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Conserved domains on  [gi|2492777|sp|Q04894|]
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RecName: Full=NADP-dependent alcohol dehydrogenase 6; AltName: Full=NADP-dependent alcohol dehydrogenase VI; AltName: Full=S-nitroso-CoA reductase; Short=ScorR; AltName: Full=ScADHVI

Protein Classification

NAD(P)-dependent alcohol dehydrogenase( domain architecture ID 10143012)

NAD(P)-dependent alcohol dehydrogenase catalyzes the reversible conversion of an alcohol to its corresponding aldehyde

CATH:  3.40.50.720|3.90.180.10
EC:  1.1.-.-
Gene Ontology:  GO:0016491

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 8-352 2.37e-156

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: 442.32  E-value: 2.37e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    8 EGIAIQSHEdwKNPKKTKYDPKPFYDHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKV 87
Cdd:cd05283   1 KGYAARDAS--GKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKV-TKFKV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   88 GQRVGVGAQVFSCLECDRCKNDNEPYCTKFVTTYSQPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLT 167
Cdd:cd05283  78 GDRVGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKYPDGTITQGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGIT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  168 VYSPLVRNGCGPGKKvgivglggigsMGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEGDWgEKYFDTFDLI 247
Cdd:cd05283 158 VYSPLKRNGVGPGKRvgvvgigglghLAVKFAKALGAEVTAFSRSPSKKEDALKLGADEFIATKDPEAM-KKAAGSLDLI 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  248 VVCASSltDIDFNIMPKAMKVGGRIVSISIPEQHemLSLKPYGL--KAVSISYSALGSIKELNQLLKLVSEKDIKIWVET 325
Cdd:cd05283 237 IDTVSA--SHDLDPYLSLLKPGGTLVLVGAPEEP--LPVPPFPLifGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEV 312

                       330       340
                ....*....|....*....|....*..
gi 2492777  326 LPVgeAGVHEAFERMEKGDVRYRFTLV 352
Cdd:cd05283 313 IPM--DGINEALERLEKGDVRYRFVLD 337
 
Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 8-352 2.37e-156

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: 442.32  E-value: 2.37e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    8 EGIAIQSHEdwKNPKKTKYDPKPFYDHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKV 87
Cdd:cd05283   1 KGYAARDAS--GKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKV-TKFKV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   88 GQRVGVGAQVFSCLECDRCKNDNEPYCTKFVTTYSQPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLT 167
Cdd:cd05283  78 GDRVGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKYPDGTITQGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGIT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  168 VYSPLVRNGCGPGKKvgivglggigsMGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEGDWgEKYFDTFDLI 247
Cdd:cd05283 158 VYSPLKRNGVGPGKRvgvvgigglghLAVKFAKALGAEVTAFSRSPSKKEDALKLGADEFIATKDPEAM-KKAAGSLDLI 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  248 VVCASSltDIDFNIMPKAMKVGGRIVSISIPEQHemLSLKPYGL--KAVSISYSALGSIKELNQLLKLVSEKDIKIWVET 325
Cdd:cd05283 237 IDTVSA--SHDLDPYLSLLKPGGTLVLVGAPEEP--LPVPPFPLifGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEV 312

                       330       340
                ....*....|....*....|....*..
gi 2492777  326 LPVgeAGVHEAFERMEKGDVRYRFTLV 352
Cdd:cd05283 313 IPM--DGINEALERLEKGDVRYRFVLD 337
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 27-352 5.64e-99

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 296.25  E-value: 5.64e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPfydHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGAqVFSCLECDRC 106
Cdd:COG1064  22 EPGP---GEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGV-TGFKVGDRVGVGW-VDSCGTCEYC 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  107 KNDNEPYCTKFVTTysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPGKKvgiv 186
Cdd:COG1064  97 RSGRENLCENGRFT-------GYTTDGGYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITAYRALRRAGVGPGDRvavi 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  187 glggigSMGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATlEEGDWGEKYFD--TFDLIVVCASSltDIDFNIMPK 264
Cdd:COG1064 170 gagglgHLAVQIAKALGAEVIAVDRSPEKLELARELGADHVVNS-SDEDPVEAVREltGADVVIDTVGA--PATVNAALA 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  265 AMKVGGRIVSISIPEqhEMLSLKPYGL--KAVSISYSALGSIKELNQLLKLVSEKDIKIWVETLPVGEAGvhEAFERMEK 342
Cdd:COG1064 247 LLRRGGRLVLVGLPG--GPIPLPPFDLilKERSIRGSLIGTRADLQEMLDLAAEGKIKPEVETIPLEEAN--EALERLRA 322

                       330
                ....*....|
gi 2492777  343 GDVRYRFTLV 352
Cdd:COG1064 323 GKVRGRAVLD 332
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
 35-351 3.50e-66

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 213.12  E-value: 3.50e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    35 DIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGAQVFSCLECDRCKNDNEPYC 114
Cdd:PLN02514  36 DVVIKVIYCGICHTDLHQIKNDLGMSNYPMVPGHEVVGEVVEVGSDV-SKFTVGDIVGVGVIVGCCGECSPCKSDLEQYC 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   115 TKFVTTYSQPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVR-NGCGPGKKVGIVGLGGIGS 193
Cdd:PLN02514 115 NKRIWSYNDVYTDGKPTQGGFASAMVVDQKFVVKIPEGMAPEQAAPLLCAGVTVYSPLSHfGLKQSGLRGGILGLGGVGH 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   194 MGTLISKAMGAETYVISRSSRKREDAMK-MGADHYIATLEEGDWgEKYFDTFDLIVVCASSLTDIDFNImpKAMKVGGRI 272
Cdd:PLN02514 195 MGVKIAKAMGHHVTVISSSDKKREEALEhLGADDYLVSSDAAEM-QEAADSLDYIIDTVPVFHPLEPYL--SLLKLDGKL 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   273 V---SISIPEQ--HEMLSLkpyGLKAVSISYsaLGSIKELNQLLKLVSEKDIKIWVETLPVGEagVHEAFERMEKGDVRY 347
Cdd:PLN02514 272 IlmgVINTPLQfvTPMLML---GRKVITGSF--IGSMKETEEMLEFCKEKGLTSMIEVVKMDY--VNTAFERLEKNDVRY 344


                 ....
gi 2492777   348 RFTL 351
Cdd:PLN02514 345 RFVV 348
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 34-148 1.22e-36

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: 128.11  E-value: 1.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777     34 HDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPkSNSGLKVGQRVGVGAQVfSCLECDRCKNDNEPY 113
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGP-GVTGLKVGDRVVVEPLI-PCGKCEYCREGRYNL 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2492777    114 CTKFVTTysqpyedGYVSQGGYANYVRVHEHFVVP 148
Cdd:pfam08240  79 CPNGRFL-------GYDRDGGFAEYVVVPERNLVP 106
adh_fam_2 TIGR02822
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
 38-224 4.09e-23

zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct subset of the larger family of oxidoreductases that includes zinc-binding alcohol dehydrogenases and NADPH:quinone reductases (pfam00107). The gene neighborhood of members of this family is not conserved and it appears that no members are characterized. The sequence of the family includes 6 invariant cysteine residues and one invariant histidine. It appears that no member is characterized. [Energy metabolism, Fermentation]


Pssm-ID: 131869 [Multi-domain]  Cd Length: 329  Bit Score: 98.07  E-value: 4.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777     38 IKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGpKSNSGLKVGQRVGVGAQVFSCLECDRCKNDNEPYCTKf 117
Cdd:TIGR02822  32 VRVRACGVCRTDLHVSEGDLPVHRPRVTPGHEVVGEVAGRG-ADAGGFAVGDRVGIAWLRRTCGVCRYCRRGAENLCPA- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    118 vTTYSqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIVGLGGIGSMGTL 197
Cdd:TIGR02822 110 -SRYT-----GWDTDGGYAEYTTVPAAFAYRLPTGYDDVELAPLLCAGIIGYRALLRASLPPGGRLGLYGFGGSAHLTAQ 183

                         170       180
                  ....*....|....*....|....*..
gi 2492777    198 ISKAMGAETYVISRSSRKREDAMKMGA 224
Cdd:TIGR02822 184 VALAQGATVHVMTRGAAARRLALALGA 210
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 38-343 1.07e-08

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 55.47  E-value: 1.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777      38 IKIEACGVCGSDIHCAAGhwgNMKMPLVVGHEIVGKVVKLGPkSNSGLKVGQRVgVGaqvfsclecdrckndnepyctkf 117
Cdd:smart00829   1 IEVRAAGLNFRDVLIALG---LYPGEAVLGGECAGVVTRVGP-GVTGLAVGDRV-MG----------------------- 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777     118 vttysqpyedgyVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVY-------------SPLVRNGCGpgkkvg 184
Cdd:smart00829  53 ------------LAPGAFATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYyalvdlarlrpgeSVLIHAAAG------ 114

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777     185 ivglggigsmGT-----LISKAMGAETYVISRSSRKRE--DAMKMGADHyI--------------ATLEEGdwgekyfdt 243
Cdd:smart00829 115 ----------GVgqaaiQLARHLGAEVFATAGSPEKRDflRALGIPDDH-IfssrdlsfadeilrATGGRG--------- 174

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777     244 FDLIVvcaSSLTDiDFniMPKAMKV---GGRIVSISI-----PEQHEMLSLKPyglkavSISYSA--LGSIKE------- 306
Cdd:smart00829 175 VDVVL---NSLSG-EF--LDASLRClapGGRFVEIGKrdirdNSQLAMAPFRP------NVSYHAvdLDALEEgpdrire 242

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2492777     307 -LNQLLKLVSEKDIK-IWVETLPVGEagVHEAFERMEKG 343
Cdd:smart00829 243 lLAEVLELFAEGVLRpLPVTVFPISD--AEDAFRYMQQG 279
 
Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 8-352 2.37e-156

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: 442.32  E-value: 2.37e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    8 EGIAIQSHEdwKNPKKTKYDPKPFYDHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKV 87
Cdd:cd05283   1 KGYAARDAS--GKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKV-TKFKV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   88 GQRVGVGAQVFSCLECDRCKNDNEPYCTKFVTTYSQPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLT 167
Cdd:cd05283  78 GDRVGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKYPDGTITQGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGIT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  168 VYSPLVRNGCGPGKKvgivglggigsMGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEGDWgEKYFDTFDLI 247
Cdd:cd05283 158 VYSPLKRNGVGPGKRvgvvgigglghLAVKFAKALGAEVTAFSRSPSKKEDALKLGADEFIATKDPEAM-KKAAGSLDLI 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  248 VVCASSltDIDFNIMPKAMKVGGRIVSISIPEQHemLSLKPYGL--KAVSISYSALGSIKELNQLLKLVSEKDIKIWVET 325
Cdd:cd05283 237 IDTVSA--SHDLDPYLSLLKPGGTLVLVGAPEEP--LPVPPFPLifGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEV 312

                       330       340
                ....*....|....*....|....*..
gi 2492777  326 LPVgeAGVHEAFERMEKGDVRYRFTLV 352
Cdd:cd05283 313 IPM--DGINEALERLEKGDVRYRFVLD 337
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 10-351 1.36e-154

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: 437.52  E-value: 1.36e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   10 IAIQSHEDWKNPKKTKYDPKPFYDHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSNsGLKVGQ 89
Cdd:cd08245   1 KAAVVHAAGGPLEPEEVPVPEPGPGEVLIKIEACGVCHTDLHAAEGDWGGSKYPLVPGHEIVGEVVEVGAGVE-GRKVGD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   90 RVGVGAQVFSCLECDRCKNDNEPYCTKFVTTysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVY 169
Cdd:cd08245  80 RVGVGWLVGSCGRCEYCRRGLENLCQKAVNT-------GYTTQGGYAEYMVADAEYTVLLPDGLPLAQAAPLLCAGITVY 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  170 SPLVRNGCGPGKKVGIVGLGGIGSMGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEGDWGEkYFDTFDLIVV 249
Cdd:cd08245 153 SALRDAGPRPGERVAVLGIGGLGHLAVQYARAMGFETVAITRSPDKRELARKLGADEVVDSGAELDEQA-AAGGADVILV 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  250 CASSLTdiDFNIMPKAMKVGGRIVSISIPEQHEMLS-LKPYGLKAVSISYSALGSIKELNQLLKLVSEKDIKIWVETLPV 328
Cdd:cd08245 232 TVVSGA--AAEAALGGLRRGGRIVLVGLPESPPFSPdIFPLIMKRQSIAGSTHGGRADLQEALDFAAEGKVKPMIETFPL 309

                       330       340
                ....*....|....*....|...
gi 2492777  329 geAGVHEAFERMEKGDVRYRFTL 351
Cdd:cd08245 310 --DQANEAYERMEKGDVRFRFVL 330
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 27-352 5.64e-99

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 296.25  E-value: 5.64e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPfydHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGAqVFSCLECDRC 106
Cdd:COG1064  22 EPGP---GEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGV-TGFKVGDRVGVGW-VDSCGTCEYC 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  107 KNDNEPYCTKFVTTysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPGKKvgiv 186
Cdd:COG1064  97 RSGRENLCENGRFT-------GYTTDGGYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITAYRALRRAGVGPGDRvavi 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  187 glggigSMGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATlEEGDWGEKYFD--TFDLIVVCASSltDIDFNIMPK 264
Cdd:COG1064 170 gagglgHLAVQIAKALGAEVIAVDRSPEKLELARELGADHVVNS-SDEDPVEAVREltGADVVIDTVGA--PATVNAALA 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  265 AMKVGGRIVSISIPEqhEMLSLKPYGL--KAVSISYSALGSIKELNQLLKLVSEKDIKIWVETLPVGEAGvhEAFERMEK 342
Cdd:COG1064 247 LLRRGGRLVLVGLPG--GPIPLPPFDLilKERSIRGSLIGTRADLQEMLDLAAEGKIKPEVETIPLEEAN--EALERLRA 322

                       330
                ....*....|
gi 2492777  343 GDVRYRFTLV 352
Cdd:COG1064 323 GKVRGRAVLD 332
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
 35-351 3.50e-66

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 213.12  E-value: 3.50e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    35 DIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGAQVFSCLECDRCKNDNEPYC 114
Cdd:PLN02514  36 DVVIKVIYCGICHTDLHQIKNDLGMSNYPMVPGHEVVGEVVEVGSDV-SKFTVGDIVGVGVIVGCCGECSPCKSDLEQYC 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   115 TKFVTTYSQPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVR-NGCGPGKKVGIVGLGGIGS 193
Cdd:PLN02514 115 NKRIWSYNDVYTDGKPTQGGFASAMVVDQKFVVKIPEGMAPEQAAPLLCAGVTVYSPLSHfGLKQSGLRGGILGLGGVGH 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   194 MGTLISKAMGAETYVISRSSRKREDAMK-MGADHYIATLEEGDWgEKYFDTFDLIVVCASSLTDIDFNImpKAMKVGGRI 272
Cdd:PLN02514 195 MGVKIAKAMGHHVTVISSSDKKREEALEhLGADDYLVSSDAAEM-QEAADSLDYIIDTVPVFHPLEPYL--SLLKLDGKL 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   273 V---SISIPEQ--HEMLSLkpyGLKAVSISYsaLGSIKELNQLLKLVSEKDIKIWVETLPVGEagVHEAFERMEKGDVRY 347
Cdd:PLN02514 272 IlmgVINTPLQfvTPMLML---GRKVITGSF--IGSMKETEEMLEFCKEKGLTSMIEVVKMDY--VNTAFERLEKNDVRY 344


                 ....
gi 2492777   348 RFTL 351
Cdd:PLN02514 345 RFVV 348
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
 33-351 3.58e-64

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 208.19  E-value: 3.58e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    33 DHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGpKSNSGLKVGQRVGVGAQVFSCLECDRCKNDNEP 112
Cdd:PLN02586  37 DEDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLG-KNVKKFKEGDRVGVGVIVGSCKSCESCDQDLEN 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   113 YCTKFVTTYSQPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNG-CGPGKKVGIVGLGGI 191
Cdd:PLN02586 116 YCPKMIFTYNSIGHDGTKNYGGYSDMIVVDQHFVLRFPDNLPLDAGAPLLCAGITVYSPMKYYGmTEPGKHLGVAGLGGL 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   192 GSMGTLISKAMGAETYVISRSSRKREDAM-KMGADHYIATLEEGDWgEKYFDTFDLIVVCASSLTDIdfNIMPKAMKVGG 270
Cdd:PLN02586 196 GHVAVKIGKAFGLKVTVISSSSNKEDEAInRLGADSFLVSTDPEKM-KAAIGTMDYIIDTVSAVHAL--GPLLGLLKVNG 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   271 RIVSISIPEQHEMLSLKPYGLKAVSISYSALGSIKELNQLLKLVSEKDIKIWVETLPVGEagVHEAFERMEKGDVRYRFT 350
Cdd:PLN02586 273 KLITLGLPEKPLELPIFPLVLGRKLVGGSDIGGIKETQEMLDFCAKHNITADIELIRMDE--INTAMERLAKSDVRYRFV 350


