIEERPIPQPAAGEVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGEGVDAA-RIGE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  81 WVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEASAAEPFACAINAQE 160
Cdd:PRK10083  80 RVAVDPVISCGHCYPCSIGKPNVCTSLVVLGVHRDGGFSEYAVVP-----AKNAHRIPDAIADQYAVMVEPFTIAANVTG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 161 QLGIEKGDFLVIFGAGPIGCMHTRIARGVHKVGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMEltngRGAD- 239
Cdd:PRK10083 155 RTGPTEQDVALIYGAGPVGLTIVQVLKGVYNVKAVIVADRIDERLAL-AKESGADWVINNAQEPLGEALEE----KGIKp 229

                        250       260       270
                 ....*....|....*....|....*....|
gi 488471907 240 -VIITATPANITQEQALSMAARNGRISFFG 268
Cdd:PRK10083 230 tLIIDAACHPSILEEAVTLASPAARIVLMG 259
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
 1-348 1.12e-34

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: 129.74  E-value: 1.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPEC-KPDEIKIKVRNCSTCGTDvkiLH--NGHQNITGVTTMGHEVAGEIVEIGSEVAGdWK 77
Cdd:cd08287    1 MRATVIHGPGDIRVEEVPDPVIeEPTDAVIRVVATCVCGSD---LWpyRGVSPTRAPAPIGHEFVGVVEEVGSEVTS-VK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  78 VGDWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPpqvlKVDG-LNRIPDDVDFDEASAAEPFACA- 155
Cdd:cd08287   77 PGDFVIAPFAISDGTCPFCRAGFTTSCVHGGFWGAFVDGGQGEYVRVP----LADGtLVKVPGSPSDDEDLLPSLLALSd 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 156 -----INAQEQLGIEKGDFLVIFGAGPIGCMHTrIARGVHKVGTIVMIDINAERLAMSAAAVKPDItIDGSQEDVVAKVM 230
Cdd:cd08287  153 vmgtgHHAAVSAGVRPGSTVVVVGDGAVGLCAV-LAAKRLGAERIIAMSRHEDRQALAREFGATDI-VAERGEEAVARVR 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 231 ELTNGRGADVIITATPANITQEQALSMAARNGRISFFgGLPKTNPTItcDSNLIHYRQLHIHGanGSAPehnKRA----- 305
Cdd:cd08287  231 ELTGGVGADAVLECVGTQESMEQAIAIARPGGRVGYV-GVPHGGVEL--DVRELFFRNVGLAG--GPAP---VRRylpel 302

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 488471907 306 LQYIASGQVPVKDLITRHVKLDDVMTVFDIVAKGEAIKVTVEP 348
Cdd:cd08287  303 LDDVLAGRINPGRVFDLTLPLDEVAEGYRAMDERRAIKVLLRP 345
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 8-347 6.21e-34

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: 127.09  E-value: 6.21e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   8 APEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNG-----HQNITGVTtmGHEVAGEIVEIGSEVAGdWKVGDWV 82
Cdd:cd08269    3 GPGRFEVEEHPRPTPGPGQVLVRVEGCGVCGSDLPAFNQGrpwfvYPAEPGGP--GHEGWGRVVALGPGVRG-LAVGDRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  83 QSIAAvpcgqchecrkgwmqvcqnqtsvgyqydGGFAEYMIVppqvlKVDGLNRIPDDVDfDEASAAEPFACAINAQEQL 162
Cdd:cd08269   80 AGLSG----------------------------GAFAEYDLA-----DADHAVPLPSLLD-GQAFPGEPLGCALNVFRRG 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 163 GIEKGDFLVIFGAGPIGCMHTRIA--RGVHKVgtiVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMELTNGRGADV 240
Cdd:cd08269  126 WIRAGKTVAVIGAGFIGLLFLQLAaaAGARRV---IAIDRRPARLAL-ARELGATEVVTDDSEAIVERVRELTGGAGADV 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 241 IITATPANITQEQALSMAARNGRISFFG---GLPKTNPTITCDSNLIHYRQLHIHgANGSAPEHNKRALQYIASGQVPVK 317
Cdd:cd08269  202 VIEAVGHQWPLDLAGELVAERGRLVIFGyhqDGPRPVPFQTWNWKGIDLINAVER-DPRIGLEGMREAVKLIADGRLDLG 280

                        330       340       350
                 ....*....|....*....|....*....|..
gi 488471907 318 DLITRHVKLDDVMTVFDIVAKGEA--IKVTVE 347
Cdd:cd08269  281 SLLTHEFPLEELGDAFEAARRRPDgfIKGVIV 312
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
1-210 1.63e-33

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 126.87  E-value: 1.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECK-PDEIKIKVRNCSTCGTDV-KILHNGHQNITgvTTMGHEVAGEIVEIGSEVAgDWKV 78
Cdd:PRK10309   1 MKSVVNDTDGIVRVAESPIPEIKhQDDVLVKVASSGLCGSDIpRIFKNGAHYYP--ITLGHEFSGYVEAVGSGVD-DLHP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  79 GDWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVppqvlKVDGLNRIPDDVDFDEASAAEPFACAINA 158
Cdd:PRK10309  78 GDAVACVPLLPCFTCPECLRGFYSLCAKYDFIGSRRDGGNAEYIVV-----KRKNLFALPTDMPIEDGAFIEPITVGLHA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488471907 159 QEQLGIEKGDFLVIFGAGPIGCMHTRIARGVhKVGTIVMIDINAERLAMSAA 210
Cdd:PRK10309 153 FHLAQGCEGKNVIIIGAGTIGLLAIQCAVAL-GAKSVTAIDINSEKLALAKS 203
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 9-347 1.03e-29

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: 117.09  E-value: 1.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   9 PEDVRLEDVPEPecKPDEIKIKVRNCSTCGTDVKILhNGHQNITGVTTMGHEVAGEIVEIGSEVaGDWKVGDWVQSIAAV 88
Cdd:cd08281   20 PLVIEEVELDPP--GPGEVLVKIAAAGLCHSDLSVI-NGDRPRPLPMALGHEAAGVVVEVGEGV-TDLEVGDHVVLVFVP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  89 PCGQCHECRKGWMQVCQNQTSV---GYQYDGG------------------FAEYMIVPPQvlkvdGLNRIPDDVDFDEAS 147
Cdd:cd08281   96 SCGHCRPCAEGRPALCEPGAAAngaGTLLSGGrrlrlrggeinhhlgvsaFAEYAVVSRR-----SVVKIDKDVPLEIAA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 148 AaepFACAI-----NAQEQLGIEKGDFLVIFGAGPIG--CMHTRIARGVhkvGTIVMIDINAERLAMsAAAVKPDITIDG 220
Cdd:cd08281  171 L---FGCAVltgvgAVVNTAGVRPGQSVAVVGLGGVGlsALLGAVAAGA---SQVVAVDLNEDKLAL-ARELGATATVNA 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 221 SQEDVVAKVMELTNGrGADVIITATPANITQEQALSMAARNGRIsFFGGLPKTNPTITcdsnlihYRQLHIHGAN----- 295
Cdd:cd08281  244 GDPNAVEQVRELTGG-GVDYAFEMAGSVPALETAYEITRRGGTT-VTAGLPDPEARLS-------VPALSLVAEErtlkg 314

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488471907 296 ---GSA-PEHN-KRALQYIASGQVPVKDLITRHVKLDDVMTVFDIVAKGEAIKVTVE 347
Cdd:cd08281  315 symGSCvPRRDiPRYLALYLSGRLPVDKLLTHRLPLDEINEGFDRLAAGEAVRQVIL 371
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 25-127 1.63e-29

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: 109.24  E-value: 1.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   25 DEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVGDWVQSIAAVPCGQCHECRKGWMQVC 104
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTG-LKVGDRVVVEPLIPCGKCEYCREGRYNLC 79

                          90       100
                  ....*....|....*....|...
gi 488471907  105 QNQTSVGYQYDGGFAEYMIVPPQ 127
Cdd:pfam08240  80 PNGRFLGYDRDGGFAEYVVVPER 102
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 1-348 2.63e-29

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: 115.77  E-value: 2.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLEDVPEPECK-PDEIKIKVRNCSTCGTDvkiLHNGHQnITGV---TTMGHEVAGEIVEIGSEVAGdW 76
Cdd:cd08282    1 MKAVVYGGPGNVAVEDVPDPKIEhPTDAIVRITTTAICGSD---LHMYRG-RTGAepgLVLGHEAMGEVEEVGSAVES-L 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  77 KVGDWVqSIA-AVPCGQCHECRKGWMQVCQN------QTSVGYQ----YDGGFAEYMIVPpqvLKVDGLNRIPDDVDFDE 145
Cdd:cd08282   76 KVGDRV-VVPfNVACGRCRNCKRGLTGVCLTvnpgraGGAYGYVdmgpYGGGQAEYLRVP---YADFNLLKLPDRDGAKE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 146 ASA----AEPFACAINAQEQLGIEKGDFLVIFGAGPIGCM--HTRIARGVHKVgtIVmIDINAERLAMSAA--AvkpdIT 217
Cdd:cd08282  152 KDDylmlSDIFPTGWHGLELAGVQPGDTVAVFGAGPVGLMaaYSAILRGASRV--YV-VDHVPERLDLAESigA----IP 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 218 IDGSQEDVVAKVMELTnGRGADVIITAT-----------PANITQEQALSMAARNGRIS----FFGGLPKT------NPT 276
Cdd:cd08282  225 IDFSDGDPVEQILGLE-PGGVDRAVDCVgyeardrggeaQPNLVLNQLIRVTRPGGGIGivgvYVAEDPGAgdaaakQGE 303

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488471907 277 ITCDSNLIHYRQLHIHGanGSAP--EHNKRALQYIASGQVPVKDLITRHVKLDDVMTVFDIVAKGEAIKVTVEP 348
Cdd:cd08282  304 LSFDFGLLWAKGLSFGT--GQAPvkKYNRQLRDLILAGRAKPSFVVSHVISLEDAPEAYARFDKRLETKVVIKP 375
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 1-296 1.43e-28

