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Conserved domains on  [gi|1264919701|gb|PGO54625|]
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alcohol dehydrogenase [Bacillus thuringiensis]

Protein Classification

zinc-dependent alcohol dehydrogenase( domain architecture ID 10169599)

zinc-dependent alcohol dehydrogenase belonging to the medium chain dehydrogenase/reductase (MDR) family, similar to Escherichia coli D-guloside 3-dehydrogenase that catalyzes the NAD(+)-dependent oxidation of the hydroxyl group at C3 of D-gulosides leading to 3-dehydro-D-gulosides

CATH:  3.40.50.720|3.90.180.10
EC:  1.1.1.-
Gene Ontology:  GO:0030554|GO:0016616|GO:0008270
PubMed:  19011745|19011751|12199705|7957243|8749365
SCOP:  3000040

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 53-303 1.66e-53

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: 175.92  E-value: 1.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  53 TDTNPFY-PRKTGYESYGEVIQVGNKVTHVNVGDKVVSFYGHETIGIVKGYKVIRVPSSIQPKVALLSILSCDAAKGVLK 131
Cdd:cd08255    13 TGTEKLPlPLPPGYSSVGRVVEVGSGVTGFKPGDRVFCFGPHAERVVVPANLLVPLPDGLPPERAALTALAATALNGVRD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 132 LNLRQDEKVLITGMGVIGLLACYFLKYYvGVEHVDVVEPNKNRKDFAKKFGAKN-IYDSEEKIIETYNYG--FECSATNS 208
Cdd:cd08255    93 AEPRLGERVAVVGLGLVGLLAAQLAKAA-GAREVVGVDPDAARRELAEALGPADpVAADTADEIGGRGADvvIEASGSPS 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 209 GFHTLQKALKTNGEICILSDGNIEELTLIANFYQKELQIIGSSDG----YDYQKH--ADWFFKEIGK---TPFIEEIFQH 279
Cdd:cd08255   172 ALETALRLLRDRGRVVLVGWYGLKPLLLGEEFHFKRLPIRSSQVYgigrYDRPRRwtEARNLEEALDllaEGRLEALITH 251

                         250       260
                  ....*....|....*....|....
gi 1264919701 280 EIHYTSLIECFDELSLGIIKPLKV 303
Cdd:cd08255   252 RVPFEDAPEAYRLLFEDPPECLKV 275
MDR super family cl16912
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 9-88 1.60e-05

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.


The actual alignment was detected with superfamily member cd08282:

Pssm-ID: 450120 [Multi-domain]  Cd Length: 375  Bit Score: 46.05  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   9 KGPKQLEwetneIKDIQDDEI------IVKTIAGAISiGAELPQYNGSdvtdTNPFYPRKTGYESYGEVIQVGNKVTHVN 82
Cdd:cd08282     7 GGPGNVA-----VEDVPDPKIehptdaIVRITTTAIC-GSDLHMYRGR----TGAEPGLVLGHEAMGEVEEVGSAVESLK 76


                  ....*.
gi 1264919701  83 VGDKVV 88
Cdd:cd08282    77 VGDRVV 82
 
Name Accession Description Interval E-value
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 53-303 1.66e-53

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: 175.92  E-value: 1.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  53 TDTNPFY-PRKTGYESYGEVIQVGNKVTHVNVGDKVVSFYGHETIGIVKGYKVIRVPSSIQPKVALLSILSCDAAKGVLK 131
Cdd:cd08255    13 TGTEKLPlPLPPGYSSVGRVVEVGSGVTGFKPGDRVFCFGPHAERVVVPANLLVPLPDGLPPERAALTALAATALNGVRD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 132 LNLRQDEKVLITGMGVIGLLACYFLKYYvGVEHVDVVEPNKNRKDFAKKFGAKN-IYDSEEKIIETYNYG--FECSATNS 208
Cdd:cd08255    93 AEPRLGERVAVVGLGLVGLLAAQLAKAA-GAREVVGVDPDAARRELAEALGPADpVAADTADEIGGRGADvvIEASGSPS 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 209 GFHTLQKALKTNGEICILSDGNIEELTLIANFYQKELQIIGSSDG----YDYQKH--ADWFFKEIGK---TPFIEEIFQH 279
Cdd:cd08255   172 ALETALRLLRDRGRVVLVGWYGLKPLLLGEEFHFKRLPIRSSQVYgigrYDRPRRwtEARNLEEALDllaEGRLEALITH 251