                 .
gi 2492777   351 L 351
Cdd:PLN02586 351 I 351
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 28-351 5.33e-59

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: 193.90  E-value: 5.33e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPfYDHDIDIKIEACGVCGSDIHCAAGHWGNM-KMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGAQVFSCLECDRC 106
Cdd:cd08297  22 PEP-GPGEVLVKLEASGVCHTDLHAALGDWPVKpKLPLIGGHEGAGVVVAVGPGV-SGLKVGDRVGVKWLYDACGKCEYC 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  107 KNDNEPYCTKFVTTysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGP------- 179
Cdd:cd08297 100 RTGDETLCPNQKNS-------GYTVDGTFAEYAIADARYVTPIPDGLSFEQAAPLLCAGVTVYKALKKAGLKPgdwvvis 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  180 ------GkkvgivglggigSMGTLISKAMGAETYVISRSSRKREDAMKMGADHYI---------ATLEEGDWGekyfdTF 244
Cdd:cd08297 173 gaggglG------------HLGVQYAKAMGLRVIAIDVGDEKLELAKELGADAFVdfkksddveAVKELTGGG-----GA 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  245 DLIVVCASSLTdiDFNIMPKAMKVGGRIVSISIPEQhEMLSLKPYG--LKAVSISYSALGSIKELNQLLKLVSEKDIKIW 322
Cdd:cd08297 236 HAVVVTAVSAA--AYEQALDYLRPGGTLVCVGLPPG-GFIPLDPFDlvLRGITIVGSLVGTRQDLQEALEFAARGKVKPH 312

                       330       340
                ....*....|....*....|....*....
gi 2492777  323 VETLPVGEAGvhEAFERMEKGDVRYRFTL 351
Cdd:cd08297 313 IQVVPLEDLN--EVFEKMEEGKIAGRVVV 339
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 28-352 1.18e-58

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: 192.84  E-value: 1.18e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPfYDHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPkSNSGLKVGQRVGVGAQVFSCLECDRCK 107
Cdd:cd08296  21 PLP-GPGEVLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVGE-GVSRWKVGDRVGVGWHGGHCGTCDACR 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  108 NDNepyctkFVTTYSQPYeDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIVG 187
Cdd:cd08296  99 RGD------FVHCENGKV-TGVTRDGGYAEYMLAPAEALARIPDDLDAAEAAPLLCAGVTTFNALRNSGAKPGDLVAVQG 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  188 LGGIGSMGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATlEEGDWGEKYFDT--FDLIVVCASSltdidfnimPKA 265
Cdd:cd08296 172 IGGLGHLAVQYAAKMGFRTVAISRGSDKADLARKLGAHHYIDT-SKEDVAEALQELggAKLILATAPN---------AKA 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  266 M-------KVGGRIVSISIPEQHEMLSLKPYGLKAVSISYSALGSIKELNQLLKLVSEKDIKIWVETLPVGEAgvHEAFE 338
Cdd:cd08296 242 IsalvgglAPRGKLLILGAAGEPVAVSPLQLIMGRKSIHGWPSGTALDSEDTLKFSALHGVRPMVETFPLEKA--NEAYD 319

                       330
                ....*....|....
gi 2492777  339 RMEKGDVRYRFTLV 352
Cdd:cd08296 320 RMMSGKARFRVVLT 333
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
 33-351 1.11e-57

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 191.78  E-value: 1.11e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    33 DHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGpKSNSGLKVGQRVGVGAQVFSCLECDRCKNDNEP 112
Cdd:PLN02178  31 ENDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVG-KNVTKFKEGDRVGVGVIIGSCQSCESCNQDLEN 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   113 YCTKFVTTYSQPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCG--PGKKVGIVGLGG 190
Cdd:PLN02178 110 YCPKVVFTYNSRSSDGTRNQGGYSDVIVVDHRFVLSIPDGLPSDSGAPLLCAGITVYSPMKYYGMTkeSGKRLGVNGLGG 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   191 IGSMGTLISKAMGAETYVISRSSRKREDAM-KMGADHYIATLEEGDWGEKYfDTFDLIVVCASSltdiDFNIMP--KAMK 267
Cdd:PLN02178 190 LGHIAVKIGKAFGLRVTVISRSSEKEREAIdRLGADSFLVTTDSQKMKEAV-GTMDFIIDTVSA----EHALLPlfSLLK 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   268 VGGRIVSISIPEQHEMLSLKPYGLKAVSISYSALGSIKELNQLLKLVSEKDIKIWVETLPVGEagVHEAFERMEKGDVRY 347
Cdd:PLN02178 265 VSGKLVALGLPEKPLDLPIFPLVLGRKMVGGSQIGGMKETQEMLEFCAKHKIVSDIELIKMSD--INSAMDRLAKSDVRY 342


                 ....
gi 2492777   348 RFTL 351
Cdd:PLN02178 343 RFVI 346
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 35-314 1.46e-51

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: 172.51  E-value: 1.46e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   35 DIDIKIEACGVCGSDIHCAAG-HWGNMKMPLVVGHEIVGKVVKLGPKsNSGLKVGQRVGVGAQVfSCLECDRCKndnepy 113
Cdd:cd05188   1 EVLVRVEAAGLCGTDLHIRRGgYPPPPKLPLILGHEGAGVVVEVGPG-VTGVKVGDRVVVLPNL-GCGTCELCR------ 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  114 ctkfvTTYSQPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGC-GPGKKVGIVGlggIG 192
Cdd:cd05188  73 -----ELCPGGGILGEGLDGGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVlKPGDTVLVLG---AG 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  193 SMGTL---ISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEGDWGEKYFDT---FDLIVVCASSLTDIDFNImpKAM 266
Cdd:cd05188 145 GVGLLaaqLAKAAGARVIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRLTGgggADVVIDAVGGPETLAQAL--RLL 222

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 2492777  267 KVGGRIVSISIPEQHEMLS-LKPYGLKAVSISYSALGSIKELNQLLKLV 314
Cdd:cd05188 223 RPGGRIVVVGGTSGGPPLDdLRRLLFKELTIIGSTGGTREDFEEALDLL 271
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 27-346 7.96e-49

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: 166.97  E-value: 7.96e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPfydHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGAQVFSCLECDRC 106
Cdd:cd08298  26 EPGP---GEVLIKVEACGVCRTDLHIVEGDLPPPKLPLIPGHEIVGRVEAVGPGV-TRFSVGDRVGVPWLGSTCGECRYC 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  107 KNDNEPYCTKFVTTysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIV 186
Cdd:cd08298 102 RSGRENLCDNARFT-------GYTVDGGYAEYMVADERFAYPIPEDYDDEEAAPLLCAGIIGYRALKLAGLKPGQRLGLY 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  187 GLGGIGSMGTLISKAMGAETYVISRSSRKREDAMKMGADhyiatlEEGDWGEKYFDTFDLIVVCASSltdidFNIMPKAM 266
Cdd:cd08298 175 GFGASAHLALQIARYQGAEVFAFTRSGEHQELARELGAD------WAGDSDDLPPEPLDAAIIFAPV-----GALVPAAL 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  267 KV---GGRIVS--ISIPEQHEMLSLKPYGLKavSISYSALGSIKELNQLLKLVSEKDIKIWVETLPVGEAgvHEAFERME 341
Cdd:cd08298 244 RAvkkGGRVVLagIHMSDIPAFDYELLWGEK--TIRSVANLTRQDGEEFLKLAAEIPIKPEVETYPLEEA--NEALQDLK 319


                ....*
gi 2492777  342 KGDVR 346
Cdd:cd08298 320 EGRIR 324
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 27-344 7.04e-44

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: 154.53  E-value: 7.04e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPfYDHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVgVGAQVFSCLECDRC 106
Cdd:COG1063  19 DPEP-GPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGV-TGLKVGDRV-VVEPNIPCGECRYC 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  107 KNDNEPYCTKFVTTysqpyedGYV-SQGGYANYVRVHEHFVVPIPENIPSHLAA---PLLCG-----------GLTVysp 171
Cdd:COG1063  96 RRGRYNLCENLQFL-------GIAgRDGGFAEYVRVPAANLVKVPDGLSDEAAAlvePLAVAlhaveragvkpGDTV--- 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  172 LVrNGCGP-GkkvgivglggigSMGTLISKAMGAET-YVISRSSRKREDAMKMGADHYIATLEEgDWGEKYFDT-----F 244
Cdd:COG1063 166 LV-IGAGPiG------------LLAALAARLAGAARvIVVDRNPERLELARELGADAVVNPREE-DLVEAVRELtggrgA 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  245 DLIVVCASSltDIDFNIMPKAMKVGGRIVSISIPEQHEMLSLKPYGLKAVSISYSALGSIKELNQLLKLVSEKDI---KI 321
Cdd:COG1063 232 DVVIEAVGA--PAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIdlePL 309

                       330       340
                ....*....|....*....|...
gi 2492777  322 WVETLPVGEAgvHEAFERMEKGD 344
Cdd:COG1063 310 ITHRFPLDDA--PEAFEAAADRA 330
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 38-352 1.56e-42

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: 150.86  E-value: 1.56e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   38 IKIEACGVCGSDIHCAAGH-WGNMKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGAqVFSCLECDRCKNDNEPYCTK 116
Cdd:cd08254  31 VKVKAAGVCHSDLHILDGGvPTLTKLPLTLGHEIAGTVVEVGAGV-TNFKVGDRVAVPA-VIPCGACALCRRGRGNLCLN 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  117 fvttysqPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGC-GPGKKVGIVGLGGIGSMG 195
Cdd:cd08254 109 -------QGMPGLGIDGGFAEYIVVPARALVPVPDGVPFAQAAVATDAVLTPYHAVVRAGEvKPGETVLVIGLGGLGLNA 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  196 TLISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEGDWGEKYFD---TFDLIVVCASslTDIDFNIMPKAMKVGGRI 272
Cdd:cd08254 182 VQIAKAMGAAVIAVDIKEEKLELAKELGADEVLNSLDDSPKDKKAAGlggGFDVIFDFVG--TQPTFEDAQKAVKPGGRI 259

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  273 VSISIPEQHEMLSLKPYGLKAVSISYSALGSIKELNQLLKLVSEKDIKIWVETLPVGEagVHEAFERMEKGDVRYRFTLV 352
Cdd:cd08254 260 VVVGLGRDKLTVDLSDLIARELRIIGSFGGTPEDLPEVLDLIAKGKLDPQVETRPLDE--IPEVLERLHKGKVKGRVVLV 337
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 27-345 9.86e-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: 145.92  E-value: 9.86e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPFYDhDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGpKSNSGLKVGQRVGVGAQVFsCLECDRC 106
Cdd:cd08259  20 DPEPGPG-EVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVG-EGVERFKPGDRVILYYYIP-CGKCEYC 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  107 KNDNEPYCTkfvttysQPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIV 186
Cdd:cd08259  97 LSGEENLCR-------NRAEYGEEVDGGFAEYVKVPERSLVKLPDNVSDESAALAACVVGTAVHALKRAGVKKGDTVLVT 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  187 GLGGIGSMGTL-ISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEGDWGEKYFDTfDLIVVCASSLTdidFNIMPKA 265
Cdd:cd08259 170 GAGGGVGIHAIqLAKALGARVIAVTRSPEKLKILKELGADYVIDGSKFSEDVKKLGGA-DVVIELVGSPT---IEESLRS 245

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  266 MKVGGRIVSI--SIPEQHEmLSLKPYGLKAVSISYSALGSIKELNQLLKLVSEKDIKIWVETLpVGEAGVHEAFERMEKG 343
Cdd:cd08259 246 LNKGGRLVLIgnVTPDPAP-LRPGLLILKEIRIIGSISATKADVEEALKLVKEGKIKPVIDRV-VSLEDINEALEDLKSG 323


                ..
gi 2492777  344 DV 345
Cdd:cd08259 324 KV 325
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 29-352 1.15e-38

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: 140.83  E-value: 1.15e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   29 KPFYDHDID----------IKIEACGVCGSDIHCAAGHW--GN----------MKMPLVVGHEIVGKVVKLGPkSNSGLK 86
Cdd:cd08240  11 KPLEEVEIDtpkppgtevlVKVTACGVCHSDLHIWDGGYdlGGgktmslddrgVKLPLVLGHEIVGEVVAVGP-DAADVK 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   87 VGQRVGVGAQVfSCLECDRCKNDNEPYCTKfvttysqPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGL 166
Cdd:cd08240  90 VGDKVLVYPWI-GCGECPVCLAGDENLCAK-------GRALGIFQDGGYAEYVIVPHSRYLVDPGGLDPALAATLACSGL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  167 TVYS------------PLVRNGCGpgkkvgivglgGIGSMGTLISKAMG-AETYVISRSSRKREDAMKMGADHYIatlee 233
Cdd:cd08240 162 TAYSavkklmplvadePVVIIGAG-----------GLGLMALALLKALGpANIIVVDIDEAKLEAAKAAGADVVV----- 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  234 gdWGEKYFDTFDLIVVCASSLTD-IDF-NIMP------KAMKVGGRIVSI-----SIPeqhemLSLKPYGLKAVSISYSA 300
Cdd:cd08240 226 --NGSDPDAAKRIIKAAGGGVDAvIDFvNNSAtaslafDILAKGGKLVLVglfggEAT-----LPLPLLPLRALTIQGSY 298

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 2492777  301 LGSIKELNQLLKLVSEKDIK-IWVETLPVGEagVHEAFERMEKGDVRYRFTLV 352
Cdd:cd08240 299 VGSLEELRELVALAKAGKLKpIPLTERPLSD--VNDALDDLKAGKVVGRAVLK 349
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 34-148 1.22e-36

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: 128.11  E-value: 1.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777     34 HDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPkSNSGLKVGQRVGVGAQVfSCLECDRCKNDNEPY 113
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGP-GVTGLKVGDRVVVEPLI-PCGKCEYCREGRYNL 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2492777    114 CTKFVTTysqpyedGYVSQGGYANYVRVHEHFVVP 148
Cdd:pfam08240  79 CPNGRFL-------GYDRDGGFAEYVVVPERNLVP 106
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 27-352 3.14e-36

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: 134.23  E-value: 3.14e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPfYDHDIDIKIEACGVCGSDIHCAAGHWGN---MKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGAqVFSCLEC 103
Cdd:cd05284  20 VPEP-GPGQVLVRVGGAGVCHSDLHVIDGVWGGilpYKLPFTLGHENAGWVEEVGSGV-DGLKEGDPVVVHP-PWGCGTC 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  104 DRCKNDNEPYCtkfvttySQPYEDGYVSQGGYANYVRVHEHFVVPIPENI-PSHlAAPLLCGGLTVYSPLVR--NGCGPG 180
Cdd:cd05284  97 RYCRRGEENYC-------ENARFPGIGTDGGFAEYLLVPSRRLVKLPRGLdPVE-AAPLADAGLTAYHAVKKalPYLDPG 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  181 KKVGIVGLGGIGSMGTLISKAMGAETYV-ISRSSRKREDAMKMGADHyiATLEEGDWGEKYFDT-----FDLIVVCASSL 254
Cdd:cd05284 169 STVVVIGVGGLGHIAVQILRALTPATVIaVDRSEEALKLAERLGADH--VLNASDDVVEEVRELtggrgADAVIDFVGSD 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  255 TDIDfnIMPKAMKVGGRIV------SISIPEQHEMlslkPYGlkaVSISYSALGSIKELNQLLKLVSEKDIKIWVETLPV 328
Cdd:cd05284 247 ETLA--LAAKLLAKGGRYVivgyggHGRLPTSDLV----PTE---ISVIGSLWGTRAELVEVVALAESGKVKVEITKFPL 317

                       330       340
                ....*....|....*....|....
gi 2492777  329 GEAgvHEAFERMEKGDVRYRFTLV 352
Cdd:cd05284 318 EDA--NEALDRLREGRVTGRAVLV 339
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 38-347 4.42e-35