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: 112.83  E-value: 1.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAP--EDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILhnghqNITGVTTMGH----EVAGEIVEIGSEVAG 74
Cdd:cd08264    1 MKALVFEKSgiENLKVEDVKDPKPGPGEVLIRVKMAGVNPVDYNVI-----NAVKVKPMPHipgaEFAGVVEEVGDHVKG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  75 dWKVGDWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPQvlkvdGLNRIPDDVDFDEAsAAEPFAC 154
Cdd:cd08264   76 -VKKGDRVVVYNRVFDGTCDMCLSGNEMLCRNGGIIGVVSNGGYAEYIVVPEK-----NLFKIPDSISDELA-ASLPVAA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 155 --AINAQEQLGIEKGDFLVIFGA-GPIGCMHTRIARgvhKVGTIVMIDINAERLAMSAAavkpDITIDGsqEDVVAKVME 231
Cdd:cd08264  149 ltAYHALKTAGLGPGETVVVFGAsGNTGIFAVQLAK---MMGAEVIAVSRKDWLKEFGA----DEVVDY--DEVEEKVKE 219

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488471907 232 LTngRGADVIITATPANItQEQALSMAARNGRISFFGGLpkTNPTITCDSNLIHYRQLHIHGANG 296
Cdd:cd08264  220 IT--KMADVVINSLGSSF-WDLSLSVLGRGGRLVTFGTL--TGGEVKLDLSDLYSKQISIIGSTG 279
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 1-348 2.08e-28

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 112.82  E-value: 2.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAP-EDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVG 79
Cdd:PRK13771   1 MKAVILPGFkQGYRIEEVPDPKPGKDEVVIKVNYAGLCYRDLLQLQGFYPRMKYPVILGHEVVGTVEEVGENVKG-FKPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  80 DWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVppqvlKVDGLNRIPDDVDFDEASAAepfACA---- 155
Cdd:PRK13771  80 DRVASLLYAPDGTCEYCRSGEEAYCKNRLGYGEELDGFFAEYAKV-----KVTSLVKVPPNVSDEGAVIV---PCVtgmv 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 156 INAQEQLGIEKGDFLVIFGA-GPIGCMHTRIARGV-HKVGTIVMIDINAERLAMSAaavkpDITIDGSQ--EDVvakvme 231
Cdd:PRK13771 152 YRGLRRAGVKKGETVLVTGAgGGVGIHAIQVAKALgAKVIAVTSSESKAKIVSKYA-----DYVIVGSKfsEEV------ 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 232 lTNGRGADVIITA--TPaniTQEQALSMAARNGRISFFGGLpKTNPTITCDSNLIHYRQLHIHGANGSAPEHNKRALQYI 309
Cdd:PRK13771 221 -KKIGGADIVIETvgTP---TLEESLRSLNMGGKIIQIGNV-DPSPTYSLRLGYIILKDIEIIGHISATKRDVEEALKLV 295

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 488471907 310 ASGQvpVKDLITRHVKLDDVMTVFDIVAKGEAI-KVTVEP 348
Cdd:PRK13771 296 AEGK--IKPVIGAEVSLSEIDKALEELKDKSRIgKILVKP 333
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 10-343 2.35e-27

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: 110.28  E-value: 2.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  10 EDVRLEDVpepecKPDEIKIKVRNCSTCGTDVKILhnghQNITGVTT---MGHEVAGEIVEIGSEVaGDWKVGDWV-QSI 85
Cdd:cd08278   18 EDVELDDP-----RPDEVLVRIVATGICHTDLVVR----DGGLPTPLpavLGHEGAGVVEAVGSAV-TGLKPGDHVvLSF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  86 AAvpCGQCHECRKGWMQVCQNQT-----------SVGYQYDGG------------FAEYMIVPP-QVLKVDGlnripddv 141
Cdd:cd08278   88 AS--CGECANCLSGHPAYCENFFplnfsgrrpdgSTPLSLDDGtpvhghffgqssFATYAVVHErNVVKVDK-------- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 142 DFDEASAAePFACAI--------NAqeqLGIEKGDFLVIFGAGPIG---CMHTRIARgvhkVGTIVMIDINAERLAMsAA 210
Cdd:cd08278  158 DVPLELLA-PLGCGIqtgagavlNV---LKPRPGSSIAVFGAGAVGlaaVMAAKIAG----CTTIIAVDIVDSRLEL-AK 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 211 AVKPDITIDGSQEDVVAKVMELTnGRGADVII--TATPANItqEQALSMAARNGRISFFgGLPKTNPTITCDSNLIHYRQ 288
Cdd:cd08278  229 ELGATHVINPKEEDLVAAIREIT-GGGVDYALdtTGVPAVI--EQAVDALAPRGTLALV-GAPPPGAEVTLDVNDLLVSG 304

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488471907 289 LHIHGAN-GSA------PehnkRALQYIASGQVPVKDLITrHVKLDDVMTVFDIVAKGEAIK 343
Cdd:cd08278  305 KTIRGVIeGDSvpqefiP----RLIELYRQGKFPFDKLVT-FYPFEDINQAIADSESGKVIK 361
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 1-347 4.24e-27

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: 108.74  E-value: 4.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHA---PEDVRLEDV-PEPEcKPDEIKIKVRNCSTCGTDVKILHNGHQNitGVT---TMGHEVAGEIVEIGSEVA 73
Cdd:cd08241    1 MKAVVCKElggPEDLVLEEVpPEPG-APGEVRIRVEAAGVNFPDLLMIQGKYQV--KPPlpfVPGSEVAGVVEAVGEGVT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  74 GdWKVGDWVqsiaavpcgqchecrkgwmqvcqnqtsVGYQYDGGFAEYMIVPPqvlkvDGLNRIPDDVDFDEAsAAEP-- 151
Cdd:cd08241   78 G-FKVGDRV---------------------------VALTGQGGFAEEVVVPA-----AAVFPLPDGLSFEEA-AALPvt 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 152 FACAINAQEQLG-IEKGDFLVIFGA-GPIGCMHTRIARGVhkvGTIVmidI----NAERLAMsAAAVKPDITIDGSQEDV 225
Cdd:cd08241  124 YGTAYHALVRRArLQPGETVLVLGAaGGVGLAAVQLAKAL---GARV---IaaasSEEKLAL-ARALGADHVIDYRDPDL 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 226 VAKVMELTNGRGADVIITATPANITqEQALSMAARNGR---ISFFGGLPKTNPTitcdsNLIHYRQLHIHGAN-----GS 297
Cdd:cd08241  197 RERVKALTGGRGVDVVYDPVGGDVF-EASLRSLAWGGRllvIGFASGEIPQIPA-----NLLLLKNISVVGVYwgayaRR 270

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488471907 298 APEHNKRA----LQYIASGQVPVkdLITRHVKLDDVMTVFDIVAKGEAI-KVTVE 347
Cdd:cd08241  271 EPELLRANlaelFDLLAEGKIRP--HVSAVFPLEQAAEALRALADRKATgKVVLT 323
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 1-187 4.43e-27

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: 108.81  E-value: 4.43e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDV-----RLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGd 75
Cdd:cd08298    1 MKAMVLEKPGPIeenplRLTEVPVPEPGPGEVLIKVEACGVCRTDLHIVEGDLPPPKLPLIPGHEIVGRVEAVGPGVTR- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  76 WKVGDWVqsiaAVP-----CGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPqvlkvDGLNRIPDdvDFDEASAAe 150
Cdd:cd08298   80 FSVGDRV----GVPwlgstCGECRYCRSGRENLCDNARFTGYTVDGGYAEYMVADE-----RFAYPIPE--DYDDEEAA- 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 488471907 151 PFACA----INAQEQLGIEKGDFLVIFGAGPIGCMHTRIAR 187
Cdd:cd08298  148 PLLCAgiigYRALKLAGLKPGQRLGLYGFGASAHLALQIAR 188
dearomat_had TIGR03201
6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase; Members of this protein family are ...
 15-340 2.08e-26

6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase; Members of this protein family are 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase, an enzyme in the anaerobic metabolism of aromatic enzymes by way of benzoyl-CoA, as seen in Thauera aromatica, Geobacter metallireducens, and Azoarcus sp. The experimentally characterized form from T. aromatica uses only NAD+, not NADP+. Note that Rhodopseudomonas palustris uses a different pathway to perform a similar degradation of benzoyl-CoA to 3-hydroxpimelyl-CoA.


Pssm-ID: 132245 [Multi-domain]  Cd Length: 349  Bit Score: 107.30  E-value: 2.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   15 EDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVT-TMGHEVAGEIVEIGSEvAGDWkVGDWVQSIAAVPCGQC 93
Cdd:TIGR03201  14 TRVEIPELGAGDVVVKVAGCGVCHTDLSYYYMGVRTNHALPlALGHEISGRVIQAGAG-AASW-IGKAVIVPAVIPCGEC 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   94 HECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPQVL-KVDGLNRIPDDVDFDEAS-AAEPFACAINAQEQLGIEKGDFLV 171
Cdd:TIGR03201  92 ELCKTGRGTICRAQKMPGNDMQGGFASHIVVPAKGLcVVDEARLAAAGLPLEHVSvVADAVTTPYQAAVQAGLKKGDLVI 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  172 IFGAGPIGCMHTRIARGVHkvGTIVMIDINAERLAMSAAAvKPDITI---DGSQEDVVAKVMELTNGRGAD----VIITA 244
Cdd:TIGR03201 172 VIGAGGVGGYMVQTAKAMG--AAVVAIDIDPEKLEMMKGF-GADLTLnpkDKSAREVKKLIKAFAKARGLRstgwKIFEC 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  245 TPANITQEQALSMAARNGRISFFG-GLPKTNPTItcdSNLI--HYRQLhihGANGSAPEHNKRALQYIASGQVPVKDLIT 321
Cdd:TIGR03201 249 SGSKPGQESALSLLSHGGTLVVVGyTMAKTEYRL---SNLMafHARAL---GNWGCPPDRYPAALDLVLDGKIQLGPFVE 322

                         330
                  ....*....|....*....
gi 488471907  322 RHvKLDDVMTVFDIVAKGE 340
Cdd:TIGR03201 323 RR-PLDQIEHVFAAAHHHK 340
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 57-346 1.51e-25