                         250       260
                  ....*....|....*....|....
gi 1264919701 280 EIHYTSLIECFDELSLGIIKPLKV 303
Cdd:cd08255   252 RVPFEDAPEAYRLLFEDPPECLKV 275
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 6-250 1.61e-34

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: 128.33  E-value: 1.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   6 LIVKGPKQLEWETNEIKDIQDDEIIVKTIAGAISigaelpqynGSDV---TDTNPF--YPRKTGYESYGEVIQVGNKVTH 80
Cdd:COG1063     4 LVLHGPGDLRLEEVPDPEPGPGEVLVRVTAVGIC---------GSDLhiyRGGYPFvrPPLVLGHEFVGEVVEVGEGVTG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  81 VNVGDKVV------------------------SFYGHETIG-------IVKGYKVIRVPSSIQPKVALLS-ILSCdAAKG 128
Cdd:COG1063    75 LKVGDRVVvepnipcgecrycrrgrynlcenlQFLGIAGRDggfaeyvRVPAANLVKVPDGLSDEAAALVePLAV-ALHA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 129 VLKLNLRQDEKVLITGMGVIGLLACYFLKYYvGVEHVDVVEPNKNRKDFAKKFGAKNIYD-SEEKIIE-----TYNYG-- 200
Cdd:COG1063   154 VERAGVKPGDTVLVIGAGPIGLLAALAARLA-GAARVIVVDRNPERLELARELGADAVVNpREEDLVEavrelTGGRGad 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1264919701 201 --FECSATNSGFHTLQKALKTNGEICILSdGNIEELTL-IANFYQKELQIIGS 250
Cdd:COG1063   233 vvIEAVGAPAALEQALDLVRPGGTVVLVG-VPGGPVPIdLNALVRKELTLRGS 284
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 60-227 7.00e-13

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 67.93  E-value: 7.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  60 PRKTGYESYGEVIQVGNKVTHVNVGDKVvSFYGH------------------ETIGI-------------VKGYKVIRVP 108
Cdd:PRK05396   58 PMVVGHEFVGEVVEVGSEVTGFKVGDRV-SGEGHivcghcrncragrrhlcrNTKGVgvnrpgafaeylvIPAFNVWKIP 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 109 SSIQPKVAllSILscD----AAKGVLKLNLrQDEKVLITGMGVIGLLACYFLKyYVGVEHVDVVEPNKNRKDFAKKFGAK 184
Cdd:PRK05396  137 DDIPDDLA--AIF--DpfgnAVHTALSFDL-VGEDVLITGAGPIGIMAAAVAK-HVGARHVVITDVNEYRLELARKMGAT 210

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1264919701 185 NIYD-SEEKIIE-----TYNYGF----ECSATNSGFHTLQKALKTNGEICILS 227
Cdd:PRK05396  211 RAVNvAKEDLRDvmaelGMTEGFdvglEMSGAPSAFRQMLDNMNHGGRIAMLG 263
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
148-265 4.50e-07

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 47.99  E-value: 4.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 148 IGLLACYFLKYYvGVEhVDVVEPNKNRKDFAKKFGAKNIYDSE-----EKIIE-TYNYG----FECSATNSGFHTLQKAL 217
Cdd:pfam00107   2 VGLAAIQLAKAA-GAK-VIAVDGSEEKLELAKELGADHVINPKetdlvEEIKElTGGKGvdvvFDCVGSPATLEQALKLL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1264919701 218 KTNGEICILsdGNIEELT--LIANFYQKELQIIGS--SDGYDYQKHADWFFK 265
Cdd:pfam00107  80 RPGGRVVVV--GLPGGPLplPLAPLLLKELTILGSflGSPEEFPEALDLLAS 129
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 9-88 1.60e-05