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: 131.20  E-value: 4.42e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   38 IKIEACGVCGSDIHCAAGHWgNMKMPLVVGHEIVGKVVKLGPKsNSGLKVGQRVGVgAQVFSCLECDRCKNDNEPYCTKF 117
Cdd:cd08236  29 VKVKACGICGSDIPRYLGTG-AYHPPLVLGHEFSGTVEEVGSG-VDDLAVGDRVAV-NPLLPCGKCEYCKKGEYSLCSNY 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  118 vttysqpyedGYV---SQGGYANYVRVHEHFVVPIPENIPSHLAA---PLLCGGLTVY-SPLVRN------GCGPgkkvg 184
Cdd:cd08236 106 ----------DYIgsrRDGAFAEYVSVPARNLIKIPDHVDYEEAAmiePAAVALHAVRlAGITLGdtvvviGAGT----- 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  185 ivglggigsMGTLIS---KAMGAET-YVISRSSRKREDAMKMGADHYIATLEEG-DWGEKYFD--TFDLIVVCASSLTDI 257
Cdd:cd08236 171 ---------IGLLAIqwlKILGAKRvIAVDIDDEKLAVARELGADDTINPKEEDvEKVRELTEgrGADLVIEAAGSPATI 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  258 DFNIMpkAMKVGGRIVSISIPEQHEMLSLKPYG---LKAVSI-----SYSALGSIKELNQLLKLVSEKDIKI---WVETL 326
Cdd:cd08236 242 EQALA--LARPGGKVVLVGIPYGDVTLSEEAFEkilRKELTIqgswnSYSAPFPGDEWRTALDLLASGKIKVeplITHRL 319

                       330       340
                ....*....|....*....|.
gi 2492777  327 PVGEAGvhEAFERMEKGDVRY 347
Cdd:cd08236 320 PLEDGP--AAFERLADREEFS 338
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 27-346 3.22e-31

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: 120.32  E-value: 3.22e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPFyDHDIDIKIEACGVCGSDIHCAAGHWGNmKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGAQVFsCLECDRC 106
Cdd:cd08234  19 VPEPG-PDEVLIKVAACGICGTDLHIYEGEFGA-APPLVPGHEFAGVVVAVGSKV-TGFKVGDRVAVDPNIY-CGECFYC 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  107 KNDNEPYCTKF----VTTysqpyedgyvsQGGYANYVRVHEHFVVPIPENIPSHLAA---PLLC---G----GLTVYSPL 172
Cdd:cd08234  95 RRGRPNLCENLtavgVTR-----------NGGFAEYVVVPAKQVYKIPDNLSFEEAAlaePLSCavhGldllGIKPGDSV 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  173 VRNGCGPgkkvgivglggigsMGTL---ISKAMGAETYVIS-RSSRKREDAMKMGADHYIATLEE--GDWGEKYFDTFDl 246
Cdd:cd08234 164 LVFGAGP--------------IGLLlaqLLKLNGASRVTVAePNEEKLELAKKLGATETVDPSREdpEAQKEDNPYGFD- 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  247 IVVCASSLTDIdFNIMPKAMKVGGRIVSISIPEQHEMLSLKPYGL--KAVSI--SYSALGSIKelnQLLKLVSEKDIKIW 322
Cdd:cd08234 229 VVIEATGVPKT-LEQAIEYARRGGTVLVFGVYAPDARVSISPFEIfqKELTIigSFINPYTFP---RAIALLESGKIDVK 304

                       330       340
                ....*....|....*....|....*..
gi 2492777  323 V---ETLPVGEagVHEAFERMEKGDVR 346
Cdd:cd08234 305 GlvsHRLPLEE--VPEALEGMRSGGAL 329
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 35-344 4.32e-30

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: 117.70  E-value: 4.32e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   35 DIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGpKSNSGLKVGQRVGVgAQVFSCLECDRCKNDNEPYC 114
Cdd:cd08235  26 EVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVG-DGVTGFKVGDRVFV-APHVPCGECHYCLRGNENMC 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  115 TKFvttysqpYEDGYVSQGGYANYVRVHEHFVV-----PIPENIPSHLAA---PLLCggltVYSPLVRNGCGPGKKVGIV 186
Cdd:cd08235 104 PNY-------KKFGNLYDGGFAEYVRVPAWAVKrggvlKLPDNVSFEEAAlvePLAC----CINAQRKAGIKPGDTVLVI 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  187 GLGGIGSMGTLISKAMGAETYVISRSSRKR-EDAMKMGADHYIATLEEgDWGEKYFDT-----FDLIVVCASSltdidFN 260
Cdd:cd08235 173 GAGPIGLLHAMLAKASGARKVIVSDLNEFRlEFAKKLGADYTIDAAEE-DLVEKVRELtdgrgADVVIVATGS-----PE 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  261 IMPKAMKV---GGRIVSISIPEQHEMLSLKP----YGLKAVSISYSAlgSIKELNQLLKLVSEKDI---KIWVETLPVGE 330
Cdd:cd08235 247 AQAQALELvrkGGRILFFGGLPKGSTVNIDPnlihYREITITGSYAA--SPEDYKEALELIASGKIdvkDLITHRFPLED 324

                       330
                ....*....|....
gi 2492777  331 AgvHEAFERMEKGD 344
Cdd:cd08235 325 I--EEAFELAADGK 336
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
 38-348 4.47e-30

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 117.44  E-value: 4.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    38 IKIEACGVCGSDIHCAAGHWGNmKMPLVVGHEIVGKVVKLGPKSNSgLKVGQRVGVGAQVFSCLECDRCKNDNEPYCTKF 117
Cdd:PRK09422  30 VKMEYCGVCHTDLHVANGDFGD-KTGRILGHEGIGIVKEVGPGVTS-LKVGDRVSIAWFFEGCGHCEYCTTGRETLCRSV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   118 VTTysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIVGLggiGSMGTL 197
Cdd:PRK09422 108 KNA-------GYTVDGGMAEQCIVTADYAVKVPEGLDPAQASSITCAGVTTYKAIKVSGIKPGQWIAIYGA---GGLGNL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   198 ----ISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEGDWGEKYFDTF---DLIVVCASSltDIDFNIMPKAMKVGG 270
Cdd:PRK09422 178 alqyAKNVFNAKVIAVDINDDKLALAKEVGADLTINSKRVEDVAKIIQEKTggaHAAVVTAVA--KAAFNQAVDAVRAGG 255

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2492777   271 RIVSISIPEQHEMLSLKPYGLKAVSISYSALGSIKELNQLLKLVSEKDIKIWVETLPVGEagVHEAFERMEKGDVRYR 348
Cdd:PRK09422 256 RVVAVGLPPESMDLSIPRLVLDGIEVVGSLVGTRQDLEEAFQFGAEGKVVPKVQLRPLED--INDIFDEMEQGKIQGR 331
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 27-228 7.12e-30

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: 116.93  E-value: 7.12e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPfYDHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPkSNSGLKVGQRVGVGAqVFSCLECDRC 106
Cdd:cd08260  20 DPEP-PPDGVVVEVEACGVCRSDWHGWQGHDPDVTLPHVPGHEFAGVVVEVGE-DVSRWRVGDRVTVPF-VLGCGTCPYC 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  107 KNDNEPYCtkfvTTYSQPyedGYVSQGGYANYVRVH--EHFVVPIPENIPSHLAAPLLCGGLTVYSPLV-RNGCGPGKKV 183
Cdd:cd08260  97 RAGDSNVC----EHQVQP---GFTHPGSFAEYVAVPraDVNLVRLPDDVDFVTAAGLGCRFATAFRALVhQARVKPGEWV 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 2492777  184 GIVGLGGIGSMGTLISKAMGAETYVISRSSRKREDAMKMGADHYI 228
Cdd:cd08260 170 AVHGCGGVGLSAVMIASALGARVIAVDIDDDKLELARELGAVATV 214
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 38-345 8.02e-30

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: 117.36  E-value: 8.02e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   38 IKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPK-----SNSGLKVGQRVgVGAQVFSCLECDRCKN-DNE 111
Cdd:cd08231  30 VRVRLAGVCGSDVHTVAGRRPRVPLPIILGHEGVGRVVALGGGvttdvAGEPLKVGDRV-TWSVGAPCGRCYRCLVgDPT 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  112 PYCTKFVTTYSQPYEDGYVSqGGYANYVRVH-EHFVVPIPENIPSHLAAPLLCGGLTVYSPL------------VRNGCG 178
Cdd:cd08231 109 KCENRKKYGHEASCDDPHLS-GGYAEHIYLPpGTAIVRVPDNVPDEVAAPANCALATVLAALdragpvgagdtvVVQGAG 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  179 PgkkvgivglggigsMG---TLISKAMGAE-TYVISRSSRKREDAMKMGADHYIATLEEGDWGEK-------YFDTFDLI 247
Cdd:cd08231 188 P--------------LGlyaVAAAKLAGARrVIVIDGSPERLELAREFGADATIDIDELPDPQRRaivrditGGRGADVV 253

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  248 VVCASSLTDIDFNIMpkAMKVGGRIVSISIPEQHEMLSLKPYGL--KAVSISYSALGSIKELNQLLKLVSE-KDIKIWVE 324
Cdd:cd08231 254 IEASGHPAAVPEGLE--LLRRGGTYVLVGSVAPAGTVPLDPERIvrKNLTIIGVHNYDPSHLYRAVRFLERtQDRFPFAE 331

                       330       340
                ....*....|....*....|...
gi 2492777  325 --TLPVGEAGVHEAFERMEKGDV 345
Cdd:cd08231 332 lvTHRYPLEDINEALELAESGTA 354
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 27-346 1.04e-29

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: 116.02  E-value: 1.04e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPfydHDIDIKIEACGVCGSDIHCAAGHWGNM-KMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGvgaqvfsclecdr 105
Cdd:COG0604  24 EPGP---GEVLVRVKAAGVNPADLLIRRGLYPLPpGLPFIPGSDAAGVVVAVGEGV-TGFKVGDRVA------------- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  106 ckndnepyctkfvttysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRN---------- 175
Cdd:COG0604  87 ----------------------GLGRGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRgrlkpgetvl 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  176 ------GCGpgkkvgivglggigSMGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATlEEGDWGEK-----YFDTF 244
Cdd:COG0604 145 vhgaagGVG--------------SAAVQLAKALGARVIATASSPEKAELLRALGADHVIDY-REEDFAERvraltGGRGV 209

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  245 DLIV--VCASSLTDIdfnimPKAMKVGGRIVSI-SIPEQHEMLSLKPYGLKAVSISYSALGSI------KELNQLLKLVS 315
Cdd:COG0604 210 DVVLdtVGGDTLARS-----LRALAPGGRLVSIgAASGAPPPLDLAPLLLKGLTLTGFTLFARdpaerrAALAELARLLA 284

                       330       340       350
                ....*....|....*....|....*....|..
gi 2492777  316 EKDIKIWV-ETLPVGEAGvhEAFERMEKGDVR 346
Cdd:COG0604 285 AGKLRPVIdRVFPLEEAA--EAHRLLESGKHR 314
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 18-338 2.40e-28

(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: 113.02  E-value: 2.40e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   18 WKNPKKTKYD---PKPFYDHDIDIKIEACGVCGSDIH-----------CAAGHWGNMKMPLVVGHEIVGKVVKLGPKSNs 83
Cdd:cd08233   6 YHGRKDIRVEevpEPPVKPGEVKIKVAWCGICGSDLHeyldgpifiptEGHPHLTGETAPVTLGHEFSGVVVEVGSGVT- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   84 GLKVGQRVGVGAqVFSCLECDRCKNDNEPYCTKFVTTysqpyedGYVSQ-GGYANYVRVHEHFVVPIPENIPSHLAA--- 159
Cdd:cd08233  85 GFKVGDRVVVEP-TIKCGTCGACKRGLYNLCDSLGFI-------GLGGGgGGFAEYVVVPAYHVHKLPDNVPLEEAAlve 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  160 PL-------LCGGLTVYSPLVRNGCGP-GkkvgivglggigsMGT-LISKAMGAETYVISR-SSRKREDAMKMGADHYIA 229
Cdd:cd08233 157 PLavawhavRRSGFKPGDTALVLGAGPiG-------------LLTiLALKAAGASKIIVSEpSEARRELAEELGATIVLD 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  230 TLEEGDW-------GEKYFD-TFDlivvCASSltDIDFNIMPKAMKVGGRIVSISIPEQ----HEM-LSLKPYGLKAvSI 296
Cdd:cd08233 224 PTEVDVVaevrkltGGGGVDvSFD----CAGV--QATLDTAIDALRPRGTAVNVAIWEKpisfNPNdLVLKEKTLTG-SI 296

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 2492777  297 SYSAlgsiKELNQLLKLVSEKDIKiwVETLPVG----EAGVHEAFE 338
Cdd:cd08233 297 CYTR----EDFEEVIDLLASGKID--AEPLITSriplEDIVEKGFE 336
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 28-278 5.59e-28

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: 111.25  E-value: 5.59e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPfYDHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGAQVFSCLECDRCK 107
Cdd:cd08258  22 PEP-GPGEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEVGPDV-EGWKVGDRVVSETTFSTCGRCPYCR 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  108 NDNEPYCTKFVTtysqpyeDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAA---PLLCGGLTVYSP-LVRNG-----CG 178
Cdd:cd08258 100 RGDYNLCPHRKG-------IGTQADGGFAEYVLVPEESLHELPENLSLEAAAltePLAVAVHAVAERsGIRPGdtvvvFG 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  179 PGkkvgivglggigSMGTL---ISKAMGAETYV--ISRSSRKREDAMKMGADHYIATLE---EGDWGEKYFDTFDLIVVC 250
Cdd:cd08258 173 PG------------PIGLLaaqVAKLQGATVVVvgTEKDEVRLDVAKELGADAVNGGEEdlaELVNEITDGDGADVVIEC 240

                       250       260
                ....*....|....*....|....*...
gi 2492777  251 ASSLtdIDFNIMPKAMKVGGRIVSISIP 278
Cdd:cd08258 241 SGAV--PALEQALELLRKGGRIVQVGIF 266
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 35-348 1.72e-26

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: 108.23  E-value: 1.72e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   35 DIDIKIEACGVCGSDIHCAAGHWGnMKMPLVVGHEIVGKVVKLGP--KSNSGLKVGQRVgVGAQVFSCLECDRCKNDNEP 112
Cdd:cd08263  27 EILIRVAACGVCHSDLHVLKGELP-FPPPFVLGHEISGEVVEVGPnvENPYGLSVGDRV-VGSFIMPCGKCRYCARGKEN 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  113 YCTKFVT-----------TYSQPYEDG---YV-SQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNG- 176
Cdd:cd08263 105 LCEDFFAynrlkgtlydgTTRLFRLDGgpvYMySMGGLAEYAVVPATALAPLPESLDYTESAVLGCAGFTAYGALKHAAd 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  177 CGPGKKVGIVGLGGIGSMGTLISKAMGAETYV-ISRSSRKREDAMKMGADHYIATLEEGDWGEKYFDTF----DLIVVCA 251
Cdd:cd08263 185 VRPGETVAVIGVGGVGSSAIQLAKAFGASPIIaVDVRDEKLAKAKELGATHTVNAAKEDAVAAIREITGgrgvDVVVEAL 264

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  252 SSLTDIDFNIMpkAMKVGGRIVsisipeqheMLSLKPYGLKA-------VSISYSALGSI-----KELNQLLKLVSEKDI 319
Cdd:cd08263 265 GKPETFKLALD--VVRDGGRAV---------VVGLAPGGATAeipitrlVRRGIKIIGSYgarprQDLPELVGLAASGKL 333

                       330       340       350
                ....*....|....*....|....*....|..
gi 2492777  320 KIwvETLPVGEAG---VHEAFERMEKGDVRYR 348
Cdd:cd08263 334 DP--EALVTHKYKleeINEAYENLRKGLIHGR 363
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 27-343 5.14e-26

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 106.27  E-value: 5.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    27 DPKPFYDHDIdIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGpKSNSGLKVGQRVgVGAQVFSCLECDRC 106
Cdd:PRK13771  20 DPKPGKDEVV-IKVNYAGLCYRDLLQLQGFYPRMKYPVILGHEVVGTVEEVG-ENVKGFKPGDRV-ASLLYAPDGTCEYC 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   107 KNDNEPYCtkfvttysqPYEDGYVS--QGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVG 184
Cdd:PRK13771  97 RSGEEAYC---------KNRLGYGEelDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVTGMVYRGLRRAGVKKGETVL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   185 IVGLGGIGSMGTL-ISKAMGAETYVISRSSRKREdAMKMGADHYIATLEEGDWGEKYFDTfDLIVVCASSLTdidFNIMP 263
Cdd:PRK13771 168 VTGAGGGVGIHAIqVAKALGAKVIAVTSSESKAK-IVSKYADYVIVGSKFSEEVKKIGGA-DIVIETVGTPT---LEESL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   264 KAMKVGGRIVSIS--IPEQHEMLSLKPYGLKAVSISYSALGSIKELNQLLKLVSEKDIKiwvetlPVgeAGVHEAFERME 341
Cdd:PRK13771 243 RSLNMGGKIIQIGnvDPSPTYSLRLGYIILKDIEIIGHISATKRDVEEALKLVAEGKIK------PV--IGAEVSLSEID 314