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: 103.50  E-value: 1.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  57 MGHEVAGEIVEIGSEVAGDWkVGDWVqsiaAVPCGQchecrkgwmqvcqnqtsvgyqydggfAEYMIVPPQVLKvdglnR 136
Cdd:cd08255   24 PGYSSVGRVVEVGSGVTGFK-PGDRV----FCFGPH--------------------------AERVVVPANLLV-----P 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 137 IPDDVDFDEASAAEPFACAINAQEQLGIEKGDFLVIFGAGPIGCMHTRIARgVHKVGTIVMIDINAERLAMSAAavkpdi 216
Cdd:cd08255   68 LPDGLPPERAALTALAATALNGVRDAEPRLGERVAVVGLGLVGLLAAQLAK-AAGAREVVGVDPDAARRELAEA------ 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 217 tiDGSQEDVVAKVMELTNGRGADVII--TATPANItqEQALSMAARNGRI---SFFGGLPKTNptitcdSNLIHYRQLHI 291
Cdd:cd08255  141 --LGPADPVAADTADEIGGRGADVVIeaSGSPSAL--ETALRLLRDRGRVvlvGWYGLKPLLL------GEEFHFKRLPI 210

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488471907 292 ---HGANGSAPEHNKR---------ALQYIASGqvPVKDLITRHVKLDDVMTVFDIVAKGEAIKVTV 346
Cdd:cd08255  211 rssQVYGIGRYDRPRRwtearnleeALDLLAEG--RLEALITHRVPFEDAPEAYRLLFEDPPECLKV 275
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 11-344 2.89e-25

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 104.47  E-value: 2.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  11 DVRLEDVPEPECKPDEIKIKVRNCSTCGTDV---KILHNGHQNITGVTTMGHEVAGEIVEIGSEVAgDWKVGDWVQSIAA 87
Cdd:PLN02702  28 TLKIQPFKLPPLGPHDVRVRMKAVGICGSDVhylKTMRCADFVVKEPMVIGHECAGIIEEVGSEVK-HLVVGDRVALEPG 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  88 VPCGQCHECRKGWMQVCQNQTSVGYQ-YDGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEASAAEPFACAINAQEQLGIEK 166
Cdd:PLN02702 107 ISCWRCNLCKEGRYNLCPEMKFFATPpVHGSLANQVVHP-----ADLCFKLPENVSLEEGAMCEPLSVGVHACRRANIGP 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 167 GDFLVIFGAGPIGCMhTRIARGVHKVGTIVMIDINAERLAMSAAAVKPDIT-IDGSQEDVVAKVMELTNGRGADVIITAT 245
Cdd:PLN02702 182 ETNVLVMGAGPIGLV-TMLAARAFGAPRIVIVDVDDERLSVAKQLGADEIVlVSTNIEDVESEVEEIQKAMGGGIDVSFD 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 246 PA--NITQEQALSMAARNGRISFFG------GLPKTnPTITCDSNLI---HYRQLHihgangsapehnKRALQYIASGQV 314
Cdd:PLN02702 261 CVgfNKTMSTALEATRAGGKVCLVGmghnemTVPLT-PAAAREVDVVgvfRYRNTW------------PLCLEFLRSGKI 327

                        330       340       350
                 ....*....|....*....|....*....|...
gi 488471907 315 PVKDLITRHVKLD--DVMTVFDIVAKG-EAIKV 344
Cdd:PLN02702 328 DVKPLITHRFGFSqkEVEEAFETSARGgNAIKV 360
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
 1-244 1.68e-24

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 102.03  E-value: 1.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRF-HAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTtMGHEVAGEIVEIGSEVaGDWKVG 79
Cdd:PRK09422   1 MKAAVVnKDHTGDVVVEKTLRPLKHGEALVKMEYCGVCHTDLHVANGDFGDKTGRI-LGHEGIGIVKEVGPGV-TSLKVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  80 DWVqSIAAV--PCGQCHECRKGWMQVCQNQTSVGYQYDGGFAEYMIVppqvlKVDGLNRIPDDVDFDEASAaepFACA-- 155
Cdd:PRK09422  79 DRV-SIAWFfeGCGHCEYCTTGRETLCRSVKNAGYTVDGGMAEQCIV-----TADYAVKVPEGLDPAQASS---ITCAgv 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 156 --INAQEQLGIEKGDFLVIFGAGPIGCMHTRIARGVHKVGTIVmIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMELT 233
Cdd:PRK09422 150 ttYKAIKVSGIKPGQWIAIYGAGGLGNLALQYAKNVFNAKVIA-VDINDDKLAL-AKEVGADLTINSKRVEDVAKIIQEK 227

                        250
                 ....*....|..
gi 488471907 234 NGrGAD-VIITA 244
Cdd:PRK09422 228 TG-GAHaAVVTA 238
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-329 2.15e-24

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


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 101.52  E-value: 2.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHA---PEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVkILHNGHQNITGV--TTMGHEVAGEIVEIGSEVAGD 75
Cdd:cd08268    1 MRAVRFHQfggPEVLRIEELPVPAPGAGEVLIRVEAIGLNRADA-MFRRGAYIEPPPlpARLGYEAAGVVEAVGAGVTGF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  76 WkVGDWVQSIAAVPCGQchecrkgwmqvcqnqtsvgyqYdGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEASAA-EPFAC 154
Cdd:cd08268   80 A-VGDRVSVIPAADLGQ---------------------Y-GTYAEYALVP-----AAAVVKLPDGLSFVEAAALwMQYLT 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 155 AINA-QEQLGIEKGDFLVIFGA-GPIGCMHTRIAR--GVHKVGTIVMIDINAERLAMSAAAVkpditIDGSQEDVVAKVM 230
Cdd:cd08268  132 AYGAlVELAGLRPGDSVLITAAsSSVGLAAIQIANaaGATVIATTRTSEKRDALLALGAAHV-----IVTDEEDLVAEVL 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 231 ELTNGRGADVIITAT--PAnitQEQALSMAARNGRISFFGGL-PKTNPTITCDsNLIHYRQLHIHGANG--SAPEHNKRA 305
Cdd:cd08268  207 RITGGKGVDVVFDPVggPQ---FAKLADALAPGGTLVVYGALsGEPTPFPLKA-ALKKSLTFRGYSLDEitLDPEARRRA 282

                        330       340
                 ....*....|....*....|....*...
gi 488471907 306 LQYI----ASGQvpVKDLITRHVKLDDV 329
Cdd:cd08268  283 IAFIldglASGA--LKPVVDRVFPFDDI 308
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 1-341 2.98e-24

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: 100.71  E-value: 2.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHA---PEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVT---TMGHEVAGEIVEIGSEVaG 74
Cdd:cd05289    1 MKAVRIHEyggPEVLELADVPTPEPGPGEVLVKVHAAGVNPVDLKIREGLLKAAFPLTlplIPGHDVAGVVVAVGPGV-T 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  75 DWKVGDWVqsiaavpCGqchecrkgwmqvcqnqtSVGYQYDGGFAEYMIVPPqvlkvDGLNRIPDDVDFDEAsAAEPFAc 154
Cdd:cd05289   80 GFKVGDEV-------FG-----------------MTPFTRGGAYAEYVVVPA-----DELALKPANLSFEEA-AALPLA- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 155 AINA----QEQLGIEKGDFLVIFGA-GPIGCMHTRIAR--GVHKVGTIvmidinAERlamSAAAVK---PDITIDGSQED 224
Cdd:cd05289  129 GLTAwqalFELGGLKAGQTVLIHGAaGGVGSFAVQLAKarGARVIATA------SAA---NADFLRslgADEVIDYTKGD 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 225 VVAKvmelTNGRGADVIITATPANiTQEQALSMAARNGRISffgglpkTNPTITCDSNLIHYRQLHIHGANGSAPEHNKR 304
Cdd:cd05289  200 FERA----AAPGGVDAVLDTVGGE-TLARSLALVKPGGRLV-------SIAGPPPAEQAAKRRGVRAGFVFVEPDGEQLA 267

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 488471907 305 AL-QYIASGQVPVkdLITRHVKLDDVMTVFDIVAKGEA 341
Cdd:cd05289  268 ELaELVEAGKLRP--VVDRVFPLEDAAEAHERLESGHA 303
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 1-347 8.26e-24

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: 100.37  E-value: 8.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPE-DVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGH-QNITGVTTM--GHEVAGEIVEIGSevAGDW 76
Cdd:cd08230    1 MKAIAVKPGKpGVRVVDIPEPEPTPGEVLVRTLEVGVCGTDREIVAGEYgTAPPGEDFLvlGHEALGVVEEVGD--GSGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  77 KVGDWVQSIAAVPCGQCHECRKGWMQVCQN--QTSVGYQYDGGF-AEYMIVPPQVLkVdglnRIPDDVDfDEASAAEPFA 153
Cdd:cd08230   79 SPGDLVVPTVRRPPGKCLNCRIGRPDFCETgeYTERGIKGLHGFmREYFVDDPEYL-V----KVPPSLA-DVGVLLEPLS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 154 C-------AINAQEQLGIEKGDFLVIFGAGPIGCMHTRIARGVHKvgTIVMIDINaerlamSAAAVKPDIT-------ID 219
Cdd:cd08230  153 VvekaieqAEAVQKRLPTWNPRRALVLGAGPIGLLAALLLRLRGF--EVYVLNRR------DPPDPKADIVeelgatyVN 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 220 GSQEDV--VAKVMEltngrgADVIITATPANITQEQALSMAARNGRISFFGGLPKTNPTITCDSNLIHYRQLH---IHGA 294
Cdd:cd08230  225 SSKTPVaeVKLVGE------FDLIIEATGVPPLAFEALPALAPNGVVILFGVPGGGREFEVDGGELNRDLVLGnkaLVGS 298

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488471907 295 NGSAPEHNKRALQYIASGQVP----VKDLITRHVKLDDVMTVFDIVAKGEaIKVTVE 347
Cdd:cd08230  299 VNANKRHFEQAVEDLAQWKYRwpgvLERLITRRVPLEEFAEALTEKPDGE-IKVVIE 354
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 1-285 1.09e-22