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: 46.05  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   9 KGPKQLEwetneIKDIQDDEI------IVKTIAGAISiGAELPQYNGSdvtdTNPFYPRKTGYESYGEVIQVGNKVTHVN 82
Cdd:cd08282     7 GGPGNVA-----VEDVPDPKIehptdaIVRITTTAIC-GSDLHMYRGR----TGAEPGLVLGHEAMGEVEEVGSAVESLK 76


                  ....*.
gi 1264919701  83 VGDKVV 88
Cdd:cd08282    77 VGDRVV 82
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 64-189 1.93e-05

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 45.46  E-value: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   64 GYESYGEVIQVGNKVTHVNVGDKVVSFY--GHETIGIVKGYKVIRVPSSIQ-------PKVALLSILS-CDAAkgvlklN 133
Cdd:smart00829  27 GGECAGVVTRVGPGVTGLAVGDRVMGLApgAFATRVVTDARLVVPIPDGWSfeeaatvPVVFLTAYYAlVDLA------R 100

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  134 LRQDEKVLI-TGMGVIGLLACYFLKyYVGVE-HVDVVEPNKnrKDFAKKFG--AKNIYDS 189
Cdd:smart00829 101 LRPGESVLIhAAAGGVGQAAIQLAR-HLGAEvFATAGSPEK--RDFLRALGipDDHIFSS 157
 
Name Accession Description Interval E-value
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 53-303 1.66e-53

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: 175.92  E-value: 1.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  53 TDTNPFY-PRKTGYESYGEVIQVGNKVTHVNVGDKVVSFYGHETIGIVKGYKVIRVPSSIQPKVALLSILSCDAAKGVLK 131
Cdd:cd08255    13 TGTEKLPlPLPPGYSSVGRVVEVGSGVTGFKPGDRVFCFGPHAERVVVPANLLVPLPDGLPPERAALTALAATALNGVRD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 132 LNLRQDEKVLITGMGVIGLLACYFLKYYvGVEHVDVVEPNKNRKDFAKKFGAKN-IYDSEEKIIETYNYG--FECSATNS 208
Cdd:cd08255    93 AEPRLGERVAVVGLGLVGLLAAQLAKAA-GAREVVGVDPDAARRELAEALGPADpVAADTADEIGGRGADvvIEASGSPS 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 209 GFHTLQKALKTNGEICILSDGNIEELTLIANFYQKELQIIGSSDG----YDYQKH--ADWFFKEIGK---TPFIEEIFQH 279
Cdd:cd08255   172 ALETALRLLRDRGRVVLVGWYGLKPLLLGEEFHFKRLPIRSSQVYgigrYDRPRRwtEARNLEEALDllaEGRLEALITH 251

                         250       260
                  ....*....|....*....|....
gi 1264919701 280 EIHYTSLIECFDELSLGIIKPLKV 303
Cdd:cd08255   252 RVPFEDAPEAYRLLFEDPPECLKV 275
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 6-250 1.61e-34

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: 128.33  E-value: 1.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   6 LIVKGPKQLEWETNEIKDIQDDEIIVKTIAGAISigaelpqynGSDV---TDTNPF--YPRKTGYESYGEVIQVGNKVTH 80
Cdd:COG1063     4 LVLHGPGDLRLEEVPDPEPGPGEVLVRVTAVGIC---------GSDLhiyRGGYPFvrPPLVLGHEFVGEVVEVGEGVTG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  81 VNVGDKVV------------------------SFYGHETIG-------IVKGYKVIRVPSSIQPKVALLS-ILSCdAAKG 128
Cdd:COG1063    75 LKVGDRVVvepnipcgecrycrrgrynlcenlQFLGIAGRDggfaeyvRVPAANLVKVPDGLSDEAAALVePLAV-ALHA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 129 VLKLNLRQDEKVLITGMGVIGLLACYFLKYYvGVEHVDVVEPNKNRKDFAKKFGAKNIYD-SEEKIIE-----TYNYG-- 200
Cdd:COG1063   154 VERAGVKPGDTVLVIGAGPIGLLAALAARLA-GAARVIVVDRNPERLELARELGADAVVNpREEDLVEavrelTGGRGad 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1264919701 201 --FECSATNSGFHTLQKALKTNGEICILSdGNIEELTL-IANFYQKELQIIGS 250
Cdd:COG1063   233 vvIEAVGAPAALEQALDLVRPGGTVVLVG-VPGGPVPIdLNALVRKELTLRGS 284
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 6-250 2.19e-26