                 ..
gi 2492777   342 KG 343
Cdd:PRK13771 315 KA 316
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 27-344 5.51e-26

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: 105.90  E-value: 5.51e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPfYDHDIDIKIEACGVCGSDIHCAAGHWGNmKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGAQVFsCLECDRC 106
Cdd:cd08264  21 DPKP-GPGEVLIRVKMAGVNPVDYNVINAVKVK-PMPHIPGAEFAGVVEEVGDHV-KGVKKGDRVVVYNRVF-DGTCDMC 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  107 KNDNEPYCTkfvttysQPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIV 186
Cdd:cd08264  97 LSGNEMLCR-------NGGIIGVVSNGGYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYHALKTAGLGPGETVVVF 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  187 GLGGIGSMGTL-ISKAMGAETYVISRssrkREDAMKMGADH---YIATLEEGDWGEKYFDtfdlIVV--CASSLTDIDFn 260
Cdd:cd08264 170 GASGNTGIFAVqLAKMMGAEVIAVSR----KDWLKEFGADEvvdYDEVEEKVKEITKMAD----VVInsLGSSFWDLSL- 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  261 impKAMKVGGRIVSISIPEQHEM-LSLKPYGLKAVSISYSALGSIKELNQLLKLVSEKDIKIWvETLPVGEAgvHEAFER 339
Cdd:cd08264 241 ---SVLGRGGRLVTFGTLTGGEVkLDLSDLYSKQISIIGSTGGTRKELLELVKIAKDLKVKVW-KTFKLEEA--KEALKE 314


                ....*
gi 2492777  340 MEKGD 344
Cdd:cd08264 315 LFSKE 319
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 27-291 1.87e-25

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: 105.32  E-value: 1.87e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPfydHDIDIKIEACGVCGSDIHCAAGHWGNMkMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVgVGAQVFSCLECDRC 106
Cdd:cd08279  22 DPGP---GEVLVRIAAAGLCHSDLHVVTGDLPAP-LPAVLGHEGAGVVEEVGPGV-TGVKPGDHV-VLSWIPACGTCRYC 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  107 KNDNEPYCTKFVTTYSQPYEDGY---------VSQ----GGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLT-----V 168
Cdd:cd08279  96 SRGQPNLCDLGAGILGGQLPDGTrrftadgepVGAmcglGTFAEYTVVPEASVVKIDDDIPLDRAALLGCGVTTgvgavV 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  169 YSPLVRN-------GCGpgkkvgivglggigsmGTLISKAMGAetyVISRSSR---------KREDAMKMGADHYIATLE 232
Cdd:cd08279 176 NTARVRPgdtvaviGCG----------------GVGLNAIQGA---RIAGASRiiavdpvpeKLELARRFGATHTVNASE 236

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2492777  233 E----------GDWGekyfdtFDLIVVCASSLTDID--FNIMPKamkvGGRIVSISIPEQHEMLSLKPYGL 291
Cdd:cd08279 237 DdaveavrdltDGRG------ADYAFEAVGRAATIRqaLAMTRK----GGTAVVVGMGPPGETVSLPALEL 297
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 28-346 3.26e-23

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: 98.02  E-value: 3.26e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPFyDHDIDIKIEACGVCGSDIHCAAGHWGNM---KMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVgvgaqvfsclecd 104
Cdd:cd05289  23 PEPG-PGEVLVKVHAAGVNPVDLKIREGLLKAAfplTLPLIPGHDVAGVVVAVGPGV-TGFKVGDEV------------- 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  105 rckndnepyctkfvttYSQPYEDGyvsQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGC-GPGKKV 183
Cdd:cd05289  88 ----------------FGMTPFTR---GGAYAEYVVVPADELALKPANLSFEEAAALPLAGLTAWQALFELGGlKAGQTV 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  184 givglggigsmgtLIS--------------KAMGAetYVISRSSRKREDAMK-MGADHYIATLEEGDWGEKYFDTFDLIV 248
Cdd:cd05289 149 -------------LIHgaaggvgsfavqlaKARGA--RVIATASAANADFLRsLGADEVIDYTKGDFERAAAPGGVDAVL 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  249 VCASSLTDIDFnimPKAMKVGGRIVSISIPEQHEmLSLKPYGLKAVSISYSALGsiKELNQLLKLVSEKDIKIWV-ETLP 327
Cdd:cd05289 214 DTVGGETLARS---LALVKPGGRLVSIAGPPPAE-QAAKRRGVRAGFVFVEPDG--EQLAELAELVEAGKLRPVVdRVFP 287

                       330
                ....*....|....*....
gi 2492777  328 VGEAgvHEAFERMEKGDVR 346
Cdd:cd05289 288 LEDA--AEAHERLESGHAR 304
adh_fam_2 TIGR02822
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
 38-224 4.09e-23

zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct subset of the larger family of oxidoreductases that includes zinc-binding alcohol dehydrogenases and NADPH:quinone reductases (pfam00107). The gene neighborhood of members of this family is not conserved and it appears that no members are characterized. The sequence of the family includes 6 invariant cysteine residues and one invariant histidine. It appears that no member is characterized. [Energy metabolism, Fermentation]


Pssm-ID: 131869 [Multi-domain]  Cd Length: 329  Bit Score: 98.07  E-value: 4.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777     38 IKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGpKSNSGLKVGQRVGVGAQVFSCLECDRCKNDNEPYCTKf 117
Cdd:TIGR02822  32 VRVRACGVCRTDLHVSEGDLPVHRPRVTPGHEVVGEVAGRG-ADAGGFAVGDRVGIAWLRRTCGVCRYCRRGAENLCPA- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    118 vTTYSqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIVGLGGIGSMGTL 197
Cdd:TIGR02822 110 -SRYT-----GWDTDGGYAEYTTVPAAFAYRLPTGYDDVELAPLLCAGIIGYRALLRASLPPGGRLGLYGFGGSAHLTAQ 183

                         170       180
                  ....*....|....*....|....*..
gi 2492777    198 ISKAMGAETYVISRSSRKREDAMKMGA 224
Cdd:TIGR02822 184 VALAQGATVHVMTRGAAARRLALALGA 210
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 28-280 5.17e-23

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 97.97  E-value: 5.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    28 PKPFYDH-DIDIKIEACGVCGSDIHCAAghW-----GNMKMPLVVGHEIVGKVVKLGPkSNSGLKVGQRV-GVGAQVfsC 100
Cdd:PRK05396  19 PVPEPGPnDVLIKVKKTAICGTDVHIYN--WdewaqKTIPVPMVVGHEFVGEVVEVGS-EVTGFKVGDRVsGEGHIV--C 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   101 LECDRCKNDNEPYC--TKFVttysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAA---PL-------LCGGLTV 168
Cdd:PRK05396  94 GHCRNCRAGRRHLCrnTKGV---------GVNRPGAFAEYLVIPAFNVWKIPDDIPDDLAAifdPFgnavhtaLSFDLVG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   169 YSPLVrNGCGP-GkkvgivglggigSMGTLISKAMGAETYVISRSSRKRED-AMKMGADHYIATLEEG------DWGEKY 240
Cdd:PRK05396 165 EDVLI-TGAGPiG------------IMAAAVAKHVGARHVVITDVNEYRLElARKMGATRAVNVAKEDlrdvmaELGMTE 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 2492777   241 -FDtfdliVVCASSLTDIDFNIMPKAMKVGGRIVSISIPEQ 280
Cdd:PRK05396 232 gFD-----VGLEMSGAPSAFRQMLDNMNHGGRIAMLGIPPG 267
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 27-230 9.00e-23

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: 97.39  E-value: 9.00e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPFYDhDIDIKIEACGVCGSDIHC-AAGHWGNMKMPLVVGHEIVGKVVKLGPKSNSGlKVGQRVGVGAQVFsCLECDR 105
Cdd:cd08239  19 VPVPGPG-EVLLRVKASGLCGSDLHYyYHGHRAPAYQGVIPGHEPAGVVVAVGPGVTHF-RVGDRVMVYHYVG-CGACRN 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  106 CKNDNEPYCTKFVTTYsqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGI 185
Cdd:cd08239  96 CRRGWMQLCTSKRAAY------GWNRDGGHAEYMLVPEKTLIPLPDDLSFADGALLLCGIGTAYHALRRVGVSGRDTVLV 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 2492777  186 VGLGGIGSMGTLISKAMGAET-YVISRSSRKREDAMKMGADHYIAT 230
Cdd:cd08239 170 VGAGPVGLGALMLARALGAEDvIGVDPSPERLELAKALGADFVINS 215
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 28-279 2.99e-22

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: 95.76  E-value: 2.99e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPfYDHDIDIKIEACGVCGSDIHC------AAGHwgnMKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGAQVfSCL 101
Cdd:cd05281  21 PKP-GPGEVLIKVLAASICGTDVHIyewdewAQSR---IKPPLIFGHEFAGEVVEVGEGV-TRVKVGDYVSAETHI-VCG 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  102 ECDRCKNDNEPYC--TKFVttysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAA---PL-------LCGGLTVY 169
Cdd:cd05281  95 KCYQCRTGNYHVCqnTKIL---------GVDTDGCFAEYVVVPEENLWKNDKDIPPEIASiqePLgnavhtvLAGDVSGK 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  170 SPLVrNGCGPgkkvgivglggIGSMGTLISKAMGAET-YVISRSSRKREDAMKMGADHYIATLEEgDWGEKYfDTFDLI- 247
Cdd:cd05281 166 SVLI-TGCGP-----------IGLMAIAVAKAAGASLvIASDPNPYRLELAKKMGADVVINPREE-DVVEVK-SVTDGTg 231

                       250       260       270
                ....*....|....*....|....*....|....
gi 2492777  248 --VVCASSLTDIDFNIMPKAMKVGGRIVSISIPE 279
Cdd:cd05281 232 vdVVLEMSGNPKAIEQGLKALTPGGRVSILGLPP 265
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 27-339 4.16e-21

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: 92.76  E-value: 4.16e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPFyDHDIDIKIEACGVCGSDIHCAAG-------HWGNMKM----PLVVGHEIVGKVVKLGPKSNSGLKVGQRVgVGA 95
Cdd:cd08262  18 DPEPG-PGQVLVKVLACGICGSDLHATAHpeamvddAGGPSLMdlgaDIVLGHEFCGEVVDYGPGTERKLKVGTRV-TSL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   96 QVFSCLECDRCKndnepyCTKFVTTYsqpyedgyvsqGGYANYVRVHEHFVVPIPENIPSHLAA---PL--------LCG 164
Cdd:cd08262  96 PLLLCGQGASCG------IGLSPEAP-----------GGYAEYMLLSEALLLRVPDGLSMEDAAltePLavglhavrRAR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  165 GLTVYSPLVRnGCGPgkkvgivglggigsMG---TLISKAMGAETYVIS-RSSRKREDAMKMGADHYI---ATLEEGDWG 237
Cdd:cd08262 159 LTPGEVALVI-GCGP--------------IGlavIAALKARGVGPIVASdFSPERRALALAMGADIVVdpaADSPFAAWA 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  238 EKYFDTF----DLIVVCASSLTDIDFNImpKAMKVGGRIVSISIPEQ----HEMLSLkpygLKAVSISYSALGSIKELNQ 309
Cdd:cd08262 224 AELARAGgpkpAVIFECVGAPGLIQQII--EGAPPGGRIVVVGVCMEsdniEPALAI----RKELTLQFSLGYTPEEFAD 297

                       330       340       350
                ....*....|....*....|....*....|....
gi 2492777  310 LLKLVSEKDIK----IwveTLPVGEAGVHEAFER 339
Cdd:cd08262 298 ALDALAEGKVDvapmV---TGTVGLDGVPDAFEA 328
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 61-345 9.72e-21

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: 91.55  E-value: 9.72e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   61 KMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGAQVfSCLECDRCKNDNEPYCTKFVTTysqpyedGYVSQGGYANYVR 140
Cdd:cd08266  56 PLPHILGSDGAGVVEAVGPGV-TNVKPGQRVVIYPGI-SCGRCEYCLAGRENLCAQYGIL-------GEHVDGGYAEYVA 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  141 VHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRN------------GCGPGkkvgivglggIGSMGTLISKAMGAETYV 208
Cdd:cd08266 127 VPARNLLPIPDNLSFEEAAAAPLTFLTAWHMLVTRarlrpgetvlvhGAGSG----------VGSAAIQIAKLFGATVIA 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  209 ISRSSRKREDAMKMGADHYIaTLEEGDWGEKYFD-TF----DLIVVCASSLTdidFNIMPKAMKVGGRIVSI-----SIP 278
Cdd:cd08266 197 TAGSEDKLERAKELGADYVI-DYRKEDFVREVRElTGkrgvDVVVEHVGAAT---WEKSLKSLARGGRLVTCgattgYEA 272

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2492777  279 EqhemLSLKPYGLKAVSISYSALGSIKELNQLLKLVSEKDIKIWVET-LPVGEAgvHEAFERMEKGDV 345
Cdd:cd08266 273 P----IDLRHVFWRQLSILGSTMGTKAELDEALRLVFRGKLKPVIDSvFPLEEA--AEAHRRLESREQ 334
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 33-275 1.53e-20

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: 91.14  E-value: 1.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   33 DHDIDIKIEACGVCGSDIHCAA-GHWGN--MKMPLVVGHEIVGKVVKLGPkSNSGLKVGQRVGVGAQVfSCLECDRCKND 109
Cdd:cd08232  21 PGEVRVRVAAGGICGSDLHYYQhGGFGTvrLREPMVLGHEVSGVVEAVGP-GVTGLAPGQRVAVNPSR-PCGTCDYCRAG 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  110 NEPYCT--KFVTTYSQ-PYEdgyvsQGGYANYVRVHEHFVVPIPENIPSHLAA---PL--------LCGGLTVYSPLVrN 175
Cdd:cd08232  99 RPNLCLnmRFLGSAMRfPHV-----QGGFREYLVVDASQCVPLPDGLSLRRAAlaePLavalhavnRAGDLAGKRVLV-T 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  176 GCGPgkkvgivglggigsMGTLI---SKAMGAETYVISR-SSRKREDAMKMGADHYI-ATLEEGDWGEKYFDTFDLIVVC 250
Cdd:cd08232 173 GAGP--------------IGALVvaaARRAGAAEIVATDlADAPLAVARAMGADETVnLARDPLAAYAADKGDFDVVFEA 238

                       250       260
                ....*....|....*....|....*
gi 2492777  251 ASSLTDIDFNImpKAMKVGGRIVSI 275
Cdd:cd08232 239 SGAPAALASAL--RVVRPGGTVVQV 261
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 27-233 8.76e-20

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: 89.10  E-value: 8.76e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPfydHDIDIKIEACGVCGSDIHCAAGHWGNMkMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGaqvF-SCLECDR 105
Cdd:cd08278  24 DPRP---DEVLVRIVATGICHTDLVVRDGGLPTP-LPAVLGHEGAGVVEAVGSAV-TGLKPGDHVVLS---FaSCGECAN 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  106 CKNDNEPYCTKFV------------TTYSQPYE----DGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLT-- 167
Cdd:cd08278  96 CLSGHPAYCENFFplnfsgrrpdgsTPLSLDDGtpvhGHFFGQSSFATYAVVHERNVVKVDKDVPLELLAPLGCGIQTga 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  168 --VY--------SPLVRNGCGpgkkvgivglggigSMG---TLISKAMGAETYV-ISRSSRKREDAMKMGADHYIATLEE 233
Cdd:cd08278 176 gaVLnvlkprpgSSIAVFGAG--------------AVGlaaVMAAKIAGCTTIIaVDIVDSRLELAKELGATHVINPKEE 241
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
193-316 3.35e-19

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 82.66  E-value: 3.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    193 SMGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATlEEGDWGEKYFD-T----FDLIVVCASSltDIDFNIMPKAMK 267
Cdd:pfam00107   4 LAAIQLAKAAGAKVIAVDGSEEKLELAKELGADHVINP-KETDLVEEIKElTggkgVDVVFDCVGS--PATLEQALKLLR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2492777    268 VGGRIVSISIPEQHEMLSLKPYGLKAVSISYSALGSIKELNQLLKLVSE 316
Cdd:pfam00107  81 PGGRVVVVGLPGGPLPLPLAPLLLKELTILGSFLGSPEEFPEALDLLAS 129
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 33-242 6.24e-19