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


Pssm-ID: 176215 [Multi-domain]  Cd Length: 325  Bit Score: 96.50  E-value: 1.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHA--PEDV-RLEDVPEPECKPDEIKIKVRNCSTCGTDVKILH-NGHQNITGVTTMGHEVAGEIVEIGSEVAGdW 76
Cdd:cd08253    1 MRAIRYHEfgAPDVlRLGDLPVPTPGPGEVLVRVHASGVNPVDTYIRAgAYPGLPPLPYVPGSDGAGVVEAVGEGVDG-L 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  77 KVGDWVqsiaavpcgqchecrkgWMqvcqnqTSVGYQYD-GGFAEYMIVPPqvlkvDGLNRIPDDVDFDE-ASAAEPFAC 154
Cdd:cd08253   80 KVGDRV-----------------WL------TNLGWGRRqGTAAEYVVVPA-----DQLVPLPDGVSFEQgAALGIPALT 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 155 AINAQEQL-GIEKGD-FLVIFGAGPIGCMHTRIAR--GVHKVGTiVMIDINAErLAMSAAAvkpDITIDGSQEDVVAKVM 230
Cdd:cd08253  132 AYRALFHRaGAKAGEtVLVHGGSGAVGHAAVQLARwaGARVIAT-ASSAEGAE-LVRQAGA---DAVFNYRAEDLADRIL 206

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488471907 231 ELTNGRGADVII-TATPANItqEQALSMAARNGRISFFGGLPKT-----NPTITCDSNLIH 285
Cdd:cd08253  207 AATAGQGVDVIIeVLANVNL--AKDLDVLAPGGRIVVYGSGGLRgtipiNPLMAKEASIRG 265
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 1-329 5.95e-22

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: 94.43  E-value: 5.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALR---FHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDvkILH-NGHQNIT-GVT-TMGHEVAGEIVEIGSEVaG 74
Cdd:cd05276    1 MKAIVikePGGPEVLELGEVPKPAPGPGEVLIRVAAAGVNRAD--LLQrQGLYPPPpGASdILGLEVAGVVVAVGPGV-T 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  75 DWKVGDWVqsiaavpCGQCHecrkGwmqvcqnqtsvgyqydGGFAEYMIVPP-QVLkvdglnRIPDDVDFDEASA-AEPF 152
Cdd:cd05276   78 GWKVGDRV-------CALLA----G----------------GGYAEYVVVPAgQLL------PVPEGLSLVEAAAlPEVF 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 153 ACAINAQEQLG-IEKGD-FLVIFGAGPIGCMHTRIAR--GVHKVGTIVmidiNAERLAMsAAAVKPDITIDGSQEDVVAK 228
Cdd:cd05276  125 FTAWQNLFQLGgLKAGEtVLIHGGASGVGTAAIQLAKalGARVIATAG----SEEKLEA-CRALGADVAINYRTEDFAEE 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 229 VMELTNGRGADVIITATPANITQeQALSMAARNGR---ISFFGGlpktnPTITCDSNLIHYRQLHIHGAN-GSAPEHNKR 304
Cdd:cd05276  200 VKEATGGRGVDVILDMVGGDYLA-RNLRALAPDGRlvlIGLLGG-----AKAELDLAPLLRKRLTLTGSTlRSRSLEEKA 273

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 488471907 305 AL---------QYIASGQV-PVkdlITRHVKLDDV 329
Cdd:cd05276  274 ALaaafrehvwPLFASGRIrPV---IDKVFPLEEA 305
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-320 2.23e-21

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: 92.98  E-value: 2.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAP---EDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHqnitGVTTMGHEV-----AGEIVEIGSEV 72
Cdd:cd08276    1 MKAWRLSGGgglDNLKLVEEPVPEPGPGEVLVRVHAVSLNYRDLLILNGRY----PPPVKDPLIplsdgAGEVVAVGEGV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  73 aGDWKVGDWVQSIAAVpcgqchECRKGWMQVCQNQTSVGYQYDGGFAEYMIVPPqvlkvDGLNRIPDDVDFDEASAaepF 152
Cdd:cd08276   77 -TRFKVGDRVVPTFFP------NWLDGPPTAEDEASALGGPIDGVLAEYVVLPE-----EGLVRAPDHLSFEEAAT---L 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 153 AC----AINA-QEQLGIEKGDFLVIFGAGPIGCMHTRIARGVhkvGTIVMI----DINAERL-AMSAaavkpDITIDGSQ 222
Cdd:cd08276  142 PCagltAWNAlFGLGPLKPGDTVLVQGTGGVSLFALQFAKAA---GARVIAtsssDEKLERAkALGA-----DHVINYRT 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 223 E-DVVAKVMELTNGRGADVII-TATPANItqEQALSMAARNGRIS---FFGGLPKTNPTItcdsnLIHYRQLHIHG-ANG 296
Cdd:cd08276  214 TpDWGEEVLKLTGGRGVDHVVeVGGPGTL--AQSIKAVAPGGVISligFLSGFEAPVLLL-----PLLTKGATLRGiAVG 286

                        330       340
                 ....*....|....*....|....*.
gi 488471907 297 S--APEHNKRALQyiASGQVPVKDLI 320
Cdd:cd08276  287 SraQFEAMNRAIE--AHRIRPVIDRV 310
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 23-346 2.42e-21

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: 93.66  E-value: 2.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  23 KPDEIKIKVRNCSTCGTDVKILhNGHQNITGVTTMGHEVAGEIVEIGSEVAgDWKVGDWVQSIAAVPCGQCHECRKGWMQ 102
Cdd:cd05279   24 KAGEVRIKVVATGVCHTDLHVI-DGKLPTPLPVILGHEGAGIVESIGPGVT-TLKPGDKVIPLFGPQCGKCKQCLNPRPN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 103 VCQ---NQTSVGYQYDG------------------GFAEYMIVPPQvlkvdGLNRIPDDVDFDEASaaePFACAIN---- 157
Cdd:cd05279  102 LCSksrGTNGRGLMSDGtsrftckgkpihhflgtsTFAEYTVVSEI-----SLAKIDPDAPLEKVC---LIGCGFStgyg 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 158 -AQEQLGIEKGDFLVIFGAGPIGcMHTRIARGVHKVGTIVMIDINAERLAMsAAAVKPDITIDG--SQEDVVAKVMELTN 234
Cdd:cd05279  174 aAVNTAKVTPGSTCAVFGLGGVG-LSVIMGCKAAGASRIIAVDINKDKFEK-AKQLGATECINPrdQDKPIVEVLTEMTD 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 235 GrGADVIITATPANITQEQALSMAARNGRISFFGGLPKTNPTITCDSNLIHYRQLhIHGA---NGSAPEHNKRALQYIAS 311
Cdd:cd05279  252 G-GVDYAFEVIGSADTLKQALDATRLGGGTSVVVGVPPSGTEATLDPNDLLTGRT-IKGTvfgGWKSKDSVPKLVALYRQ 329

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 488471907 312 GQVPVKDLITRHVKLDDVMTVFDIVAKGEAIKVTV 346
Cdd:cd05279  330 KKFPLDELITHVLPFEEINDGFDLMRSGESIRTIL 364
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-275 1.07e-20

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 91.18  E-value: 1.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAP---EDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAGdWK 77
Cdd:cd08271    1 MKAWVLPKPgaaLQLTLEEIEIPGPGAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTG-WK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  78 VGDwvqsiaavpcgqchecrkgwmQVCQNQtsvGYQYDGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEAsAAEPfaCA-- 155
Cdd:cd08271   80 VGD---------------------RVAYHA---SLARGGSFAEYTVVD-----ARAVLPLPDSLSFEEA-AALP--CAgl 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 156 ---INAQEQLGIEKGD-FLVIFGAGPIGCMHTRIARGVHKVGTIVMIDINAERLAMSAAavkpDITIDGSQEDVVAKVME 231
Cdd:cd08271  128 tayQALFKKLRIEAGRtILITGGAGGVGSFAVQLAKRAGLRVITTCSKRNFEYVKSLGA----DHVIDYNDEDVCERIKE 203

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 488471907 232 LTNGRGADVIITATPANITQEQALSMAArNGRISFFGGLPKTNP 275
Cdd:cd08271  204 ITGGRGVDAVLDTVGGETAAALAPTLAF-NGHLVCIQGRPDASP 246
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 2-268 1.67e-20

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: 90.58  E-value: 1.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   2 KALRFHA---PEDVRLEDVPEPECKPDEIKIKVR----NCstcgtdVKILH-NGHQNITGVTTMGHEVAGEIVEIGSEVA 73
Cdd:cd05286    1 KAVRIHKtggPEVLEYEDVPVPEPGPGEVLVRNTaigvNF------IDTYFrSGLYPLPLPFVLGVEGAGVVEAVGPGVT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  74 gDWKVGDwvqsiaavpcgqchecRKGWMQVcqnqtsvgyqyDGGFAEYMIVPPQVLkvdglNRIPDDVDFDEASA----- 148
Cdd:cd05286   75 -GFKVGD----------------RVAYAGP-----------PGAYAEYRVVPASRL-----VKLPDGISDETAAAlllqg 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 149 --AEPFACAINAqeqlgIEKGDFLVIFG-AGPIGCMHTRIA--RGVHKVGTIVmidiNAERLAMSAAAVKpDITIDGSQE 223
Cdd:cd05286  122 ltAHYLLRETYP-----VKPGDTVLVHAaAGGVGLLLTQWAkaLGATVIGTVS----SEEKAELARAAGA-DHVINYRDE 191

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 488471907 224 DVVAKVMELTNGRGADVIITATPANiTQEQALSMAARNGRISFFG 268
Cdd:cd05286  192 DFVERVREITGGRGVDVVYDGVGKD-TFEGSLDSLRPRGTLVSFG 235
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 24-341 1.23e-19

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: 88.32  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  24 PDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAgDWKVGD------WVQSiaavpCGQCHECR 97
Cdd:cd05283   24 PDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVT-KFKVGDrvgvgcQVDS-----CGTCEQCK 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  98 KGWMQVCQNQTSVGYQYD-------GGFAEYMIVPPQ-VLKvdglnrIPDDVDFDEASaaePFACA-I---NAQEQLGIE 165
Cdd:cd05283   98 SGEEQYCPKGVVTYNGKYpdgtitqGGYADHIVVDERfVFK------IPEGLDSAAAA---PLLCAgItvySPLKRNGVG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 166 KGDFLVIFGAGPIGCMHTRIAR--GVHkvgtIVMIDIN----AERLAMSAaavkpDITIDGSQEDVVAKVmeltnGRGAD 239
Cdd:cd05283  169 PGKRVGVVGIGGLGHLAVKFAKalGAE----VTAFSRSpskkEDALKLGA-----DEFIATKDPEAMKKA-----AGSLD 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 240 VIITATPANITQEQALSMAARNGRISFFgGLPKTNPTITcDSNLIHyRQLHIHGANGSAPEHNKRALQYIAsgqvpVKDL 319
Cdd:cd05283  235 LIIDTVSASHDLDPYLSLLKPGGTLVLV-GAPEEPLPVP-PFPLIF-GRKSVAGSLIGGRKETQEMLDFAA-----EHGI 306