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: 106.07  E-value: 2.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   6 LIVKGPKQLEWETNEIKDIQDDEIIVKTIAGAISiGAELPQYNGsdvtDTNPFYPRKTGYESYGEVIQVGNKVTHVNVGD 85
Cdd:cd08234     4 LVYEGPGELEVEEVPVPEPGPDEVLIKVAACGIC-GTDLHIYEG----EFGAAPPLVPGHEFAGVVVAVGSKVTGFKVGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  86 KVV---SFYGHE----------------TIGI-VKG----Y------KVIRVPSSIQPKVA-LLSILSCdAAKGVLKLNL 134
Cdd:cd08234    79 RVAvdpNIYCGEcfycrrgrpnlcenltAVGVtRNGgfaeYvvvpakQVYKIPDNLSFEEAaLAEPLSC-AVHGLDLLGI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 135 RQDEKVLITGMGVIGLLACYFLKYYvGVEHVDVVEPNKNRKDFAKKFGAKNIYDSEEK----IIETYNYGF----ECSAT 206
Cdd:cd08234   158 KPGDSVLVFGAGPIGLLLAQLLKLN-GASRVTVAEPNEEKLELAKKLGATETVDPSREdpeaQKEDNPYGFdvviEATGV 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1264919701 207 NSGFHTLQKALKTNGEICILSDGNIEELTLIANF--YQKELQIIGS 250
Cdd:cd08234   237 PKTLEQAIEYARRGGTVLVFGVYAPDARVSISPFeiFQKELTIIGS 282
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 10-303 5.56e-24

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: 99.61  E-value: 5.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  10 GPKQLEWETNEIKDIQDDEIIVKTIAGAISiGAELPQYNGSDVTdtnpFYPRKTGYESYGEVIQVGNKVTHVNVGDKVVS 89
Cdd:cd08236     8 GPGDLRYEDIPKPEPGPGEVLVKVKACGIC-GSDIPRYLGTGAY----HPPLVLGHEFSGTVEEVGSGVDDLAVGDRVAV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  90 F---------------Y----GHETIGI-----------VKGYKVIRVPSSIQP-KVALLSILSCdAAKGVLKLNLRQDE 138
Cdd:cd08236    83 NpllpcgkceyckkgeYslcsNYDYIGSrrdgafaeyvsVPARNLIKIPDHVDYeEAAMIEPAAV-ALHAVRLAGITLGD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 139 KVLITGMGVIGLLACYFLKYYvGVEHVDVVEPNKNRKDFAKKFGAKNIYDSEEKIIET---------YNYGFECSATNSG 209
Cdd:cd08236   162 TVVVIGAGTIGLLAIQWLKIL-GAKRVIAVDIDDEKLAVARELGADDTINPKEEDVEKvreltegrgADLVIEAAGSPAT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 210 FHTLQKALKTNGEICILsdGN-IEELTLIANFYQK----ELQIIGSSDGYDYQK-HADW-----FFKEiGKtPFIEEIFQ 278
Cdd:cd08236   241 IEQALALARPGGKVVLV--GIpYGDVTLSEEAFEKilrkELTIQGSWNSYSAPFpGDEWrtaldLLAS-GK-IKVEPLIT 316

                         330       340
                  ....*....|....*....|....*
gi 1264919701 279 HEIHYTSLIECFDELSLGIIKPLKV 303
Cdd:cd08236   317 HRLPLEDGPAAFERLADREEFSGKV 341
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 28-250 1.76e-21