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 86.66  E-value: 6.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    33 DHDIDIKIEACGVCGSDIHC-AAGHWGN--MKMPLVVGHEIVGKVVKlgpKSNSGLKVGQRVGVGAQVfSCLECDRCKND 109
Cdd:PRK09880  27 NNGTLVQITRGGICGSDLHYyQEGKVGNfvIKAPMVLGHEVIGKIVH---SDSSGLKEGQTVAINPSK-PCGHCKYCLSH 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   110 NEPYCTK---FVTTYSQPYEDgyvsqGGYANYVRVHEHFVVPIPENIPSHL---AAPL--------LCGGLTVYSPLVrN 175
Cdd:PRK09880 103 NENQCTTmrfFGSAMYFPHVD-----GGFTRYKVVDTAQCIPYPEKADEKVmafAEPLavaihaahQAGDLQGKRVFV-S 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2492777   176 GCGPgkkvgivglggigsMGTLI---SKAMGAETYVISR-SSRKREDAMKMGADHYIATLEE--GDWGEK--YFD 242
Cdd:PRK09880 177 GVGP--------------IGCLIvaaVKTLGAAEIVCADvSPRSLSLAREMGADKLVNPQNDdlDHYKAEkgYFD 237
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 28-275 7.10e-19

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: 86.39  E-value: 7.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPfYDHDIDIKIEACGVCGSDIH-CAAGHWGNM--KMPLVVGHEIVGKVVKLGPkSNSGLKVGQRVGVGAQVFsCLECD 104
Cdd:cd05285  18 PEP-GPGEVLVRVRAVGICGSDVHyYKHGRIGDFvvKEPMVLGHESAGTVVAVGS-GVTHLKVGDRVAIEPGVP-CRTCE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  105 RCKNDNepY--C--TKFVTTysQPYedgyvsQGGYANYVRVHEHFVVPIPENIPSHLAA---PLLCG-------GLTVYS 170
Cdd:cd05285  95 FCKSGR--YnlCpdMRFAAT--PPV------DGTLCRYVNHPADFCHKLPDNVSLEEGAlvePLSVGvhacrraGVRPGD 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  171 PLVRNGCGP-GkkvgivglggigSMGTLISKAMGAETYVIS-RSSRKREDAMKMGADHYI-----ATLEEGDWGEKYFDT 243
Cdd:cd05285 165 TVLVFGAGPiG------------LLTAAVAKAFGATKVVVTdIDPSRLEFAKELGATHTVnvrteDTPESAEKIAELLGG 232

                       250       260       270
                ....*....|....*....|....*....|....
gi 2492777  244 --FDLIVVCASSLTDIDFNImpKAMKVGGRIVSI 275
Cdd:cd05285 233 kgPDVVIECTGAESCIQTAI--YATRPGGTVVLV 264
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 27-343 1.49e-18

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: 85.40  E-value: 1.49e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPFYDHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSNSgLKVGQRVGVGAQVFsCLECDRC 106
Cdd:cd05278  19 DPKIQGPHDAIVRVTATSICGSDLHIYRGGVPGAKHGMILGHEFVGEVVEVGSDVKR-LKPGDRVSVPCITF-CGRCRFC 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  107 KNDNEPYCTkfvTTYSQPYeDGYVSQGGYANYVRVHE--HFVVPIPENIPshLAAPLLCG-----------------GLT 167
Cdd:cd05278  97 RRGYHAHCE---NGLWGWK-LGNRIDGGQAEYVRVPYadMNLAKIPDGLP--DEDALMLSdilptgfhgaelagikpGST 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  168 VYspLVrnGCGPgkkvgivglggIGSMGTLISKAMGAE-TYVISRSSRKREDAMKMGADhYIATLEEGDWGEKYFDT--- 243
Cdd:cd05278 171 VA--VI--GAGP-----------VGLCAVAGARLLGAArIIAVDSNPERLDLAKEAGAT-DIINPKNGDIVEQILELtgg 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  244 --FDLIVVCASSLTdiDFNIMPKAMKVGGRIVSISIPEQHEMLSLK-PYGLKAVSISYSALGSIKELNQLLKLVSEKDI- 319
Cdd:cd05278 235 rgVDCVIEAVGFEE--TFEQAVKVVRPGGTIANVGVYGKPDPLPLLgEWFGKNLTFKTGLVPVRARMPELLDLIEEGKId 312

                       330       340
                ....*....|....*....|....*.
gi 2492777  320 --KIWVETLPVGEagVHEAFERMEKG 343
Cdd:cd05278 313 psKLITHRFPLDD--ILKAYRLFDNK 336
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 18-345 2.28e-18

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: 85.00  E-value: 2.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   18 WKNPKKTKY----DPKPFYDHDIDIKIEACGVCGSDIHCAAGHWGNMKmPLVVGHEIVGKVVKLGPkSNSGLKVGQRVgV 93
Cdd:cd08284   6 FKGPGDVRVeevpIPQIQDPTDAIVKVTAAAICGSDLHIYRGHIPSTP-GFVLGHEFVGEVVEVGP-EVRTLKVGDRV-V 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   94 GAQVFSCLECDRCKNDNEPYCTK---FVTTYSQPYedgyvsQGGYANYVRV--HEHFVVPIPENIPSHLAapLLCG---- 164
Cdd:cd08284  83 SPFTIACGECFYCRRGQSGRCAKgglFGYAGSPNL------DGAQAEYVRVpfADGTLLKLPDGLSDEAA--LLLGdilp 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  165 -------------GLTVysplVRNGCGP-GKkvgivglggigsMGTLISKAMGAET-YVISRSSRKREDAMKMGA----- 224
Cdd:cd08284 155 tgyfgakraqvrpGDTV----AVIGCGPvGL------------CAVLSAQVLGAARvFAVDPVPERLERAAALGAepinf 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  225 -----DHYIATLEEGdwgekyfDTFDLI--VVCASSLTDIDFNIMPKamkvGGRIVSISIPEQHEM-LSLKPYGLKAVSI 296
Cdd:cd08284 219 edaepVERVREATEG-------RGADVVleAVGGAAALDLAFDLVRP----GGVISSVGVHTAEEFpFPGLDAYNKNLTL 287

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 2492777  297 SYSALGSIKELNQLLKLVSEKDIKIWV---ETLPVGEAGvhEAFERMEKGDV 345
Cdd:cd08284 288 RFGRCPVRSLFPELLPLLESGRLDLEFlidHRMPLEEAP--EAYRLFDKRKV 337
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 27-345 2.08e-17

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: 81.78  E-value: 2.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPFYDHDIDIKIEACGVCGSDIHCAAGHWGN-MKMPLVVGHEIVGKVVKLGPKsNSGLKVGQRVGvgaqvfsclecdr 105
Cdd:cd08241  21 PPEPGAPGEVRIRVEAAGVNFPDLLMIQGKYQVkPPLPFVPGSEVAGVVEAVGEG-VTGFKVGDRVV------------- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  106 ckndnepyctkfvttysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGC-GPGKkvg 184
Cdd:cd08241  87 ----------------------ALTGQGGFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALVRRARlQPGE--- 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  185 ivglggigsmgTL---------------ISKAMGAETYVISRSSRKREDAMKMGADHYIaTLEEGDWGEKYFDTF----- 244
Cdd:cd08241 142 -----------TVlvlgaaggvglaavqLAKALGARVIAAASSEEKLALARALGADHVI-DYRDPDLRERVKALTggrgv 209

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  245 DLIV------VCASSLtdidfnimpKAMKVGGRIVSI-----SIPEQHEMLSLkpygLKAVSI------SYSAL---GSI 304
Cdd:cd08241 210 DVVYdpvggdVFEASL---------RSLAWGGRLLVIgfasgEIPQIPANLLL----LKNISVvgvywgAYARRepeLLR 276

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 2492777  305 KELNQLLKLVSEKDIKIWV-ETLPVGEAGvhEAFERMEKGDV 345
Cdd:cd08241 277 ANLAELFDLLAEGKIRPHVsAVFPLEQAA--EALRALADRKA 316
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 38-277 2.54e-17

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: 81.85  E-value: 2.54e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   38 IKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVgVGAQVFSCLECDRCKNDNEPYCTKF 117
Cdd:cd08261  29 VRVKRVGICGSDLHIYHGRNPFASYPRILGHELSGEVVEVGEGV-AGLKVGDRV-VVDPYISCGECYACRKGRPNCCENL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  118 VTTysqpyedGYVSQGGYANYVRVHEHfVVPIPENIPSHLAA---PLLCGGLTVYsplvRNGCGPGKKVGIVGlggigsM 194
Cdd:cd08261 107 QVL-------GVHRDGGFAEYIVVPAD-ALLVPEGLSLDQAAlvePLAIGAHAVR----RAGVTAGDTVLVVG------A 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  195 G------TLISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEgDWGEKYF-----DTFDLIV--VCASSltdidfnI 261
Cdd:cd08261 169 GpiglgvIQVAKARGARVIVVDIDDERLEFARELGADDTINVGDE-DVAARLReltdgEGADVVIdaTGNPA-------S 240

                       250
                ....*....|....*....
gi 2492777  262 MPKAMKV---GGRIVSISI 277
Cdd:cd08261 241 MEEAVELvahGGRVVLVGL 259
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
 34-225 2.22e-16

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: 79.37  E-value: 2.22e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   34 HDIDIKIEACGVCGSDIHC---AAGHWGN------MKMPLVVGHEIVGKVVKLGPK-SNSGLKVGQRVgVGAQVFSCLEC 103
Cdd:cd08256  25 GEILVKVEACGICAGDIKCyhgAPSFWGDenqppyVKPPMIPGHEFVGRVVELGEGaEERGVKVGDRV-ISEQIVPCWNC 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  104 DRCKNDNEPYCTKfvttysqpyEDGYVSQ----GGYANYVRVHEHFVV-PIPENIPSHLAA---PLLCGGLTVYSPLVRN 175
Cdd:cd08256 104 RFCNRGQYWMCQK---------HDLYGFQnnvnGGMAEYMRFPKEAIVhKVPDDIPPEDAIliePLACALHAVDRANIKF 174

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 2492777  176 -------GCGPgkkvgivglgGIGSMGTLISKAMGAETYVISRSSRKREDAMKMGAD 225
Cdd:cd08256 175 ddvvvlaGAGP----------LGLGMIGAARLKNPKKLIVLDLKDERLALARKFGAD 221
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 28-346 3.53e-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: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 78.41  E-value: 3.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPFyDHDIDIKIEACGVCGSDIHCAAGHWGNM---KMPLVVGHEIVGKVVKLGPKsNSGLKVGQRVgvgaqvFSCLecd 104
Cdd:cd08267  22 PTPK-PGEVLVKVHAASVNPVDWKLRRGPPKLLlgrPFPPIPGMDFAGEVVAVGSG-VTRFKVGDEV------FGRL--- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  105 rckndnepyctkfvttysqpyedGYVSQGGYANYVRVHEHFVVPIPENIpSHL-AAPLLCGGLTVYSPLVRN-------- 175
Cdd:cd08267  91 -----------------------PPKGGGALAEYVVAPESGLAKKPEGV-SFEeAAALPVAGLTALQALRDAgkvkpgqr 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  176 --------GCGpgkkvgivglggigSMGTLISKAMGAETYVISrSSRKREDAMKMGADHYI-ATLEEGDWGEKYFDTFDL 246
Cdd:cd08267 147 vlingasgGVG--------------TFAVQIAKALGAHVTGVC-STRNAELVRSLGADEVIdYTTEDFVALTAGGEKYDV 211

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  247 IVVCASSlTDIDFNIMPKAMKVGGRIVSISIPEQ-----HEMLSLKPYGLKAVSISYSALGSIKELNQLLKLVSEKDIKI 321
Cdd:cd08267 212 IFDAVGN-SPFSLYRASLALKPGGRYVSVGGGPSglllvLLLLPLTLGGGGRRLKFFLAKPNAEDLEQLAELVEEGKLKP 290

                       330       340
                ....*....|....*....|....*.
gi 2492777  322 WV-ETLPVGEAGvhEAFERMEKGDVR 346
Cdd:cd08267 291 VIdSVYPLEDAP--EAYRRLKSGRAR 314
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 18-235 4.42e-16

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: 78.71  E-value: 4.42e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   18 WKNPK---KTKYDPKPfYDHDIDIKIEACGVCGSDIHCAAG-------HWGNMKMPLVVGHEIVGKVVKLGpKSNSGLKV 87
Cdd:cd08265  34 WRYPElrvEDVPVPNL-KPDEILIRVKACGICGSDIHLYETdkdgyilYPGLTEFPVVIGHEFSGVVEKTG-KNVKNFEK 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   88 GQRVgVGAQVFSCLECDRCKNDNEPYCTKFvttysqpYEDGYVSQGGYANYVRVHEHFVVPIPENI------PSHLAAPL 161
Cdd:cd08265 112 GDPV-TAEEMMWCGMCRACRSGSPNHCKNL-------KELGFSADGAFAEYIAVNARYAWEINELReiysedKAFEAGAL 183

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2492777  162 LCGGLTVYSPLVRNGCG--PGKKVGIVGLGGIGSMGTLISKAMGAETYVISR-SSRKREDAMKMGADHYIATLEEGD 235
Cdd:cd08265 184 VEPTSVAYNGLFIRGGGfrPGAYVVVYGAGPIGLAAIALAKAAGASKVIAFEiSEERRNLAKEMGADYVFNPTKMRD 260
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 27-154 1.59e-15

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: 76.81  E-value: 1.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPFYDHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPkSNSGLKVGQRVGVGAQVfSCLECDRC 106
Cdd:cd08283  19 DPKIEDPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGP-EVRNLKVGDRVVVPFTI-ACGECFYC 96

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2492777  107 K----------NDNEPYCTKFVTT------YSQPYeDGYvsQGGYANYVRV-HEHF-VVPIPENIP 154
Cdd:cd08283  97 KrglysqcdntNPSAEMAKLYGHAgagifgYSHLT-GGY--AGGQAEYVRVpFADVgPFKIPDDLS 159
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 34-343 2.33e-15

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: 75.68  E-value: 2.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   34 HDIDIKIEACGVCGSDIHCAAGHWGNMKMPLvvGHEIVGKVVKLGPKsNSGLKVGQRVgVGaqvfsclecdrckndnepy 113
Cdd:cd05195   1 DEVEVEVKAAGLNFRDVLVALGLLPGDETPL--GLECSGIVTRVGSG-VTGLKVGDRV-MG------------------- 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  114 ctkfvttysqpyedgyVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVR-------------NGCGPg 180
Cdd:cd05195  58 ----------------LAPGAFATHVRVDARLVVKIPDSLSFEEAATLPVAYLTAYYALVDlarlqkgesvlihAAAGG- 120

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  181 kkvgivglggigsMGTL---ISKAMGAETYVISRSSRKREDAMKMG--ADH--------YIATLEEGDWGEKyfdtFDLI 247
Cdd:cd05195 121 -------------VGQAaiqLAQHLGAEVFATVGSEEKREFLRELGgpVDHifssrdlsFADGILRATGGRG----VDVV 183

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  248 VvcaSSLTDIDFNIMPKAMKVGGRIVSIS--IPEQHEMLSLKPYglkAVSISYSA--LGSIKE---------LNQLLKLV 314
Cdd:cd05195 184 L---NSLSGELLRASWRCLAPFGRFVEIGkrDILSNSKLGMRPF---LRNVSFSSvdLDQLARerpellrelLREVLELL 257

                       330       340
                ....*....|....*....|....*....
gi 2492777  315 SEKDIKIwVETLPVGEAGVHEAFERMEKG 343
Cdd:cd05195 258 EAGVLKP-LPPTVVPSASEIDAFRLMQSG 285
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 28-345 1.38e-14

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: 74.01  E-value: 1.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPfydHDIDIKIEACGVCGSDIHCAAGHWgNMKMPLVVGHEIVGKVVKLGPkSNSGLKVGQRVgVGAQVFSCLECDRCK 107
Cdd:cd05279  23 PKA---GEVRIKVVATGVCHTDLHVIDGKL-PTPLPVILGHEGAGIVESIGP-GVTTLKPGDKV-IPLFGPQCGKCKQCL 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  108 NDNEPYCTKF-VTTYSQPYEDG-------------YVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVY---- 169
Cdd:cd05279  97 NPRPNLCSKSrGTNGRGLMSDGtsrftckgkpihhFLGTSTFAEYTVVSEISLAKIDPDAPLEKVCLIGCGFSTGYgaav 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  170 --------SPLVRNGCGpgkkvgivglggigsmGTLISKAMGAETYVISR------SSRKREDAMKMGADHYI------- 228
Cdd:cd05279 177 ntakvtpgSTCAVFGLG----------------GVGLSVIMGCKAAGASRiiavdiNKDKFEKAKQLGATECInprdqdk 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  229 ----ATLEEGDWGEKYfdTFDlivvCASSLtdidfNIMPKAMKV----GGRIVSISIPEQHEMLSLKPYGL-KAVSISYS 299
Cdd:cd05279 241 piveVLTEMTDGGVDY--AFE----VIGSA-----DTLKQALDAtrlgGGTSVVVGVPPSGTEATLDPNDLlTGRTIKGT 309