                        330       340
                 ....*....|....*....|....
gi 488471907 320 --ITRHVKLDDVMTVFDIVAKGEA 341
Cdd:cd05283  307 kpWVEVIPMDGINEALERLEKGDV 330
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 7-181 1.26e-17

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 82.43  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   7 HAPEDVRLEDvPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVT---TMGHEVAGEIVEIGSEvagDWKVGDWVQ 83
Cdd:PRK09880  11 AGKKDVAVTE-QEIEWNNNGTLVQITRGGICGSDLHYYQEGKVGNFVIKapmVLGHEVIGKIVHSDSS---GLKEGQTVA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  84 SIAAVPCGQCHECRKGWMQVCQNQTSVGY-QY----DGGFAEYMIVPP-QVLKVDglnripDDVDFDEASAAEPFACAIN 157
Cdd:PRK09880  87 INPSKPCGHCKYCLSHNENQCTTMRFFGSaMYfphvDGGFTRYKVVDTaQCIPYP------EKADEKVMAFAEPLAVAIH 160

                        170       180
                 ....*....|....*....|....
gi 488471907 158 AQEQLGIEKGDFLVIFGAGPIGCM 181
Cdd:PRK09880 161 AAHQAGDLQGKRVFVSGVGPIGCL 184
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-271 1.46e-17

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


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 82.26  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLE--DVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVT---TMGHEVAGEIVEIGSEVaGD 75
Cdd:cd08267    1 VVYTRYGSPEVLLLLevEVPIPTPKPGEVLVKVHAASVNPVDWKLRRGPPKLLLGRPfppIPGMDFAGEVVAVGSGV-TR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  76 WKVGDwvqsiaAVPcgqchecrkGWMQVCQNqtsvgyqydGGFAEYMIVPPqvlkvDGLNRIPDDVDFDEASAAePFAcA 155
Cdd:cd08267   80 FKVGD------EVF---------GRLPPKGG---------GALAEYVVAPE-----SGLAKKPEGVSFEEAAAL-PVA-G 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 156 INA----QEQLGIEKGDFLVIFGA-GPIGCMHTRIAR--GVHKVGtiVMIDINAErLAMSAAAvkpDITIDGSQEDVVAk 228
Cdd:cd08267  129 LTAlqalRDAGKVKPGQRVLINGAsGGVGTFAVQIAKalGAHVTG--VCSTRNAE-LVRSLGA---DEVIDYTTEDFVA- 201

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 488471907 229 vmELTNGRGADVII-TATPANITQEQALSMAARNGRISFFGGLP 271
Cdd:cd08267  202 --LTAGGEKYDVIFdAVGNSPFSLYRASLALKPGGRYVSVGGGP 243
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
177-311 2.50e-17

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 77.26  E-value: 2.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  177 PIGCMHTRIAR--GVHkvgtIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMELTNGRGADVIITATPANITQEQA 254
Cdd:pfam00107   1 GVGLAAIQLAKaaGAK----VIAVDGSEEKLEL-AKELGADHVINPKETDLVEEIKELTGGKGVDVVFDCVGSPATLEQA 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 488471907  255 LSMAARNGRISFFGGLPKTNPtitCDSNLIHYRQLHIHGANGSAPEHNKRALQYIAS 311
Cdd:pfam00107  76 LKLLRPGGRVVVVGLPGGPLP---LPLAPLLLKELTILGSFLGSPEEFPEALDLLAS 129
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
 2-198 3.69e-17

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: 81.16  E-value: 3.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   2 KALRFH---APEDVRLEDVPEPEC-KPDEIKIKVRNCSTCGTDVKIlHNGHQNITGVT--TMGHEVAGEIVEIGSEVAGD 75
Cdd:cd08247    2 KALTFKnntSPLTITTIKLPLPNCyKDNEIVVKVHAAALNPVDLKL-YNSYTFHFKVKekGLGRDYSGVIVKVGSNVASE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  76 WKVGDWVQSIAAVPcgqchecrkgwmqvcqnqtsvgYQYDGGFAEYMIVPPQVLKVDgLNRIPDDVDFDEASAAeP--FA 153
Cdd:cd08247   81 WKVGDEVCGIYPHP----------------------YGGQGTLSQYLLVDPKKDKKS-ITRKPENISLEEAAAW-PlvLG 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488471907 154 CAINAQEQLGIEKGD---FLVIFGAGPIGCMHTRIARGVHKVGTIVMI 198
Cdd:cd08247  137 TAYQILEDLGQKLGPdskVLVLGGSTSVGRFAIQLAKNHYNIGTVVGT 184
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 1-148 5.89e-17

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: 80.71  E-value: 5.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAPEDVRLE--DVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGvTTMGHEVAGEIVEIGSEVAGdWKV 78
Cdd:cd08249    1 QKAAVLTGPGGGLLVvvDVPVPKPGPDEVLVKVKAVALNPVDWKHQDYGFIPSYP-AILGCDFAGTVVEVGSGVTR-FKV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  79 GDWVqsiaavpCGQCHECRkgwmqvcqnqtsVGYQYDGGFAEYMIVPPQVLKvdglnRIPDDVDFDEASA 148
Cdd:cd08249   79 GDRV-------AGFVHGGN------------PNDPRNGAFQEYVVADADLTA-----KIPDNISFEEAAT 124
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-347 1.80e-16

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 79.14  E-value: 1.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKAL---RFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKIlHNGH----QNITGVTtmGHEVAGEIVEIGSEVA 73
Cdd:cd08272    1 MKALvleSFGGPEVFELREVPRPQPGPGQVLVRVHASGVNPLDTKI-RRGGaaarPPLPAIL--GCDVAGVVEAVGEGVT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  74 gDWKVGDWV----QSIAAVPcgqchecrkgwmqvcqnqtsvgyqydGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEAsAA 149
Cdd:cd08272   78 -RFRVGDEVygcaGGLGGLQ--------------------------GSLAEYAVVD-----ARLLALKPANLSMREA-AA 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 150 EPFAcAINAQEQL----GIEKGDFLVIF-GAGPIGCMHTRIARGVhkvGTIVMIDINAERLAMsAAAVKPDITIDgSQED 224
Cdd:cd08272  125 LPLV-GITAWEGLvdraAVQAGQTVLIHgGAGGVGHVAVQLAKAA---GARVYATASSEKAAF-ARSLGADPIIY-YRET 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 225 VVAKVMELTNGRGADVII-TATPANItqEQALSMAARNGRISffgglpKTNPTITCDSNLIHYRQLHIHG-------ANG 296
Cdd:cd08272  199 VVEYVAEHTGGRGFDVVFdTVGGETL--DASFEAVALYGRVV------SILGGATHDLAPLSFRNATYSGvftllplLTG 270

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488471907 297 SAPEHNKRAL----QYIASGQV-PVKDLITRHvkLDDVMTVFDIVAKGEAI-KVTVE 347
Cdd:cd08272  271 EGRAHHGEILreaaRLVERGQLrPLLDPRTFP--LEEAAAAHARLESGSARgKIVID 325
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
 24-272 1.36e-14

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 73.68  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  24 PDEIKIKVRNCSTCGTDVKILHN--GHQNITGVTtmGHEVAGEIVEIGSEVAgDWKVGDWVQSIAAV-PCGQCHECRKGW 100
Cdd:PLN02514  34 PEDVVIKVIYCGICHTDLHQIKNdlGMSNYPMVP--GHEVVGEVVEVGSDVS-KFTVGDIVGVGVIVgCCGECSPCKSDL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 101 MQVCQNQT-------SVGYQYDGGFAEYMIVpPQVLKVdglnRIPDDVDFDEASaaePFACA-INAQEQL----GIEKGD 168
Cdd:PLN02514 111 EQYCNKRIwsyndvyTDGKPTQGGFASAMVV-DQKFVV----KIPEGMAPEQAA---PLLCAgVTVYSPLshfgLKQSGL 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 169 FLVIFGAGPIGCMHTRIARGV-HKVGTIvmidinaerlamSAAAVKPDITID--GSQEDVV----AKVMELTNgrGADVI 241
Cdd:PLN02514 183 RGGILGLGGVGHMGVKIAKAMgHHVTVI------------SSSDKKREEALEhlGADDYLVssdaAEMQEAAD--SLDYI 248

                        250       260       270
                 ....*....|....*....|....*....|.
gi 488471907 242 ITATPANITQEQALSMAARNGRISFFGGLPK 272
Cdd:PLN02514 249 IDTVPVFHPLEPYLSLLKLDGKLILMGVINT 279
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 1-268 1.07e-11

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: 65.08  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHA---PEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKI---LHNGHQNITGVTTMGHEVAGEIVEIGSEVAG 74
Cdd:cd08244    1 MRAIRLHEfgpPEVLVPEDVPDPVPGPGQVRIAVAAAGVHFVDTQLrsgWGPGPFPPELPYVPGGEVAGVVDAVGPGVDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  75 DWkVGDWVqsIAAVPCGqchecrkgwmqvcqnqtsvgyqyDGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEASA-AEPFA 153
Cdd:cd08244   81 AW-LGRRV--VAHTGRA-----------------------GGGYAELAVAD-----VDSLHPVPDGLDLEAAVAvVHDGR 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 154 CAINAQEQLGIEKGDFLVIFGA-GPIGCMHTRIARGVHkvGTIVMIDINAERLAMsAAAVKPDITIDGSQEDVVAKVMEL 232
Cdd:cd08244  130 TALGLLDLATLTPGDVVLVTAAaGGLGSLLVQLAKAAG--ATVVGAAGGPAKTAL-VRALGADVAVDYTRPDWPDQVREA 206

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 488471907 233 TNGRGADVIITATPANITQEqALSMAARNGRISFFG 268
Cdd:cd08244  207 LGGGGVTVVLDGVGGAIGRA-ALALLAPGGRFLTYG 241
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 5-269 2.13e-11