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: 91.61  E-value: 1.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  28 EIIVKTIAGAIsigaelpqyNGSDV------TDTNPFYPRKTGYESYGEVIQVGNKVTHVNVGDKVV------------- 88
Cdd:cd05188     1 EVLVRVEAAGL---------CGTDLhirrggYPPPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVvlpnlgcgtcelc 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  89 -------SFYGHETIG------IVKGYKVIRVPSSIQPKVALLSI--LSCdAAKGVLKLN-LRQDEKVLITGMGVIGLLA 152
Cdd:cd05188    72 relcpggGILGEGLDGgfaeyvVVPADNLVPLPDGLSLEEAALLPepLAT-AYHALRRAGvLKPGDTVLVLGAGGVGLLA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 153 CYFLKYYVGveHVDVVEPNKNRKDFAKKFGAKNIYDS-----EEKIIETYNYG----FECSATNSGFHTLQKALKTNGEI 223
Cdd:cd05188   151 AQLAKAAGA--RVIVTDRSDEKLELAKELGADHVIDYkeedlEEELRLTGGGGadvvIDAVGGPETLAQALRLLRPGGRI 228

                         250       260
                  ....*....|....*....|....*...
gi 1264919701 224 CILS-DGNIEELTLIANFYQKELQIIGS 250
Cdd:cd05188   229 VVVGgTSGGPPLDDLRRLLFKELTIIGS 256
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 10-250 4.48e-20

(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: 88.75  E-value: 4.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  10 GPKQLEWETNEIKDIQDDEIIVKTIAGAIsIGAELPQYNGSDV---TDTNPFYPRKT-----GYESYGEVIQVGNKVTHV 81
Cdd:cd08233     8 GRKDIRVEEVPEPPVKPGEVKIKVAWCGI-CGSDLHEYLDGPIfipTEGHPHLTGETapvtlGHEFSGVVVEVGSGVTGF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  82 NVGDKVV------------------------SFYGHETIG-------IVKGYKVIRVPSSIQPKV-ALLSILSCdAAKGV 129
Cdd:cd08233    87 KVGDRVVveptikcgtcgackrglynlcdslGFIGLGGGGggfaeyvVVPAYHVHKLPDNVPLEEaALVEPLAV-AWHAV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 130 LKLNLRQDEKVLITGMGVIGLLACYFLKYyVGVEHVDVVEPNKNRKDFAKKFGAKNIYD-SEEKIIET---------YNY 199
Cdd:cd08233   166 RRSGFKPGDTALVLGAGPIGLLTILALKA-AGASKIIVSEPSEARRELAEELGATIVLDpTEVDVVAEvrkltggggVDV 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1264919701 200 GFECSATNSGFHTLQKALKTNGEICILS------DGNIEELTLianfyqKELQIIGS 250
Cdd:cd08233   245 SFDCAGVQATLDTAIDALRPRGTAVNVAiwekpiSFNPNDLVL------KEKTLTGS 295
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 26-258 2.54e-16

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: 77.74  E-value: 2.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  26 DDEIIVKTIAGAISiGAELPQYNGSDvtdTNPFYPRKTGYESYGEVIQVGNKVTHVNVGDKVVSfyghETIGIV------ 99
Cdd:cd08258    26 PGEVLIKVAAAGIC-GSDLHIYKGDY---DPVETPVVLGHEFSGTIVEVGPDVEGWKVGDRVVS----ETTFSTcgrcpy 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 100 --------------KGYKV-------IRVPSSIQPKV---------ALLSILSCdAAKGVL-KLNLRQDEKVLITGMGVI 148
Cdd:cd08258    98 crrgdynlcphrkgIGTQAdggfaeyVLVPEESLHELpenlsleaaALTEPLAV-AVHAVAeRSGIRPGDTVVVFGPGPI 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 149 GLLACYFLKyYVGVEHVDV-VEPNKNRKDFAKKFGAKNIYDSEEKIIETYNY---------GFECSATNSGFHTLQKALK 218
Cdd:cd08258   177 GLLAAQVAK-LQGATVVVVgTEKDEVRLDVAKELGADAVNGGEEDLAELVNEitdgdgadvVIECSGAVPALEQALELLR 255