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 2492777  300 ALGSIKELNQLLKLVSEKDIK------IWVETLPVGEagVHEAFERMEKGDV 345
Cdd:cd05279 310 VFGGWKSKDSVPKLVALYRQKkfpldeLITHVLPFEE--INDGFDLMRSGES 359
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 28-346 1.62e-14

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 73.46  E-value: 1.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPfYDHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGvgaqvfsclecdrck 107
Cdd:cd08271  23 PGP-GAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKV-TGWKVGDRVA--------------- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  108 ndnepyctkfvttysqpYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVY-------------SPLVR 174
Cdd:cd08271  86 -----------------YHASLARGGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYqalfkklrieagrTILIT 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  175 NGCGpgkkvgivglgGIGSMGTLISKAMGAetYVI-SRSSRKREDAMKMGADHYIATLEEgDWGEKYFDT-----FDLIV 248
Cdd:cd08271 149 GGAG-----------GVGSFAVQLAKRAGL--RVItTCSKRNFEYVKSLGADHVIDYNDE-DVCERIKEItggrgVDAVL 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  249 VCASSLTDIDfniMPKAMKVGGRIVsiSIPEQHEMLSLKPYGLkAVSISYSALGS---------IKEL----NQLLKLVS 315
Cdd:cd08271 215 DTVGGETAAA---LAPTLAFNGHLV--CIQGRPDASPDPPFTR-ALSVHEVALGAahdhgdpaaWQDLryagEELLELLA 288

                       330       340       350
                ....*....|....*....|....*....|..
gi 2492777  316 EKDIKIWV-ETLPVgEAGVhEAFERMEKGDVR 346
Cdd:cd08271 289 AGKLEPLViEVLPF-EQLP-EALRALKDRHTR 318
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 26-346 1.08e-12

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: 68.04  E-value: 1.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   26 YDPKPFYDHDID----------IKIEACGVCGSDIhcaAGHWGNMKMPLVVGHEIVGKVVKLGPKSnsglKVGQRVgVGA 95
Cdd:cd08242   7 DGGLDLRVEDLPkpepppgealVRVLLAGICNTDL---EIYKGYYPFPGVPGHEFVGIVEEGPEAE----LVGKRV-VGE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   96 QVFSCLECDRCKNDNEPYCtkfvttysqPYED--GYVSQ-GGYANYVRVHEHFVVPIPENIPSHLAA---PLLcgglTVY 169
Cdd:cd08242  79 INIACGRCEYCRRGLYTHC---------PNRTvlGIVDRdGAFAEYLTLPLENLHVVPDLVPDEQAVfaePLA----AAL 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  170 SPLVRNGCGPGKKVGIVGLGGIGSMGTLISKAMGAETYVISRSSRKREDAMKMGadhyIATLEEGDWGEKYfDTFDLIVV 249
Cdd:cd08242 146 EILEQVPITPGDKVAVLGDGKLGLLIAQVLALTGPDVVLVGRHSEKLALARRLG----VETVLPDEAESEG-GGFDVVVE 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  250 CASSLTdiDFNIMPKAMKVGGRIVSISIPEQHEMLSLKPYGLKAVSISYSALGSIKELNQLLklvsEKDiKIWVETL--- 326
Cdd:cd08242 221 ATGSPS--GLELALRLVRPRGTVVLKSTYAGPASFDLTKAVVNEITLVGSRCGPFAPALRLL----RKG-LVDVDPLita 293

                       330       340
                ....*....|....*....|...
gi 2492777  327 --PVGEAgvHEAFER-MEKGDVR 346
Cdd:cd08242 294 vyPLEEA--LEAFERaAEPGALK 314
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 27-345 1.58e-12

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


Pssm-ID: 176180 [Multi-domain]  Cd Length: 323  Bit Score: 67.47  E-value: 1.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPfYDHDIDIKIEACGVCGSDIHCAAGHWGNMK-MPLVVGHEIVGKVVKLGPkSNSGLKVGQRVgvgaqvfsclecdr 105
Cdd:cd05276  22 KPAP-GPGEVLIRVAAAGVNRADLLQRQGLYPPPPgASDILGLEVAGVVVAVGP-GVTGWKVGDRV-------------- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  106 ckndnepyCtkfvttysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLV-RNGCGPGKKvg 184
Cdd:cd05276  86 --------C-------------ALLAGGGYAEYVVVPAGQLLPVPEGLSLVEAAALPEVFFTAWQNLFqLGGLKAGETvl 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  185 ivg-lggigSMGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEgDWGEKYFDTF-----DLIV--VCASSLTD 256
Cdd:cd05276 145 ihggasgvgTAAIQLAKALGARVIATAGSEEKLEACRALGADVAINYRTE-DFAEEVKEATggrgvDVILdmVGGDYLAR 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  257 idfNImpKAMKVGGRIVSISIpeqheM----------------LSLKPYGLKAVSISY-SALgsIKEL-NQLLKLVSEKD 318
Cdd:cd05276 224 ---NL--RALAPDGRLVLIGL-----LggakaeldlapllrkrLTLTGSTLRSRSLEEkAAL--AAAFrEHVWPLFASGR 291

                       330       340
                ....*....|....*....|....*...
gi 2492777  319 IKIWV-ETLPVGEAGvhEAFERMEKGDV 345
Cdd:cd05276 292 IRPVIdKVFPLEEAA--EAHRRMESNEH 317
PRK10083 PRK10083
putative oxidoreductase; Provisional
 35-159 1.72e-12

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 67.46  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    35 DIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSNSGlKVGQRVGVGAqVFSCLECDRCKNDNEPYC 114
Cdd:PRK10083  26 EVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGEGVDAA-RIGERVAVDP-VISCGHCYPCSIGKPNVC 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 2492777   115 TKFVTTysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAA 159
Cdd:PRK10083 104 TSLVVL-------GVHRDGGFSEYAVVPAKNAHRIPDAIADQYAV 141
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 38-274 5.01e-12

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: 66.08  E-value: 5.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   38 IKIEACGVCGSDIHCAAGHWGNMK-MPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGAQVFSclecdrckndnepyctk 116
Cdd:cd08268  32 IRVEAIGLNRADAMFRRGAYIEPPpLPARLGYEAAGVVEAVGAGV-TGFAVGDRVSVIPAADL----------------- 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  117 fvTTYsqpyedgyvsqGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGcGPGKKVGIVGLGGIGSMGT 196
Cdd:cd08268  94 --GQY-----------GTYAEYALVPAAAVVKLPDGLSFVEAAALWMQYLTAYGALVELA-GLRPGDSVLITAASSSVGL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  197 L---ISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEGDWGEKYFDT----FDLIV--VCASSLTDIdfnimPKAMK 267
Cdd:cd08268 160 AaiqIANAAGATVIATTRTSEKRDALLALGAAHVIVTDEEDLVAEVLRITggkgVDVVFdpVGGPQFAKL-----ADALA 234


                ....*..
gi 2492777  268 VGGRIVS 274
Cdd:cd08268 235 PGGTLVV 241
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 27-141 7.11e-12

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: 66.08  E-value: 7.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPFYDHDIDIKIEACGVCGSDIHCAAGHWGnMKMPLVVGHEIVGKVVKLGPkSNSGLKVGQRVGVGAQVfsclECDRC 106
Cdd:cd08282  19 DPKIEHPTDAIVRITTTAICGSDLHMYRGRTG-AEPGLVLGHEAMGEVEEVGS-AVESLKVGDRVVVPFNV----ACGRC 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 2492777  107 KNDNEPYCTKFVTTYSQPYED--GYVSQGGY----ANYVRV 141
Cdd:cd08282  93 RNCKRGLTGVCLTVNPGRAGGayGYVDMGPYgggqAEYLRV 133
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 33-343 1.15e-11

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


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 64.86  E-value: 1.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   33 DHDIDIKIEACgvcgS----DIHCAAGHWGN-MKMPLVVGHEIVGKVVKLGPKsNSGLKVGQRVgvgaqvfsclecdrck 107
Cdd:cd08276  27 PGEVLVRVHAV----SlnyrDLLILNGRYPPpVKDPLIPLSDGAGEVVAVGEG-VTRFKVGDRV---------------- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  108 ndnepyctkfVTTYSQPYEDGYVS------------QGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRN 175
Cdd:cd08276  86 ----------VPTFFPNWLDGPPTaedeasalggpiDGVLAEYVVLPEEGLVRAPDHLSFEEAATLPCAGLTAWNALFGL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  176 GC-GPGKKVGIvglggigsMGT--------LISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEGDWGEKYFD-T-- 243
Cdd:cd08276 156 GPlKPGDTVLV--------QGTggvslfalQFAKAAGARVIATSSSDEKLERAKALGADHVINYRTTPDWGEEVLKlTgg 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  244 --FDLI--VVCASSLT-DIdfnimpKAMKVGGRIVSI-SIPEQHEMLSLKPYGLKAVSISYSALGSIKELNQLLKLVSEK 317
Cdd:cd08276 228 rgVDHVveVGGPGTLAqSI------KAVAPGGVISLIgFLSGFEAPVLLLPLLTKGATLRGIAVGSRAQFEAMNRAIEAH 301

                       330       340       350
                ....*....|....*....|....*....|...
gi 2492777  318 DIKiwvetlPV-------GEAgvHEAFERMEKG 343
Cdd:cd08276 302 RIR------PVidrvfpfEEA--KEAYRYLESG 326
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 30-225 1.31e-11

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 65.18  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    30 PFYDHDIDIKIEACGVCGSDIH------CAAghwGNMKMPLVVGHEIVGKVVKLGPKSNSgLKVGQRVGVGAQVfSCLEC 103
Cdd:PLN02702  38 PLGPHDVRVRMKAVGICGSDVHylktmrCAD---FVVKEPMVIGHECAGIIEEVGSEVKH-LVVGDRVALEPGI-SCWRC 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   104 DRCKNDNEPYC--TKFVTTysQPYedgyvsQGGYANYVrVH-EHFVVPIPENIPSHLAAplLCGGLTV-YSPLVRNGCGP 179
Cdd:PLN02702 113 NLCKEGRYNLCpeMKFFAT--PPV------HGSLANQV-VHpADLCFKLPENVSLEEGA--MCEPLSVgVHACRRANIGP 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 2492777   180 GKKVGIVGLGGIGSMGTLISKAMGAETYVISRSSRKR-EDAMKMGAD 225
Cdd:PLN02702 182 ETNVLVMGAGPIGLVTMLAARAFGAPRIVIVDVDDERlSVAKQLGAD 228
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
 27-237 1.39e-11

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: 65.02  E-value: 1.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPFYDHDIDIKIEACGVCGSDIHCAAGHwGNMKMPLVVGHEIVGKVVKLGPKSNSgLKVGQRVgVGAQVFSCLECDRC 106
Cdd:cd08287  19 DPVIEEPTDAVIRVVATCVCGSDLWPYRGV-SPTRAPAPIGHEFVGVVEEVGSEVTS-VKPGDFV-IAPFAISDGTCPFC 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  107 KNDNEPYCT--KFVttysqpyedGYVSQGGYANYVRV--HEHFVVPIPEN-------IPSHLAAPLLCGglTVYSPLVRN 175
Cdd:cd08287  96 RAGFTTSCVhgGFW---------GAFVDGGQGEYVRVplADGTLVKVPGSpsddedlLPSLLALSDVMG--TGHHAAVSA 164

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2492777  176 GCGPGKKVGIVGLGGIGSMGTLISKAMGAETYV-ISRSSRKREDAMKMGADHYIAtlEEGDWG 237
Cdd:cd08287 165 GVRPGSTVVVVGDGAVGLCAVLAAKRLGAERIIaMSRHEDRQALAREFGATDIVA--ERGEEA 225
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 34-169 5.05e-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: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 63.05  E-value: 5.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   34 HDIDIKIEACGVCGSDIHCAAG-HWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGvgaqvfsCLecdrckndnep 112
Cdd:cd08273  28 GEVVVKVEASGVSFADVQMRRGlYPDQPPLPFTPGYDLVGRVDALGSGV-TGFEVGDRVA-------AL----------- 88

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 2492777  113 yctkfvTTYsqpyedgyvsqGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVY 169
Cdd:cd08273  89 ------TRV-----------GGNAEYINLDAKYLVPVPEGVDAAEAVCLVLNYVTAY 128
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 27-226 6.86e-11

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: 62.37  E-value: 6.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPfYDHDIDIKIEACGVCGSDIHCAA---GHWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVgaqvfsclec 103
Cdd:cd08269  14 RPTP-GPGQVLVRVEGCGVCGSDLPAFNqgrPWFVYPAEPGGPGHEGWGRVVALGPGV-RGLAVGDRVAG---------- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  104 drckndnepyctkfvttysqpyedgyVSQGGYANYVRVHEHFVVPIPENIPSHL--AAPLLCG--GLTVYSPLvrngcgP 179
Cdd:cd08269  82 --------------------------LSGGAFAEYDLADADHAVPLPSLLDGQAfpGEPLGCAlnVFRRGWIR------A 129

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 2492777  180 GKKVGIVGLGGIGSMGTLISKAMGAETY-VISRSSRKREDAMKMGADH 226
Cdd:cd08269 130 GKTVAVIGAGFIGLLFLQLAAAAGARRViAIDRRPARLALARELGATE 177
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 38-336 7.02e-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: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 62.70  E-value: 7.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   38 IKIEACGVCGSDI-------------------HCAAGHWGN-MKMPLVVGHEIVGKVVKLGPKSNSGLkVGQRVgvgaQV 97
Cdd:cd08274  33 IRVGACGVNNTDIntregwystevdgatdstgAGEAGWWGGtLSFPRIQGADIVGRVVAVGEGVDTAR-IGERV----LV 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   98 FSCLecdRCKNDNEPYCTKFVttysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGC 177
Cdd:cd08274 108 DPSI---RDPPEDDPADIDYI---------GSERDGGFAEYTVVPAENAYPVNSPLSDVELATFPCSYSTAENMLERAGV 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  178 GPGKKVGIVGLGGIGSMGTL-ISKAMGAetYVISRSSRKREDAMK-MGADHYIATLEEGDWGEKYFD--TFDLIV-VCAS 252
Cdd:cd08274 176 GAGETVLVTGASGGVGSALVqLAKRRGA--IVIAVAGAAKEEAVRaLGADTVILRDAPLLADAKALGgePVDVVAdVVGG 253

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  253 SLtdidFNIMPKAMKVGGRIVS---ISIPEQHemLSLKPYGLKAVSISYSALGSIKELNQLLKLVSEKDIKIWVE-TLPV 328
Cdd:cd08274 254 PL----FPDLLRLLRPGGRYVTagaIAGPVVE--LDLRTLYLKDLTLFGSTLGTREVFRRLVRYIEEGEIRPVVAkTFPL 327


                ....*...
gi 2492777  329 GEagVHEA 336
Cdd:cd08274 328 SE--IREA 333
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 28-346 1.18e-10

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


Pssm-ID: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 62.24  E-value: 1.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPFYDHDIDIKIEACGVCGSDIHCAAGHwG----NMKM------------PLVVGHEIVGKVVKLGPKSNSgLKVGQRV 91
Cdd:cd08248  24 PVIRKPNQVLIKVHAASVNPIDVLMRSGY-GrtllNKKRkpqsckysgiefPLTLGRDCSGVVVDIGSGVKS-FEIGDEV 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   92 GVGAQVFSclecdrckndnepyctkfvttysqpyedgyvsQGGYANYVRVHEHFVVPIPENIpSHL-AAPLLCGGLTVYS 170
Cdd:cd08248 102 WGAVPPWS--------------------------------QGTHAEYVVVPENEVSKKPKNL-SHEeAASLPYAGLTAWS 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  171 PLVR-----------------NGCGPgkkvgivglggigsMGTLIS---KAMGAETYVISrSSRKREDAMKMGADHYIAT 230
Cdd:cd08248 149 ALVNvgglnpknaagkrvlilGGSGG--------------VGTFAIqllKAWGAHVTTTC-STDAIPLVKSLGADDVIDY 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  231 LEEGDWGE-KYFDTFDLIVVCASSLTDIdfnIMPKAMKVGGRIVSISIPEQHEM-----------------LSLKPYGLK 292
Cdd:cd08248 214 NNEDFEEElTERGKFDVILDTVGGDTEK---WALKLLKKGGTYVTLVSPLLKNTdklglvggmlksavdllKKNVKSLLK 290