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


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 64.14  E-value: 2.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   5 RFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILH-NGHQNITGVTTMGHEVAGEIVEIGSEVAGDwKVGDWVq 83
Cdd:cd08275    7 GFGGLDKLKVEKEALPEPSSGEVRVRVEACGLNFADLMARQgLYDSAPKPPFVPGFECAGTVEAVGEGVKDF-KVGDRV- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  84 siaavpcgqchecrkgwmqvcqnqtsVGYQYDGGFAEYMIVPP-QVLKvdglnrIPDDVDFDEAsAAEP--FACAINAQE 160
Cdd:cd08275   85 --------------------------MGLTRFGGYAEVVNVPAdQVFP------LPDGMSFEEA-AAFPvnYLTAYYALF 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 161 QLG-IEKGDFLVIFGA-GPIGCMHTRIARGVHKVGTivmIDINAERLAMSAAAVKPDITIDGSQEDVVAKVMELTnGRGA 238
Cdd:cd08275  132 ELGnLRPGQSVLVHSAaGGVGLAAGQLCKTVPNVTV---VGTASASKHEALKENGVTHVIDYRTQDYVEEVKKIS-PEGV 207

                        250       260       270
                 ....*....|....*....|....*....|.
gi 488471907 239 DVIITATpANITQEQALSMAARNGRISFFGG 269
Cdd:cd08275  208 DIVLDAL-GGEDTRKSYDLLKPMGRLVVYGA 237
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 23-346 3.18e-11

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: 63.90  E-value: 3.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  23 KPDEIKIKVRNCSTCGTDVKILhNGHQNITGVTTMGHEVAGEIVEIGSEVAgDWKVGDWVQSIAAVPCGQCHECRKGWMQ 102
Cdd:cd08277   26 KANEVRIKMLATSVCHTDILAI-EGFKATLFPVILGHEGAGIVESVGEGVT-NLKPGDKVIPLFIGQCGECSNCRSGKTN 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 103 VCQNQ--TSVGYQYDG------------------GFAEYMIVPPQ-VLKVDglnripDDVDFDEASAaepFACAIN---- 157
Cdd:cd08277  104 LCQKYraNESGLMPDGtsrftckgkkiyhflgtsTFSQYTVVDENyVAKID------PAAPLEHVCL---LGCGFStgyg 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 158 -AQEQLGIEKGDFLVIFGAGPIG---CMHTRIArgvhKVGTIVMIDINAERLAMSAAAVKPD-ITIDGSQEDVVAKVMEL 232
Cdd:cd08277  175 aAWNTAKVEPGSTVAVFGLGAVGlsaIMGAKIA----GASRIIGVDINEDKFEKAKEFGATDfINPKDSDKPVSEVIREM 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 233 TNGrGADVIITATPANITQEQALSMAARNGRISFFGGLPKTNPTITCDSNLIHYRQLH--IHGANGSAPEHNKRALQYiA 310
Cdd:cd08277  251 TGG-GVDYSFECTGNADLMNEALESTKLGWGVSVVVGVPPGAELSIRPFQLILGRTWKgsFFGGFKSRSDVPKLVSKY-M 328

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 488471907 311 SGQVPVKDLITRHVKLDDVMTVFDIVAKGEAIKVTV 346
Cdd:cd08277  329 NKKFDLDELITHVLPFEEINKGFDLMKSGECIRTVI 364
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
 5-314 4.71e-11

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


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 63.20  E-value: 4.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   5 RFHAPED-VRLEDVPEPECKPDEIKIKVR----NCSTCGT------DVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVA 73
Cdd:cd08246   22 RYGDPAQaIQLEDVPVPELGPGEVLVAVMaagvNYNNVWAalgepvSTFAARQRRGRDEPYHIGGSDASGIVWAVGEGVK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  74 GdWKVGDWVQSIAAVPCGQCHECRKGWMQVCQNQTSVGYQY-DGGFAEYMIVPP-QVLKVdglnriPDDVDFDEASAaeP 151
Cdd:cd08246  102 N-WKVGDEVVVHCSVWDGNDPERAGGDPMFDPSQRIWGYETnYGSFAQFALVQAtQLMPK------PKHLSWEEAAA--Y 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 152 FACAINAQEQL------GIEKGDFLVIFGA-GPIGCMHTRIARGVHKVGTIVMIDINAERLAMSAAA------------- 211
Cdd:cd08246  173 MLVGATAYRMLfgwnpnTVKPGDNVLIWGAsGGLGSMAIQLARAAGANPVAVVSSEEKAEYCRALGAegvinrrdfdhwg 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 212 VKPDITIDGSQEDVVA------KVMELTNGRGADVIITATPANITQEQALSMAARNGRISFFGGlpKTNPTITCDSNLIH 285
Cdd:cd08246  253 VLPDVNSEAYTAWTKEarrfgkAIWDILGGREDPDIVFEHPGRATFPTSVFVCDRGGMVVICAG--TTGYNHTYDNRYLW 330

                        330       340
                 ....*....|....*....|....*....
gi 488471907 286 YRQLHIHGANGSAPEHNKRALQYIASGQV 314
Cdd:cd08246  331 MRQKRIQGSHFANDREAAEANRLVMKGRI 359
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 16-263 9.87e-11

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


Pssm-ID: 176213 [Multi-domain]  Cd Length: 303  Bit Score: 61.67  E-value: 9.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  16 DVPEPEckPDEIKIKVRNCSTCGTD---VKILHNGHQNITgvTTMGHEVAGEIVEIGSEVAgDWKVGDWVQSIAAVPCgq 92
Cdd:cd08251    1 EVAPPG--PGEVRIQVRAFSLNFGDllcVRGLYPTMPPYP--FTPGFEASGVVRAVGPHVT-RLAVGDEVIAGTGESM-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  93 checrkgwmqvcqnqtsvgyqydGGFAEYMIVPPqvlkvDGLNRIPDDVDFDEASAAeP--FACAINAQEQLGIEKGDFL 170
Cdd:cd08251   74 -----------------------GGHATLVTVPE-----DQVVRKPASLSFEEACAL-PvvFLTVIDAFARAGLAKGEHI 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 171 VIFGA-GPIGCMHTRIARgvHKVGTIVMIDINAERLAMSAAAVKPDiTIDGSQEDVVAKVMELTNGRGADVIITATPANI 249
Cdd:cd08251  125 LIQTAtGGTGLMAVQLAR--LKGAEIYATASSDDKLEYLKQLGVPH-VINYVEEDFEEEIMRLTGGRGVDVVINTLSGEA 201

                        250
                 ....*....|....
gi 488471907 250 TQeQALSMAARNGR 263
Cdd:cd08251  202 IQ-KGLNCLAPGGR 214
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 1-175 2.38e-10

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: 60.70  E-value: 2.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHA---PEDVRLEDVPEPECKPDEIKIKVR----NCSTCGTdvkilHNGHQN-ITGVTTMGHEVAGEIVEIGSev 72
Cdd:cd08243    1 MKAIVIEQpggPEVLKLREIPIPEPKPGWVLIRVKafglNRSEIFT-----RQGHSPsVKFPRVLGIEAVGEVEEAPG-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  73 aGDWKVGDWVQSIAavpcgqchecrkGWMqvcqnqtsvGYQYDGGFAEYMIVPpqvlkVDGLNRIPDDVDFDE-ASAAEP 151
Cdd:cd08243   74 -GTFTPGQRVATAM------------GGM---------GRTFDGSYAEYTLVP-----NEQVYAIDSDLSWAElAALPET 126

                        170       180
                 ....*....|....*....|....*
gi 488471907 152 FACAINA-QEQLGIEKGDFLVIFGA 175
Cdd:cd08243  127 YYTAWGSlFRSLGLQPGDTLLIRGG 151
PLN02827 PLN02827
Alcohol dehydrogenase-like
 3-346 7.54e-10

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 59.53  E-value: 7.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   3 ALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHnghQNITGVTTMGHEVAGEIVEIGSEVAgDWKVGDWV 82
Cdd:PLN02827  16 AVAWGAGEALVMEEVEVSPPQPLEIRIKVVSTSLCRSDLSAWE---SQALFPRIFGHEASGIVESIGEGVT-EFEKGDHV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  83 QSIAAVPCGQCHECRKGWMQVCQ---------------NQTSVG----YQYDG--GFAEYMIVPPQ-VLKVDGLNRIpDD 140
Cdd:PLN02827  92 LTVFTGECGSCRHCISGKSNMCQvlglerkgvmhsdqkTRFSIKgkpvYHYCAvsSFSEYTVVHSGcAVKVDPLAPL-HK 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 141 VDFDEASAAEPFACAINAQEqlgIEKGDFLVIFGAGPIGcmhTRIARGVHKVGT--IVMIDINAERLAMSAA-AVKPDIT 217
Cdd:PLN02827 171 ICLLSCGVAAGLGAAWNVAD---VSKGSSVVIFGLGTVG---LSVAQGAKLRGAsqIIGVDINPEKAEKAKTfGVTDFIN 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 218 IDGSQEDVVAKVMELTNGrGADVIITATPANITQEQALSMAARNGRISFFGGLPKTNPTITCDSNL-IHYRQLHIHGANG 296
Cdd:PLN02827 245 PNDLSEPIQQVIKRMTGG-GADYSFECVGDTGIATTALQSCSDGWGLTVTLGVPKAKPEVSAHYGLfLSGRTLKGSLFGG 323

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488471907 297 SAPEHNKRAL-QYIASGQVPVKDLITRHVKLDDVMTVFDIVAKGEAIKVTV 346
Cdd:PLN02827 324 WKPKSDLPSLvDKYMNKEIMIDEFITHNLSFDEINKAFELMREGKCLRCVI 374
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 25-264 1.48e-09