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1264919701 219 TNGEICIL-----SDGNIEELTLIanfyQKELQIIGS--SDGYDYQK 258
Cdd:cd08258   256 KGGRIVQVgifgpLAASIDVERII----QKELSVIGSrsSTPASWET 298
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 10-196 1.37e-15

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: 75.86  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  10 GPKQLEWETNEIKDIQDDEIIVKTIAGAIsIGAELPQYNGSDVTDTNPFYPRKTGYESYGEVIQVGNKVTHVNVGDKVV- 88
Cdd:cd08269     3 GPGRFEVEEHPRPTPGPGQVLVRVEGCGV-CGSDLPAFNQGRPWFVYPAEPGGPGHEGWGRVVALGPGVRGLAVGDRVAg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  89 -SFYGHETIGIVKGYKVIRVPSSIQPKVALLSILSCdAAKGVLKLNLRQDEKVLITGMGVIGLLACYFLKyYVGVEHVDV 167
Cdd:cd08269    82 lSGGAFAEYDLADADHAVPLPSLLDGQAFPGEPLGC-ALNVFRRGWIRAGKTVAVIGAGFIGLLFLQLAA-AAGARRVIA 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1264919701 168 VEPNKNRKDFAKKFGA-KNIYDSEEKIIET 196
Cdd:cd08269   160 IDRRPARLALARELGAtEVVTDDSEAIVER 189
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 6-251 2.79e-15

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: 75.32  E-value: 2.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   6 LIVKGPKQLEWETNEIKDIQDDEIIVKTIAGAISigaelpqynGSDV-------TDTNPfyPRKTGYESYGEVIQVGNKV 78
Cdd:cd08235     4 AVLHGPNDVRLEEVPVPEPGPGEVLVKVRACGIC---------GTDVkkirgghTDLKP--PRILGHEIAGEIVEVGDGV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  79 THVNVGDKVVSFY------------GHET------------------------IGIVKGyKVIRVPSSIQPKVALLS-IL 121
Cdd:cd08235    73 TGFKVGDRVFVAPhvpcgechyclrGNENmcpnykkfgnlydggfaeyvrvpaWAVKRG-GVLKLPDNVSFEEAALVePL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 122 SCdAAKGVLKLNLRQDEKVLITGMGVIGLLACyFLKYYVGVEHVDVVEPNKNRKDFAKKFGAKNIYDSEEKII------E 195
Cdd:cd08235   152 AC-CINAQRKAGIKPGDTVLVIGAGPIGLLHA-MLAKASGARKVIVSDLNEFRLEFAKKLGADYTIDAAEEDLvekvreL 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1264919701 196 TYNYGFE----CSATNSGFHTLQKALKTNGEICI---LSDGNIEELTLiANFYQKELQIIGSS 251
Cdd:cd08235   230 TDGRGADvvivATGSPEAQAQALELVRKGGRILFfggLPKGSTVNIDP-NLIHYREITITGSY 291
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 6-250 1.28e-13

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: 70.21  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   6 LIVKGPKQLEWETNEIKDIQDDEIIVKTIAGAISigaelpqynGSDVTdtnpFY------------PRKTGYESYGEVIQ 73
Cdd:cd05285     2 AVLHGPGDLRLEERPIPEPGPGEVLVRVRAVGIC---------GSDVH----YYkhgrigdfvvkePMVLGHESAGTVVA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  74 VGNKVTHVNVGDKV------------------------VSFYG----HETIGivkgyKVIRVPSSIQPKV---------A 116
Cdd:cd05285    69 VGSGVTHLKVGDRVaiepgvpcrtcefcksgrynlcpdMRFAAtppvDGTLC-----RYVNHPADFCHKLpdnvsleegA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 117 LLSILSCdAAKGVLKLNLRQDEKVLITGMGVIGLLACYFLKYYvGVEHVDVVEPNKNRKDFAKKFGAKNIYDSE------ 190
Cdd:cd05285   144 LVEPLSV-GVHACRRAGVRPGDTVLVFGAGPIGLLTAAVAKAF-GATKVVVTDIDPSRLEFAKELGATHTVNVRtedtpe 221