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 2492777  293 AVSISY---SALGSIkeLNQLLKLVSEKDIKIWVE-TLPVGEagVHEAFERMEKGDVR 346
Cdd:cd08248 291 GSHYRWgffSPSGSA--LDELAKLVEDGKIKPVIDkVFPFEE--VPEAYEKVESGHAR 344
quinone_pig3 TIGR02824
putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative ...
 28-345 1.28e-10

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


Pssm-ID: 274316 [Multi-domain]  Cd Length: 325  Bit Score: 61.89  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777     28 PKPfydHDIDIKIEACGVCGSDIHCAAGHWGNMK-MPLVVGHEIVGKVVKLGPKSnSGLKVGQRVgvgaqvfsclecdrc 106
Cdd:TIGR02824  25 PKA---GEVLIRVAAAGVNRPDLLQRAGKYPPPPgASDILGLEVAGEVVAVGEGV-SRWKVGDRV--------------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    107 kndnepyCtkfvttysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLV-RNGCGPGKKVGI 185
Cdd:TIGR02824  86 -------C-------------ALVAGGGYAEYVAVPAGQVLPVPEGLSLVEAAALPETFFTVWSNLFqRGGLKAGETVLI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    186 VGLGGIG-SMGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEgDWGE--------KYFDTFdLIVVCASSLTD 256
Cdd:TIGR02824 146 HGGASGIgTTAIQLAKAFGARVFTTAGSDEKCAACEALGADIAINYREE-DFVEvvkaetggKGVDVI-LDIVGGSYLNR 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    257 idfNImpKAMKVGGRIVSISI----PEQhemLSLKPYGLKAVSISYSALGS---------IKELNQ-LLKLVSEKDIKIW 322
Cdd:TIGR02824 224 ---NI--KALALDGRIVQIGFqggrKAE---LDLGPLLAKRLTITGSTLRArpvaekaaiAAELREhVWPLLASGRVRPV 295

                         330       340
                  ....*....|....*....|....
gi 2492777    323 V-ETLPVGEAGvhEAFERMEKGDV 345
Cdd:TIGR02824 296 IdKVFPLEDAA--QAHALMESGDH 317
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 28-239 1.37e-10

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: 61.69  E-value: 1.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPfydHDIDIKIEACGVCGSDIHCAAGHWgNMKMPLVVGHEIVGKVVKLGPkSNSGLKVGQRVGvgaqvfsclecdrck 107
Cdd:cd05286  24 PGP---GEVLVRNTAIGVNFIDTYFRSGLY-PLPLPFVLGVEGAGVVEAVGP-GVTGFKVGDRVA--------------- 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  108 ndnepYCTKFvttysqpyedgyvsqGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLT-------VYSP------LVR 174
Cdd:cd05286  84 -----YAGPP---------------GAYAEYRVVPASRLVKLPDGISDETAAALLLQGLTahyllreTYPVkpgdtvLVH 143

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  175 NGCGpGkkvgivglggigsMGTL---ISKAMGAEtyVISR--SSRKREDAMKMGADHYIATLEEgDWGEK 239
Cdd:cd05286 144 AAAG-G-------------VGLLltqWAKALGAT--VIGTvsSEEKAELARAAGADHVINYRDE-DFVER 196
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
 28-176 1.98e-10

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: 61.56  E-value: 1.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKpfyDHDIDIKIEACGVCGSDIHCAAGHWGnMKMPLVVGHEIVGKVVKLGPKSNSgLKVGQRVgVGAQVFSCLECDRCK 107
Cdd:cd08299  30 PK---AHEVRIKIVATGICRSDDHVVSGKLV-TPFPVILGHEAAGIVESVGEGVTT-VKPGDKV-IPLFVPQCGKCRACL 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  108 NDNEPYCTKF-VTTYSQPYEDG-------------YVSQGGYANYVRVHEHFVVPIPEnipshlAAPLL------CGGLT 167
Cdd:cd08299 104 NPESNLCLKNdLGKPQGLMQDGtsrftckgkpihhFLGTSTFSEYTVVDEIAVAKIDA------AAPLEkvcligCGFST 177


                ....*....
gi 2492777  168 VYSPLVRNG 176
Cdd:cd08299 178 GYGAAVNTA 186
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 28-346 4.97e-10

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: 59.90  E-value: 4.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPFyDHDIDIKIEACGVCGSDIHCAAGHWGNmKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVgvgaqvfsclecdrck 107
Cdd:cd08249  22 PKPG-PDEVLVKVKAVALNPVDWKHQDYGFIP-SYPAILGCDFAGTVVEVGSGV-TRFKVGDRV---------------- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  108 ndnepyctkfvTTYSQPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIVG 187
Cdd:cd08249  83 -----------AGFVHGGNPNDPRNGAFQEYVVADADLTAKIPDNISFEEAATLPVGLVTAALALFQKLGLPLPPPKPSP 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  188 LGGIG---------SMGTL---ISKAMGAEtyVISRSSRKREDAMK-MGADH---Y------IATLEEGDWGEKY-FDTF 244
Cdd:cd08249 152 ASKGKpvliwggssSVGTLaiqLAKLAGYK--VITTASPKNFDLVKsLGADAvfdYhdpdvvEDIRAATGGKLRYaLDCI 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  245 ---DLIVVCASSLTDIDfnimpkamkvGGRIVSIS-IPEQHEmlslKPYGLKAVSIS-YSALGSIKE-------LNQLL- 311
Cdd:cd08249 230 stpESAQLCAEALGRSG----------GGKLVSLLpVPEETE----PRKGVKVKFVLgYTVFGEIPEdrefgevFWKYLp 295

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 2492777  312 KLVSEKDIK-IWVETLPVGEAGVHEAFERMEKGDVR 346
Cdd:cd08249 296 ELLEEGKLKpHPVRVVEGGLEGVQEGLDLLRKGKVS 331
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 38-228 5.62e-10

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: 59.95  E-value: 5.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   38 IKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVGAqVFSCLECDRCKNDNEPYCtkf 117
Cdd:cd08285  29 VRPTAVAPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGSEV-KDFKPGDRVIVPA-ITPDWRSVAAQRGYPSQS--- 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  118 vTTYSQPYEDGYVSQGGYANYVRVHEHF--VVPIPENIPshLAAPLLC-------------GGLTVYSPLVRNGCGPgkk 182
Cdd:cd08285 104 -GGMLGGWKFSNFKDGVFAEYFHVNDADanLAPLPDGLT--DEQAVMLpdmmstgfhgaelANIKLGDTVAVFGIGP--- 177

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 2492777  183 vgivglggIGSMGTLISKAMGAeTYVISRSSRKR--EDAMKMGADHYI 228
Cdd:cd08285 178 --------VGLMAVAGARLRGA-GRIIAVGSRPNrvELAKEYGATDIV 216
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 38-346 6.58e-10

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: 59.49  E-value: 6.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   38 IKIEACGVCGSDIHCAAGHWGNM-KMPLVVGHEIVGKVVKLGPkSNSGLKVGQRV-----GVGAQvfsclecdrckndne 111
Cdd:cd08272  32 VRVHASGVNPLDTKIRRGGAAARpPLPAILGCDVAGVVEAVGE-GVTRFRVGDEVygcagGLGGL--------------- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  112 pyctkfvttysqpyedgyvsQGGYANYVRVHEHFVVPIPENIpSHL-AAPLLCGGLTVYSPLVRNG-CGPGKKVgivglg 189
Cdd:cd08272  96 --------------------QGSLAEYAVVDARLLALKPANL-SMReAAALPLVGITAWEGLVDRAaVQAGQTV------ 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  190 gigsmgtLI--------------SKAMGAETYViSRSSRKREDAMKMGADH----------YIATLEEGDWGEKYFDTFD 245
Cdd:cd08272 149 -------LIhggaggvghvavqlAKAAGARVYA-TASSEKAAFARSLGADPiiyyretvveYVAEHTGGRGFDVVFDTVG 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  246 LIVVCASsltdidfnimPKAMKVGGRIVSISIPEQHemlSLKPYGLKAVSISY-------------SALGSIkeLNQLLK 312
Cdd:cd08272 221 GETLDAS----------FEAVALYGRVVSILGGATH---DLAPLSFRNATYSGvftllplltgegrAHHGEI--LREAAR 285

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 2492777  313 LVSEKDIKIWVE--TLPVGEAGvhEAFERMEKGDVR 346
Cdd:cd08272 286 LVERGQLRPLLDprTFPLEEAA--AAHARLESGSAR 319
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 28-343 6.77e-10

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: 59.66  E-value: 6.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPfydHDIDIKIEACGVCGSDIHCAAGhWGNMKMPLVVGHEIVGKVVKLGPKSNSgLKVGQRVgVGAQVFSCLECDRCK 107
Cdd:cd08277  25 PKA---NEVRIKMLATSVCHTDILAIEG-FKATLFPVILGHEGAGIVESVGEGVTN-LKPGDKV-IPLFIGQCGECSNCR 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  108 NDNEPYCTKFVTTYSQPYEDG-------------YVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVR 174
Cdd:cd08277  99 SGKTNLCQKYRANESGLMPDGtsrftckgkkiyhFLGTSTFSQYTVVDENYVAKIDPAAPLEHVCLLGCGFSTGYGAAWN 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  175 NGcgpgkKVGIVGLGGIGSMGTL-ISKAMGAET------YVISRSSRKREDAMKMGADHYIatleegdwGEKYFDTFDLI 247
Cdd:cd08277 179 TA-----KVEPGSTVAVFGLGAVgLSAIMGAKIagasriIGVDINEDKFEKAKEFGATDFI--------NPKDSDKPVSE 245

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  248 VVCASSLTDIDFNI--------MPKAM---KVG-GRIVSISIPEQHEMlSLKPYGLKA-VSISYSALGSIKELNQLLKLV 314
Cdd:cd08277 246 VIREMTGGGVDYSFectgnadlMNEALestKLGwGVSVVVGVPPGAEL-SIRPFQLILgRTWKGSFFGGFKSRSDVPKLV 324

                       330       340       350
                ....*....|....*....|....*....|....*
gi 2492777  315 SE-KDIKIWVE-----TLPVGEagVHEAFERMEKG 343
Cdd:cd08277 325 SKyMNKKFDLDelithVLPFEE--INKGFDLMKSG 357
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 28-154 9.30e-10

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: 59.19  E-value: 9.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPFYDHDID--IKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPkSNSGLKVGQRVGVGAqVFSCLECDR 105
Cdd:cd08286  18 PKPTIQEPTDaiVKMLKTTICGTDLHILKGDVPTVTPGRILGHEGVGVVEEVGS-AVTNFKVGDRVLISC-ISSCGTCGY 95

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 2492777  106 CKNDNEPYCTkfvttySQPYEDGYVSQGGYANYVRV-HEHF-VVPIPENIP 154
Cdd:cd08286  96 CRKGLYSHCE------SGGWILGNLIDGTQAEYVRIpHADNsLYKLPEGVD 140
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 28-343 1.01e-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: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 59.14  E-value: 1.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPFYDHdIDIKIEACGVCGSDIHCAAGHWGN-MKMPLVVGHEIVGKVVKLGPkSNSGLKVGQRVGVgaqvfsclecdrc 106
Cdd:cd08275  22 PEPSSGE-VRVRVEACGLNFADLMARQGLYDSaPKPPFVPGFECAGTVEAVGE-GVKDFKVGDRVMG------------- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  107 kndnepyCTKFvttysqpyedgyvsqGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVY-------------SPLV 173
Cdd:cd08275  87 -------LTRF---------------GGYAEVVNVPADQVFPLPDGMSFEEAAAFPVNYLTAYyalfelgnlrpgqSVLV 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  174 RN---GCGpgkkvgivglggigSMGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEgDWGEK----YFDTFDL 246
Cdd:cd08275 145 HSaagGVG--------------LAAGQLCKTVPNVTVVGTASASKHEALKENGVTHVIDYRTQ-DYVEEvkkiSPEGVDI 209

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  247 IVVCassLTDIDFNIMPKAMKVGGRIVSISIpeqHEMLSLKPYGLKAVSISY----------------SALG-------- 302
Cdd:cd08275 210 VLDA---LGGEDTRKSYDLLKPMGRLVVYGA---ANLVTGEKRSWFKLAKKWwnrpkvdpmklisenkSVLGfnlgwlfe 283

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 2492777  303 ----SIKELNQLLKLVSEKDIK-IWVETLPVGEagVHEAFERMEKG 343
Cdd:cd08275 284 erelLTEVMDKLLKLYEEGKIKpKIDSVFPFEE--VGEAMRRLQSR 327
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 38-345 5.12e-09

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: 57.00  E-value: 5.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   38 IKIEACGVCGSDIHCAAGHWGNmKMPLVVGHEIVGKVVKLGPKSNSgLKVGQRVgVGAQVFSCLECDRCKNDNEPYCTK- 116
Cdd:cd08281  38 VKIAAAGLCHSDLSVINGDRPR-PLPMALGHEAAGVVVEVGEGVTD-LEVGDHV-VLVFVPSCGHCRPCAEGRPALCEPg 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  117 ----------------FVTTYSQPYEDGyVSqgGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLT-----VYSPLVRn 175
Cdd:cd08281 115 aaangagtllsggrrlRLRGGEINHHLG-VS--AFAEYAVVSRRSVVKIDKDVPLEIAALFGCAVLTgvgavVNTAGVR- 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  176 gcgPGKKVGIVGLGGIGSMGTLISKAMGAETYV-ISRSSRKREDAMKMGADHyiaTLEEGDWG------EKYFDTFDLIV 248
Cdd:cd08281 191 ---PGQSVAVVGLGGVGLSALLGAVAAGASQVVaVDLNEDKLALARELGATA---TVNAGDPNaveqvrELTGGGVDYAF 264

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  249 VCASSLTDIDFNImpKAMKVGGRIVSISIPEQHEMLSLKPYGLKAV--SISYSALGSIkelnqllklVSEKDIKIWVE-- 324
Cdd:cd08281 265 EMAGSVPALETAY--EITRRGGTTVTAGLPDPEARLSVPALSLVAEerTLKGSYMGSC---------VPRRDIPRYLAly 333

                       330       340       350
                ....*....|....*....|....*....|..
gi 2492777  325 ---TLPV--------GEAGVHEAFERMEKGDV 345
Cdd:cd08281 334 lsgRLPVdkllthrlPLDEINEGFDRLAAGEA 365
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 38-343 1.07e-08

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 55.47  E-value: 1.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777      38 IKIEACGVCGSDIHCAAGhwgNMKMPLVVGHEIVGKVVKLGPkSNSGLKVGQRVgVGaqvfsclecdrckndnepyctkf 117
Cdd:smart00829   1 IEVRAAGLNFRDVLIALG---LYPGEAVLGGECAGVVTRVGP-GVTGLAVGDRV-MG----------------------- 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777     118 vttysqpyedgyVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVY-------------SPLVRNGCGpgkkvg 184
Cdd:smart00829  53 ------------LAPGAFATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYyalvdlarlrpgeSVLIHAAAG------ 114

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777     185 ivglggigsmGT-----LISKAMGAETYVISRSSRKRE--DAMKMGADHyI--------------ATLEEGdwgekyfdt 243
Cdd:smart00829 115 ----------GVgqaaiQLARHLGAEVFATAGSPEKRDflRALGIPDDH-IfssrdlsfadeilrATGGRG--------- 174

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777     244 FDLIVvcaSSLTDiDFniMPKAMKV---GGRIVSISI-----PEQHEMLSLKPyglkavSISYSA--LGSIKE------- 306
Cdd:smart00829 175 VDVVL---NSLSG-EF--LDASLRClapGGRFVEIGKrdirdNSQLAMAPFRP------NVSYHAvdLDALEEgpdrire 242

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2492777     307 -LNQLLKLVSEKDIK-IWVETLPVGEagVHEAFERMEKG 343
Cdd:smart00829 243 lLAEVLELFAEGVLRpLPVTVFPISD--AEDAFRYMQQG 279
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 16-291 6.38e-08

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: 53.76  E-value: 6.38e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   16 EDWKNPKKTKYDPKpfydhdidIKIEACGVCGSDIHCAAGHWGnmKMP-----LVVGHEIVGKVVKLGPksNSGLKVGQR 90
Cdd:cd08230  16 VDIPEPEPTPGEVL--------VRTLEVGVCGTDREIVAGEYG--TAPpgedfLVLGHEALGVVEEVGD--GSGLSPGDL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   91 VgVGAQVFSCLECDRCKNDNEPYCTKfvTTYsqpYEDGYVSQGGY-ANYVRVHEHFVVPIPENIPSH--LAAPLLCG--- 164
Cdd:cd08230  84 V-VPTVRRPPGKCLNCRIGRPDFCET--GEY---TERGIKGLHGFmREYFVDDPEYLVKVPPSLADVgvLLEPLSVVeka 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  165 ---GLTVYSPLVRNGC------GPGkkvgivglggigSMGTLIS---KAMGAETYVISRSSR---KREDAMKMGAdHYIA 229
Cdd:cd08230 158 ieqAEAVQKRLPTWNPrralvlGAG------------PIGLLAAlllRLRGFEVYVLNRRDPpdpKADIVEELGA-TYVN 224