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: 58.35  E-value: 1.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  25 DEIKIKVRNCSTCGTDVKILHNghQNITGVTTMGHEVAGEIVEIGSEVAgDWKVGDWVQSIAAvpcgqchecrkgwmqvc 104
Cdd:cd05195    1 DEVEVEVKAAGLNFRDVLVALG--LLPGDETPLGLECSGIVTRVGSGVT-GLKVGDRVMGLAP----------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 105 qnqtsvgyqydGGFAEYMIVPPQVLKvdglnRIPDDVDFDEASA-AEPFACAINAQEQLG-IEKGDF-LVIFGAGPIGCM 181
Cdd:cd05195   61 -----------GAFATHVRVDARLVV-----KIPDSLSFEEAATlPVAYLTAYYALVDLArLQKGESvLIHAAAGGVGQA 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 182 HTRIARGV-HKVgtIVMIDINAERLAMSAAAVKPDITIDGSQEDVVAKVMELTNGRGADVIITATPANITQEqALSMAAR 260
Cdd:cd05195  125 AIQLAQHLgAEV--FATVGSEEKREFLRELGGPVDHIFSSRDLSFADGILRATGGRGVDVVLNSLSGELLRA-SWRCLAP 201


                 ....
gi 488471907 261 NGRI 264
Cdd:cd05195  202 FGRF 205
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 15-316 2.14e-09

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


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 58.08  E-value: 2.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  15 EDVPEPECKPDEIKIKVRNCSTCGTDVK--------------ILHNGHQNITGVTTM------GHEVAGEIVEIGSEVAG 74
Cdd:cd08274   19 DDVPVPTPAPGEVLIRVGACGVNNTDINtregwystevdgatDSTGAGEAGWWGGTLsfpriqGADIVGRVVAVGEGVDT 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  75 dWKVGDWV---QSIAAVPCGQCHECRkgwmqvcqnqtSVGYQYDGGFAEYMIVPPQvlkvdglNRIPDDVDFDEASAAEp 151
Cdd:cd08274   99 -ARIGERVlvdPSIRDPPEDDPADID-----------YIGSERDGGFAEYTVVPAE-------NAYPVNSPLSDVELAT- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 152 FAC----AINAQEQLGIEKGDFLVIFGA-GPIGCMHTRIARGV-HKVGTIVMIDINAERLAMSAaavkpDITIDGSQEDV 225
Cdd:cd08274  159 FPCsystAENMLERAGVGAGETVLVTGAsGGVGSALVQLAKRRgAIVIAVAGAAKEEAVRALGA-----DTVILRDAPLL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 226 VAKVMelTNGRGADVIITATPANITQEqALSMAARNGRISFFGGLpkTNPTITCDSNLIHYRQLHIHGANGSAPEHNKRA 305
Cdd:cd08274  234 ADAKA--LGGEPVDVVADVVGGPLFPD-LLRLLRPGGRYVTAGAI--AGPVVELDLRTLYLKDLTLFGSTLGTREVFRRL 308

                        330
                 ....*....|..
gi 488471907 306 LQYIASGQV-PV 316
Cdd:cd08274  309 VRYIEEGEIrPV 320
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
 5-348 6.62e-09

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: 56.57  E-value: 6.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   5 RFHAPEDV-RLEDVPEPECKPDEIKIKVRNCStcgtdvkiLHNGH-QNITGvtTMGHE-VAGEIVeiGSEVAG--DwKVG 79
Cdd:cd08292    8 QFGDPADVlEIGEVPKPTPGAGEVLVRTTLSP--------IHNHDlWTIRG--TYGYKpELPAIG--GSEAVGvvD-AVG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  80 DWVQSIaavpcgqchecrkgwmQVCQNQTSVGYQydGGFAEYMIVPpqvlkVDGLNRIPDDVDfDEASA---AEPFAcAI 156
Cdd:cd08292   75 EGVKGL----------------QVGQRVAVAPVH--GTWAEYFVAP-----ADGLVPLPDGIS-DEVAAqliAMPLS-AL 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 157 NAQEQLGIEKGDFLVIFGA-GPIGCMHTRIA--RGVHKVGtIVMIDINAERLamsaAAVKPDITIDGSQEDVVAKVMELT 233
Cdd:cd08292  130 MLLDFLGVKPGQWLIQNAAgGAVGKLVAMLAaaRGINVIN-LVRRDAGVAEL----RALGIGPVVSTEQPGWQDKVREAA 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 234 NGRGADVIITATPANITqEQALSMAARNGRISFFGGLpkTNPTITCDSNLIHYRQLHIHGANGS-----APEHNKRALqy 308
Cdd:cd08292  205 GGAPISVALDSVGGKLA-GELLSLLGEGGTLVSFGSM--SGEPMQISSGDLIFKQATVRGFWGGrwsqeMSVEYRKRM-- 279

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 488471907 309 iasgqvpVKDLITRHVK---LDDVMTVFDIVAKGEAIKVTVEP 348
Cdd:cd08292  280 -------IAELLTLALKgqlLLPVEAVFDLGDAAKAAAASMRP 315
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 8-343 1.29e-07

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: 52.68  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   8 APEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGeIVE-IGSEVAgDWKVGDWVQSIA 86
Cdd:cd08301   11 AGKPLVIEEVEVAPPQAMEVRIKILHTSLCHTDVYFWEAKGQTPLFPRILGHEAAG-IVEsVGEGVT-DLKPGDHVLPVF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  87 AVPCGQCHECRKGWMQVCQ----NQTSVGYQYDGG------------------FAEYMIV-PPQVLKVDglnripDDVDF 143
Cdd:cd08301   89 TGECKECRHCKSEKSNMCDllriNTDRGVMINDGKsrfsingkpiyhfvgtstFSEYTVVhVGCVAKIN------PEAPL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 144 DEASAaepFACAINAQeqLG-------IEKGDFLVIFGAGPIGCMhtrIARGVHKVGT--IVMIDINAERLAMS-AAAVK 213
Cdd:cd08301  163 DKVCL---LSCGVSTG--LGaawnvakVKKGSTVAIFGLGAVGLA---VAEGARIRGAsrIIGVDLNPSKFEQAkKFGVT 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 214 PDITIDGSQEDVVAKVMELTNGrGADVIITATPANITQEQALSMAARNGRISFFGGLPKTNPTITCDS-NLIHYRQLHIH 292
Cdd:cd08301  235 EFVNPKDHDKPVQEVIAEMTGG-GVDYSFECTGNIDAMISAFECVHDGWGVTVLLGVPHKDAVFSTHPmNLLNGRTLKGT 313

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488471907 293 GANGSAPEHNKRAL--QYIaSGQVPVKDLITRHVKLDDVMTVFDIVAKGEAIK 343
Cdd:cd08301  314 LFGGYKPKTDLPNLveKYM-KKELELEKFITHELPFSEINKAFDLLLKGECLR 365
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 1-194 2.11e-07

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: 51.84  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHA---PEDVR-LEDVPEPE-CKPDEIKIKVRNCSTCGTDVKI---------------LHNGHQNITGVTTMGHE 60
Cdd:cd08248    1 MKAWQIHSyggIDSLLlLENARIPViRKPNQVLIKVHAASVNPIDVLMrsgygrtllnkkrkpQSCKYSGIEFPLTLGRD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  61 VAGEIVEIGSEVaGDWKVGDWVqsIAAVPcgqchecrkGWMQvcqnqtsvgyqydGGFAEYMIVPpqvlkvdgLNRI--- 137
Cdd:cd08248   81 CSGVVVDIGSGV-KSFEIGDEV--WGAVP---------PWSQ-------------GTHAEYVVVP--------ENEVskk 127

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488471907 138 PDDVDFDEAsAAEPFAC--AINAQEQLGIEKGDF------LVIFGAGPIGCMHTRIAR--GVHKVGT 194
Cdd:cd08248  128 PKNLSHEEA-ASLPYAGltAWSALVNVGGLNPKNaagkrvLILGGSGGVGTFAIQLLKawGAHVTTT 193
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
 1-194 2.70e-07

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


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 51.76  E-value: 2.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHAP----EDVRLED--VPEPECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAG 74
Cdd:cd08252    1 MKAIGFTQPlpitDPDSLIDieLPKPVPGGRDLLVRVEAVSVNPVDTKVRAGGAPVPGQPKILGWDASGVVEAVGSEVTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  75 DwKVGDWVqsiaavpcgqchecrkgWmqvcqnqtsvgyqYDGGF------AEYmivppQVlkVDglNRI----PDDVDFD 144
Cdd:cd08252   81 F-KVGDEV-----------------Y-------------YAGDItrpgsnAEY-----QL--VD--ERIvghkPKSLSFA 120

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488471907 145 EAsAAEPFAcAINAQE----QLGI------EKGDFLVIFGAGPIGCMHTRIAR---GVHKVGT 194
Cdd:cd08252  121 EA-AALPLT-SLTAWEalfdRLGIsedaenEGKTLLIIGGAGGVGSIAIQLAKqltGLTVIAT 181
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
 21-195 5.04e-06

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 47.95  E-value: 5.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  21 ECKPDEIKIKVRNCSTCGTDVKILHNGHQNITGVTTMGHEVAGEIVEIGSEVAgDWKVGDWVQ-SIAAVPCGQCHECRKG 99
Cdd:PLN02586  34 ENGDEDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGKNVK-KFKEGDRVGvGVIVGSCKSCESCDQD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 100 WMQVC-------QNQTSVGYQYDGGFAEyMIVPPQVLKVdglnRIPDDVDFDeasAAEPFACA----INAQEQLGI-EKG 167
Cdd:PLN02586 113 LENYCpkmiftyNSIGHDGTKNYGGYSD-MIVVDQHFVL----RFPDNLPLD---AGAPLLCAgitvYSPMKYYGMtEPG 184

                        170       180
                 ....*....|....*....|....*....
gi 488471907 168 DFLVIFGAGPIGCMHTRIARGV-HKVGTI 195
Cdd:PLN02586 185 KHLGVAGLGGLGHVAVKIGKAFgLKVTVI 213
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
 3-239 8.58e-06

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: 47.22  E-value: 8.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   3 ALRFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILhNGHqNITGV--TTMGHEVAGEIVEIGSEVAgDWKVGD 80
Cdd:cd08300    6 AVAWEAGKPLSIEEVEVAPPKAGEVRIKILATGVCHTDAYTL-SGA-DPEGLfpVILGHEGAGIVESVGEGVT-SVKPGD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  81 WVQSIAAVPCGQCHECRKGWMQVCQ---NQTSVGYQYDG------------------GFAEYMIVPPQvlkvdGLNRIPD 139
Cdd:cd08300   83 HVIPLYTPECGECKFCKSGKTNLCQkirATQGKGLMPDGtsrfsckgkpiyhfmgtsTFSEYTVVAEI-----SVAKINP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 140 DVDFDEASAaepFACAIN-----AQEQLGIEKGDFLVIFGAGPIG---CMHTRIArgvhKVGTIVMIDINAERLAMsaaA 211
Cdd:cd08300  158 EAPLDKVCL---LGCGVTtgygaVLNTAKVEPGSTVAVFGLGAVGlavIQGAKAA----GASRIIGIDINPDKFEL---A 227