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264919701 191 --EKIIE-----TYNYGFECSATNSGFHTLQKALKTNGEICILSDGNiEELTL-IANFYQKELQIIGS 250
Cdd:cd05285   222 saEKIAEllggkGPDVVIECTGAESCIQTAIYATRPGGTVVLVGMGK-PEVTLpLSAASLREIDIRGV 288
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 6-183 1.33e-13

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: 70.30  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   6 LIVKGPKQLEWETNEIKDIQDDEIIVKTIAGAISiGAELPQYNGsdvtdTNPF--YPRKTGYESYGEVIQVGNKVTHVNV 83
Cdd:cd08261     4 LVCEKPGRLEVVDIPEPVPGAGEVLVRVKRVGIC-GSDLHIYHG-----RNPFasYPRILGHELSGEVVEVGEGVAGLKV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  84 GDKV-VSFY---GH---------------ETIG----------IVKGYKVIRVPSSIQPKVALL----SIlscdAAKGVL 130
Cdd:cd08261    78 GDRVvVDPYiscGEcyacrkgrpnccenlQVLGvhrdggfaeyIVVPADALLVPEGLSLDQAALveplAI----GAHAVR 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1264919701 131 KLNLRQDEKVLITGMGVIGLLACYFLKyYVGVEhVDVVEPNKNRKDFAKKFGA 183
Cdd:cd08261   154 RAGVTAGDTVLVVGAGPIGLGVIQVAK-ARGAR-VIVVDIDDERLEFARELGA 204
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 7-250 1.65e-13

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 69.76  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   7 IVKGPKQ-LEWETNEIKDIQDDEIIVKTIAGAIsigaelpqyNGSDV-----TDTNPFYPRKTGYESYGEVIQVGNKVTH 80
Cdd:COG1064     5 VLTEPGGpLELEEVPRPEPGPGEVLVKVEACGV---------CHSDLhvaegEWPVPKLPLVPGHEIVGRVVAVGPGVTG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  81 VNVGDKV-VSFY-----------GHET-------IG-----------IVKGYKVIRVPSSIQPKVAllSILSCDAA---K 127
Cdd:COG1064    76 FKVGDRVgVGWVdscgtceycrsGRENlcengrfTGyttdggyaeyvVVPARFLVKLPDGLDPAEA--APLLCAGItayR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 128 GVLKLNLRQDEKVLITGMGVIGLLACYFLKYYvGVEhVDVVEPNKNRKDFAKKFGAKNIYDSEE-------KIIETYNYG 200
Cdd:COG1064   154 ALRRAGVGPGDRVAVIGAGGLGHLAVQIAKAL-GAE-VIAVDRSPEKLELARELGADHVVNSSDedpveavRELTGADVV 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1264919701 201 FECSATNSGFHTLQKALKTNGEICILsdGNI-EELTL-IANFYQKELQIIGS 250
Cdd:COG1064   232 IDTVGAPATVNAALALLRRGGRLVLV--GLPgGPIPLpPFDLILKERSIRGS 281
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 26-287 2.92e-13

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: 69.27  E-value: 2.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  26 DDEIIVKTIAGAISiGAELPQYNGsdvTDTNPFYPRKT-GYESYGEVIQVGNKVTHVNVGDKVVSFY------------- 91
Cdd:cd08239    24 PGEVLLRVKASGLC-GSDLHYYYH---GHRAPAYQGVIpGHEPAGVVVAVGPGVTHFRVGDRVMVYHyvgcgacrncrrg 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  92 ------------------GHETIGIVKGYKVIRVPSSIQpkVALLSILSC---DAAKGVLKLNLRQDEKVLITGMGVIGL 150
Cdd:cd08239   100 wmqlctskraaygwnrdgGHAEYMLVPEKTLIPLPDDLS--FADGALLLCgigTAYHALRRVGVSGRDTVLVVGAGPVGL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 151 LACYFLKYyVGVEHVDVVEPNKNRKDFAKKFGAKNIYDSEEKIIE-----TYNYGF----ECSATNSGFHTLQKALKTNG 221
Cdd:cd08239   178 GALMLARA-LGAEDVIGVDPSPERLELAKALGADFVINSGQDDVQeirelTSGAGAdvaiECSGNTAARRLALEAVRPWG 256