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2492777  230 TLEEGDWGEKYFDTFDLIVVC--ASSLTdidFNIMPkAMKVGGRIVSISIPEQHEMLSLKPYGL 291
Cdd:cd08230 225 SSKTPVAEVKLVGEFDLIIEAtgVPPLA---FEALP-ALAPNGVVILFGVPGGGREFEVDGGEL 284
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 27-275 1.37e-07

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: 52.59  E-value: 1.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPfYDHDIDIKIEACGVCGSDIHCAAGHWGNM-KMPLVVGHEIVGKVVKLGPkSNSGLKVGQRV---GVGAQVfscle 102
Cdd:cd08253  22 VPTP-GPGEVLVRVHASGVNPVDTYIRAGAYPGLpPLPYVPGSDGAGVVEAVGE-GVDGLKVGDRVwltNLGWGR----- 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  103 cdrckndnepyctkfvttysqpyedgyvSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCG-PGK 181
Cdd:cd08253  95 ----------------------------RQGTAAEYVVVPADQLVPLPDGVSFEQGAALGIPALTAYRALFHRAGAkAGE 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  182 KVgivglggigsmgtLIS--------------KAMGAETYVISRSSRKREDAMKMGADHYIATLEEgDWGEK-----YFD 242
Cdd:cd08253 147 TV-------------LVHggsgavghaavqlaRWAGARVIATASSAEGAELVRQAGADAVFNYRAE-DLADRilaatAGQ 212

                       250       260       270
                ....*....|....*....|....*....|....
gi 2492777  243 TFDLIV-VCASSLTDIDFNImpkaMKVGGRIVSI 275
Cdd:cd08253 213 GVDVIIeVLANVNLAKDLDV----LAPGGRIVVY 242
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
28-232 2.15e-07

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 52.14  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    28 PKPFYDHDIDI--KIEACGVCGSDIHCAAGHwGNMKMPLVVGHEIVGKVVKLGpKSNSGLKVGQRVGVgAQVFSCLECDR 105
Cdd:PRK10309  18 PIPEIKHQDDVlvKVASSGLCGSDIPRIFKN-GAHYYPITLGHEFSGYVEAVG-SGVDDLHPGDAVAC-VPLLPCFTCPE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   106 CKNDNEPYCTK--FVttysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLAA---PLLCGgltVYSPLVRNGCgPG 180
Cdd:PRK10309  95 CLRGFYSLCAKydFI---------GSRRDGGNAEYIVVKRKNLFALPTDMPIEDGAfiePITVG---LHAFHLAQGC-EG 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 2492777   181 KKVGIVGLGGIGSMGTLISKAMGAETY-VISRSSRKREDAMKMGADHYIATLE 232
Cdd:PRK10309 162 KNVIIIGAGTIGLLAIQCAVALGAKSVtAIDINSEKLALAKSLGAMQTFNSRE 214
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 38-272 2.23e-07

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: 51.84  E-value: 2.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   38 IKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGkVVKLGPKSnsGLKVGQRV-----GVGaqvfsclecdrckndnep 112
Cdd:cd08243  32 IRVKAFGLNRSEIFTRQGHSPSVKFPRVLGIEAVG-EVEEAPGG--TFTPGQRVatamgGMG------------------ 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  113 yctkfvTTYSqpyedgyvsqGGYANYVRVHEHFVVPIPENIP-SHLAA-PLLcgGLTVYSPLVRN-GCGPGKKVGIVGLG 189
Cdd:cd08243  91 ------RTFD----------GSYAEYTLVPNEQVYAIDSDLSwAELAAlPET--YYTAWGSLFRSlGLQPGDTLLIRGGT 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  190 GIGSMGTL-ISKAMGAETYVISRSSRKREDAMKMGADHYIatLEEGDWGE---KYFDTFDLI--VVCASSLTDidfniMP 263
Cdd:cd08243 153 SSVGLAALkLAKALGATVTATTRSPERAALLKELGADEVV--IDDGAIAEqlrAAPGGFDKVleLVGTATLKD-----SL 225


                ....*....
gi 2492777  264 KAMKVGGRI 272
Cdd:cd08243 226 RHLRPGGIV 234
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 28-169 7.19e-07

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


Pssm-ID: 176212 [Multi-domain]  Cd Length: 329  Bit Score: 50.33  E-value: 7.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   28 PKPfYDHDIDIKIEACGVCGSDI-HCAAGHWGNMKMPLVVGHEIVGKVVKLGPkSNSGLKVGQRVgvgaqvfsclecdrc 106
Cdd:cd08250  26 PLP-GPGEVLVKNRFVGINASDInFTAGRYDPGVKPPFDCGFEGVGEVVAVGE-GVTDFKVGDAV--------------- 88

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2492777  107 kndnepyctkfvttysqpyedGYVSQGGYANYVRVHEHFVVPIPENIPSHLaaPLLCGGLTVY 169
Cdd:cd08250  89 ---------------------ATMSFGAFAEYQVVPARHAVPVPELKPEVL--PLLVSGLTAS 128
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 60-273 7.82e-07

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: 49.96  E-value: 7.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   60 MKMPLVVGHEIVGKVVKLGPKsNSGLKVGQRVGVGaqvfsclecdrckndnepyctkfvttysqpyedgyvsqGGYANYV 139
Cdd:cd08255  18 LPLPLPPGYSSVGRVVEVGSG-VTGFKPGDRVFCF--------------------------------------GPHAERV 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  140 RVHEHFVVPIPENIPSHLAAP----------LLCGGLTVYSPLVRNGCGP-GKkvgivglggigsMGTLISKAMGAET-Y 207
Cdd:cd08255  59 VVPANLLVPLPDGLPPERAALtalaatalngVRDAEPRLGERVAVVGLGLvGL------------LAAQLAKAAGAREvV 126

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2492777  208 VISRSSRKREDAMKMGADHYIATLEEGDWGEkyfDTFDLIVVCASSLTDIDFNImpKAMKVGGRIV 273
Cdd:cd08255 127 GVDPDAARRELAEALGPADPVAADTADEIGG---RGADVVIEASGSPSALETAL--RLLRDRGRVV 187
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 63-239 9.51e-07

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


Pssm-ID: 176645 [Multi-domain]  Cd Length: 323  Bit Score: 49.97  E-value: 9.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   63 PLVVGHEIVGKVVKLGPKSnSGLKVGQRVGVgaqvfsclecdrckndnepyctkfvttysqpyedgYVSQGGYANYVRVH 142
Cdd:cd05282  57 PAVPGNEGVGVVVEVGSGV-SGLLVGQRVLP-----------------------------------LGGEGTWQEYVVAP 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  143 EHFVVPIPENIPSHLAAPLLCGGLTVY------------SPLVRNGCGP--GKkvgivglggigsMGTLISKAMGAETYV 208
Cdd:cd05282 101 ADDLIPVPDSISDEQAAMLYINPLTAWlmlteylklppgDWVIQNAANSavGR------------MLIQLAKLLGFKTIN 168

                       170       180       190
                ....*....|....*....|....*....|.
gi 2492777  209 ISRSSRKREDAMKMGADHyIATLEEGDWGEK 239
Cdd:cd05282 169 VVRRDEQVEELKALGADE-VIDSSPEDLAQR 198
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
 27-168 7.90e-06

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


Pssm-ID: 176251 [Multi-domain]  Cd Length: 324  Bit Score: 47.21  E-value: 7.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPFYDHDIDIKIEACGVCGSDIHCAAGHWGNMK-MPLVVGHEIVGKVVKLGPKSNSGLKVGQRVGVGAQvfsclecdr 105
Cdd:cd08291  24 EVPEPGPGEVLIKVEAAPINPSDLGFLKGQYGSTKaLPVPPGFEGSGTVVAAGGGPLAQSLIGKRVAFLAG--------- 94

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2492777  106 ckndnepyctkfvttysqpyedgyvSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTV 168
Cdd:cd08291  95 -------------------------SYGTYAEYAVADAQQCLPLPDGVSFEQGASSFVNPLTA 132
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
 34-344 8.00e-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: 8.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   34 HDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSNSgLKVGQRVgVGAQVFSCLECDRCKNDNEPY 113
Cdd:cd08300  28 GEVRIKILATGVCHTDAYTLSGADPEGLFPVILGHEGAGIVESVGEGVTS-VKPGDHV-IPLYTPECGECKFCKSGKTNL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  114 CTKFVTTYSQ---PyeDG-------------YVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPlVRNGC 177
Cdd:cd08300 106 CQKIRATQGKglmP--DGtsrfsckgkpiyhFMGTSTFSEYTVVAEISVAKINPEAPLDKVCLLGCGVTTGYGA-VLNTA 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  178 gpgkKVGIVGLGGIGSMGTL-ISKAMGA------ETYVISRSSRKREDAMKMGADHYI-----------ATLEEGDWGEK 239
Cdd:cd08300 183 ----KVEPGSTVAVFGLGAVgLAVIQGAkaagasRIIGIDINPDKFELAKKFGATDCVnpkdhdkpiqqVLVEMTDGGVD 258

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  240 YfdTFDLIVvcassltdiDFNIMPKAM----KVGGRIVSISIPEQHEMLSLKPYGL------KAvsisySALGSIKELNQ 309
Cdd:cd08300 259 Y--TFECIG---------NVKVMRAALeachKGWGTSVIIGVAAAGQEISTRPFQLvtgrvwKG-----TAFGGWKSRSQ 322

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 2492777  310 LLKLVSE-KDIKIWVE-----TLPVGEagVHEAFERMEKGD 344
Cdd:cd08300 323 VPKLVEDyMKGKIKVDefithTMPLDE--INEAFDLMHAGK 361
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
 27-343 8.74e-06

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


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 47.14  E-value: 8.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   27 DPKPfYDHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSnSGLKVGQRVgvgaqvfsclecdrc 106
Cdd:cd08252  25 KPVP-GGRDLLVRVEAVSVNPVDTKVRAGGAPVPGQPKILGWDASGVVEAVGSEV-TLFKVGDEV--------------- 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  107 kndnepyctkfvttysqpYEDGYVS-QGGYANYVRVHEHFVVPIPENIpSHLAA---PLLcgGLTVY------------- 169
Cdd:cd08252  88 ------------------YYAGDITrPGSNAEYQLVDERIVGHKPKSL-SFAEAaalPLT--SLTAWealfdrlgiseda 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  170 -----SPLVRNGCGpGkkvgivglggIGSMGTLISKAMGAETyVISRSSR--KREDAMKMGADHYI----ATLEEGDWGE 238
Cdd:cd08252 147 enegkTLLIIGGAG-G----------VGSIAIQLAKQLTGLT-VIATASRpeSIAWVKELGADHVInhhqDLAEQLEALG 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  239 kyFDTFDLIVvcasSLTDID--FNIMPKAMKVGGRIVSISipEQHEMLSLKPYGLKAVSI--------SYSALGSI---- 304
Cdd:cd08252 215 --IEPVDYIF----CLTDTDqhWDAMAELIAPQGHICLIV--DPQEPLDLGPLKSKSASFhwefmftrSMFQTPDMieqh 286

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 2492777  305 KELNQLLKLVSEKDIK-IWVETL-PVGEAGVHEAFERMEKG 343
Cdd:cd08252 287 EILNEVADLLDAGKLKtTLTETLgPINAENLREAHALLESG 327
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 33-346 3.24e-05

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: 45.11  E-value: 3.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   33 DHDIDIKIEACGVCGSDIHCAAGHWGNM-KMPLVVGHEIVGKVVKLGPKSNSgLKVGQRVGVGAQVfsclecdrckndne 111
Cdd:cd08251   7 PGEVRIQVRAFSLNFGDLLCVRGLYPTMpPYPFTPGFEASGVVRAVGPHVTR-LAVGDEVIAGTGE-------------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  112 pyctkfvttysqpyedgyvSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIVGLGGI 191
Cdd:cd08251  72 -------------------SMGGHATLVTVPEDQVVRKPASLSFEEACALPVVFLTVIDAFARAGLAKGEHILIQTATGG 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  192 GS-MGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEgdwgekyfdtfdlivvcassltDIDFNIMpkAMkVGG 270
Cdd:cd08251 133 TGlMAVQLARLKGAEIYATASSDDKLEYLKQLGVPHVINYVEE----------------------DFEEEIM--RL-TGG 187

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  271 RIVSISIPE------QHEMLSLKPYGlKAVSISYSALGSIKEL-------NQ------LLKLVSEKDIKIWVEtlpvgea 331
Cdd:cd08251 188 RGVDVVINTlsgeaiQKGLNCLAPGG-RYVEIAMTALKSAPSVdlsvlsnNQsfhsvdLRKLLLLDPEFIADY------- 259

                       330
                ....*....|....*
gi 2492777  332 gVHEAFERMEKGDVR 346
Cdd:cd08251 260 -QAEMVSLVEEGELR 273
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
 65-237 1.21e-04

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


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 43.56  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   65 VVGHEIVGKVVKLGPKSNsGLKVGQRVgvgaqVFSCLECDrcKNDNEPYCTKFVTTYSQP---YEDGYvsqGGYANYVRV 141
Cdd:cd08246  84 IGGSDASGIVWAVGEGVK-NWKVGDEV-----VVHCSVWD--GNDPERAGGDPMFDPSQRiwgYETNY---GSFAQFALV 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  142 HEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVR---NGCGPGKKVGI-VGLGGIGSMGTLISKAMGAETYVISRSSRKRE 217
Cdd:cd08246 153 QATQLMPKPKHLSWEEAAAYMLVGATAYRMLFGwnpNTVKPGDNVLIwGASGGLGSMAIQLARAAGANPVAVVSSEEKAE 232

                       170       180
                ....*....|....*....|
gi 2492777  218 DAMKMGADHYIATLEEGDWG 237
Cdd:cd08246 233 YCRALGAEGVINRRDFDHWG 252
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
223-346 2.30e-04

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 40.78  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777    223 GADHYI----ATLEEGDWGEKYfdtfDLIVVCASSLTDIDFNimpKAMKVGGRIVSISIPEQHEMLSLKPYGLKAVSISY 298
Cdd:pfam13602   2 GADEVIdyrtTDFVQATGGEGV----DVVLDTVGGEAFEASL---RVLPGGGRLVTIGGPPLSAGLLLPARKRGGRGVKY 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2492777    299 SALGSI-----KELNQLLKLVSEKDIKIWV-ETLPVGEAGvhEAFERMEKGDVR 346
Cdd:pfam13602  75 LFLFVRpnlgaDILQELADLIEEGKLRPVIdRVFPLEEAA--EAHRYLESGRAR 126
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 38-164 4.88e-04

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: 41.51  E-value: 4.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777   38 IKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSNsGLKVGQRVgvgAQVFS--CLECDRCKNDNEPYCT 115
Cdd:cd08301  32 IKILHTSLCHTDVYFWEAKGQTPLFPRILGHEAAGIVESVGEGVT-DLKPGDHV---LPVFTgeCKECRHCKSEKSNMCD 107

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2492777  116 KFVTTYSQ--PYEDG-------------YVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCG 164
Cdd:cd08301 108 LLRINTDRgvMINDGksrfsingkpiyhFVGTSTFSEYTVVHVGCVAKINPEAPLDKVCLLSCG 171
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 128-177 1.71e-03

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 40.01  E-value: 1.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 2492777   128 GYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGC 177
Cdd:PTZ00354  88 ALLPGGGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGD 137
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
 125-233 3.23e-03

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


Pssm-ID: 176249 [Multi-domain]  Cd Length: 326  Bit Score: 38.85  E-value: 3.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2492777  125 YEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLT----VYSpLVRNGCGP--GKKVGIVGLGGIGSMGTLI 198
Cdd:cd08289  88 YDLGVSHHGGYSEYARVPAEWVVPLPKGLTLKEAMILGTAGFTaalsIHR-LEENGLTPeqGPVLVTGATGGVGSLAVSI 166

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 2492777  199 SKAMGaetYVISRSSRKREDA---MKMGADHYIATLEE 233
Cdd:cd08289 167 LAKLG---YEVVASTGKADAAdylKKLGAKEVIPREEL 201
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
 133-179 4.74e-03

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


Pssm-ID: 274315 [Multi-domain]  Cd Length: 323  Bit Score: 38.31  E-value: 4.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2492777    133 GGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLT----VYSpLVRNGCGP 179
Cdd:TIGR02823  95 GGYSQYARVPADWLVPLPEGLSLREAMALGTAGFTaalsVMA-LERNGLTP 144
 
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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