                        250       260       270
                 ....*....|....*....|....*....|..
gi 488471907 212 VKPDIT--IDGS--QEDVVAKVMELTNGrGAD 239
Cdd:cd08300  228 KKFGATdcVNPKdhDKPIQQVLVEMTDG-GVD 258
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 1-343 9.15e-06

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 46.95  E-value: 9.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKAL---RFHAPEDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILHN------GHQNItgvttMGHEVAGEIVEIGSE 71
Cdd:PTZ00354   2 MRAVtlkGFGGVDVLKIGESPKPAPKRNDVLIKVSAAGVNRADTLQRQGkyppppGSSEI-----LGLEVAGYVEDVGSD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  72 VaGDWKVGDWVQSIAAvpcgqchecrkgwmqvcqnqtsvgyqyDGGFAEYMIVPP-QVLKvdglnrIPDDVDFDEASA-A 149
Cdd:PTZ00354  77 V-KRFKEGDRVMALLP---------------------------GGGYAEYAVAHKgHVMH------IPQGYTFEEAAAiP 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 150 EPFACAINAQEQLG-IEKGDFLVIF-GAGPIGcmhTRIARGVHKVGTIVMIDINAE-RLAMSAAAVKPDITIDGSQEDVV 226
Cdd:PTZ00354 123 EAFLTAWQLLKKHGdVKKGQSVLIHaGASGVG---TAAAQLAEKYGAATIITTSSEeKVDFCKKLAAIILIRYPDEEGFA 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 227 AKVMELTNGRGADVIITATPANITQEQALSMaARNGR---ISFFGGLPKTNPTITcdsNLIHYRqLHIHGAN-------- 295
Cdd:PTZ00354 200 PKVKKLTGEKGVNLVLDCVGGSYLSETAEVL-AVDGKwivYGFMGGAKVEKFNLL---PLLRKR-ASIIFSTlrsrsdey 274

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488471907 296 --GSAPEHNKRALQYIASGQV--------PVKDLITRHVKLDDVMTVFDIVAKGEAIK 343
Cdd:PTZ00354 275 kaDLVASFEREVLPYMEEGEIkpivdrtyPLEEVAEAHTFLEQNKNIGKVVLTVNEPL 332
PLN02740 PLN02740
Alcohol dehydrogenase-like
 2-239 2.97e-05

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 45.56  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   2 KALRFHAP-EDVRLEDVPEPECKPDEIKIKVRNCSTCGTDVKILhNGHQNITGV--TTMGHEVAGeIVEIGSEVAGDWKV 78
Cdd:PLN02740  12 KAAVAWGPgEPLVMEEIRVDPPQKMEVRIKILYTSICHTDLSAW-KGENEAQRAypRILGHEAAG-IVESVGEGVEDLKA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  79 GDWVQSIAAVPCGQCHECRKGWMQVCQ----NQTSVGYQYDGG--------------------FAEYMIVPPQ-VLKVDG 133
Cdd:PLN02740  90 GDHVIPIFNGECGDCRYCKRDKTNLCEtyrvDPFKSVMVNDGKtrfstkgdgqpiyhflntstFTEYTVLDSAcVVKIDP 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 134 LNRIpDDVDFDEASAAEPFACAINAQEqlgIEKGDFLVIFGAGPIGCMhtrIARGVHKVGT--IVMIDINAERLAMSAAA 211
Cdd:PLN02740 170 NAPL-KKMSLLSCGVSTGVGAAWNTAN---VQAGSSVAIFGLGAVGLA---VAEGARARGAskIIGVDINPEKFEKGKEM 242

                        250       260
                 ....*....|....*....|....*....
gi 488471907 212 VKPD-ITIDGSQEDVVAKVMELTNGrGAD 239
Cdd:PLN02740 243 GITDfINPKDSDKPVHERIREMTGG-GVD 270
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
 1-149 3.50e-05

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: 44.90  E-value: 3.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907   1 MKALRFHA------PEDVRLEDVPEPECKPDEIKIKVR----NCStcgtDVKILhNGHQNITGV--TTMGHEVAGEIVEI 68
Cdd:cd08291    1 MKALLLEEygkpleVKELSLPEPEVPEPGPGEVLIKVEaapiNPS----DLGFL-KGQYGSTKAlpVPPGFEGSGTVVAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  69 GSEVAGDWKVGdwvQSIAAVPCGqchecrkgwmqvcqnqtsvgyqyDGGFAEYMIVPP-QVLKvdglnrIPDDVDFDEAS 147
Cdd:cd08291   76 GGGPLAQSLIG---KRVAFLAGS-----------------------YGTYAEYAVADAqQCLP------LPDGVSFEQGA 123


                 ..
gi 488471907 148 AA 149
Cdd:cd08291  124 SS 125
ribitol-5-phosphate_DH cd08237
ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of ...
 57-311 4.30e-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: 4.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  57 MGHEVAGEIVeigSEVAGDWKVGDWVQSIAAVPCGQCHECRKGWMQVCQNQTSvgyQYDGGFAEYMIVPPqvlkvDGLNR 136
Cdd:cd08237   62 LIHEGIGVVV---SDPTGTYKVGTKVVMVPNTPVEKDEIIPENYLPSSRFRSS---GYDGFMQDYVFLPP-----DRLVK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 137 IPDDVDFDEASAAEPFACAINAQ---EQLGIEKGDFLVIFGAGPIGCMHTRIARGVHKVGTIVMIDINAERLAMSAAAVK 213
Cdd:cd08237  131 LPDNVDPEVAAFTELVSVGVHAIsrfEQIAHKDRNVIGVWGDGNLGYITALLLKQIYPESKLVVFGKHQEKLDLFSFADE 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 214 PDITIDGSQEDVVAKVMELTNGRGADVIItatpanitqEQALSMAARNGRISFFGglpKTNPTITCDSNLIHYRQLHIHG 293
Cdd:cd08237  211 TYLIDDIPEDLAVDHAFECVGGRGSQSAI---------NQIIDYIRPQGTIGLMG---VSEYPVPINTRMVLEKGLTLVG 278

                        250
                 ....*....|....*...
gi 488471907 294 ANGSAPEHNKRALQYIAS 311
Cdd:cd08237  279 SSRSTREDFERAVELLSR 296
OCDMu COG2423
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid ...
 170-247 6.63e-05

Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid transport and metabolism]; Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 441972 [Multi-domain]  Cd Length: 322  Bit Score: 43.98  E-value: 6.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 170 LVIFGAGPIGCMHTRIARGVHKVGTIVMIDIN---AERLAMSAAAVKPDITIDGSQEDVVakvmeltngRGADVIITATP 246
Cdd:COG2423  130 LGIIGAGVQARTQLRALAAVRPIERVRVWGRDpekAEAFAARLAAEGLPVEAADDLEEAV---------ADADIIVTATP 200


                 .
gi 488471907 247 A 247
Cdd:COG2423  201 S 201
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
 23-269 2.21e-03

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: 39.60  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  23 KPDEIKIKVRNCSTCGTDVKILhNGHQNITGVTTMGHEVAGeIVE-IGSEVAgDWKVGDWVQSIAAVPCGQCHECRKGWM 101
Cdd:cd08299   31 KAHEVRIKIVATGICRSDDHVV-SGKLVTPFPVILGHEAAG-IVEsVGEGVT-TVKPGDKVIPLFVPQCGKCRACLNPES 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 102 QVC---QNQTSVGYQYDG------------------GFAEYMivppqVLKVDGLNRIPDDVDFDEASA-----AEPFACA 155
Cdd:cd08299  108 NLClknDLGKPQGLMQDGtsrftckgkpihhflgtsTFSEYT-----VVDEIAVAKIDAAAPLEKVCLigcgfSTGYGAA 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907 156 INAQEqlgIEKGDFLVIFGAGP------IGCMHTRIARgvhkvgtIVMIDINAERLA----------------------- 206
Cdd:cd08299  183 VNTAK---VTPGSTCAVFGLGGvglsaiMGCKAAGASR-------IIAVDINKDKFAkakelgatecinpqdykkpiqev 252

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488471907 207 ---MSAAAVKPDITIDGSQEDVVAKVMELTNGRGADVIITATPA--NITQEQALSMAARNGRISFFGG 269
Cdd:cd08299  253 lteMTDGGVDFSFEVIGRLDTMKAALASCHEGYGVSVIVGVPPSsqNLSINPMLLLTGRTWKGAVFGG 320
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 12-148 4.69e-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: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 38.40  E-value: 4.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471907  12 VRLEDVPEPEckPDEIKIKVRNCSTCGTDVKI-LHNGHQNITGVTTMGHEVAGEIVEIGSEVAGdWKVGDWVqsiAAVPC 90
Cdd:cd08273   17 VVEADLPEPA--AGEVVVKVEASGVSFADVQMrRGLYPDQPPLPFTPGYDLVGRVDALGSGVTG-FEVGDRV---AALTR 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488471907  91 GqchecrkgwmqvcqnqtsvgyqydGGFAEYMIVPpqvlkVDGLNRIPDDVDFDEASA 148
Cdd:cd08273   91 V------------------------GGNAEYINLD-----AKYLVPVPEGVDAAEAVC 119
ADH_N_assoc pfam13823
Alcohol dehydrogenase GroES-associated; This short domain is frequently found at the ...
 1-21 6.88e-03

Alcohol dehydrogenase GroES-associated; This short domain is frequently found at the N-terminus of the alcohol dehydrogenase GroES-like domain, Pfam: PF08240.


Pssm-ID: 433504 [Multi-domain]  Cd Length: 23  Bit Score: 33.53  E-value: 6.88e-03
                          10        20
                  ....*....|....*....|.
gi 488471907    1 MKALRFHAPEDVRLEDVPEPE 21
Cdd:pfam13823   1 MKAVTYQGPKDVRVEEVPDPR 21
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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