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1264919701 222 EICILSDGNIEELTLIANFYQKELQIIGSsdgydyqkhadWFFKEIGKTPFIEEIFQHEIHYTSLI 287
Cdd:cd08239   257 RLVLVGEGGELTIEVSNDLIRKQRTLIGS-----------WYFSVPDMEECAEFLARHKLEVDRLV 311
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 10-218 3.67e-13

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: 68.84  E-value: 3.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  10 GPKQLEWETNEIKDIQ-DDEIIVKTIAGAISiGAELPQYNGSdvTDTNPFyPRKTGYESYGEVIQVGNKVTHVNVGDKVV 88
Cdd:cd05278     8 GPGKIGLEEVPDPKIQgPHDAIVRVTATSIC-GSDLHIYRGG--VPGAKH-GMILGHEFVGEVVEVGSDVKRLKPGDRVS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  89 ---------------SFYGH--ETIGIVKGYKVI------------------RVPSSIQPKVALLsiLSCDAAKG----V 129
Cdd:cd05278    84 vpcitfcgrcrfcrrGYHAHceNGLWGWKLGNRIdggqaeyvrvpyadmnlaKIPDGLPDEDALM--LSDILPTGfhgaE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 130 LKlNLRQDEKVLITGMGVIGLLA---CYFLkyyvGVEHVDVVEPNKNRKDFAKKFGAKNIYDS-----EEKIIE-TYNYG 200
Cdd:cd05278   162 LA-GIKPGSTVAVIGAGPVGLCAvagARLL----GAARIIAVDSNPERLDLAKEAGATDIINPkngdiVEQILElTGGRG 236

                         250
                  ....*....|....*....
gi 1264919701 201 FECSATNSGF-HTLQKALK 218
Cdd:cd05278   237 VDCVIEAVGFeETFEQAVK 255
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 60-227 7.00e-13

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 67.93  E-value: 7.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  60 PRKTGYESYGEVIQVGNKVTHVNVGDKVvSFYGH------------------ETIGI-------------VKGYKVIRVP 108
Cdd:PRK05396   58 PMVVGHEFVGEVVEVGSEVTGFKVGDRV-SGEGHivcghcrncragrrhlcrNTKGVgvnrpgafaeylvIPAFNVWKIP 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 109 SSIQPKVAllSILscD----AAKGVLKLNLrQDEKVLITGMGVIGLLACYFLKyYVGVEHVDVVEPNKNRKDFAKKFGAK 184
Cdd:PRK05396  137 DDIPDDLA--AIF--DpfgnAVHTALSFDL-VGEDVLITGAGPIGIMAAAVAK-HVGARHVVITDVNEYRLELARKMGAT 210

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1264919701 185 NIYD-SEEKIIE-----TYNYGF----ECSATNSGFHTLQKALKTNGEICILS 227
Cdd:PRK05396  211 RAVNvAKEDLRDvmaelGMTEGFdvglEMSGAPSAFRQMLDNMNHGGRIAMLG 263
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 6-196 8.23e-11

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: 61.89  E-value: 8.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   6 LIVKGPKQLEWETNEIKDIQD-DEIIVKTIAGAISiGAELPQYNGSDVTDTNPFyprkTGYESYGEVIQVGNKVTHVNVG 84
Cdd:cd08284     4 VVFKGPGDVRVEEVPIPQIQDpTDAIVKVTAAAIC-GSDLHIYRGHIPSTPGFV----LGHEFVGEVVEVGPEVRTLKVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  85 DKVVS------------------------FYGHETIGIVKGYK------------VIRVPSSIQPKVALL--SILSCdAA 126
Cdd:cd08284    79 DRVVSpftiacgecfycrrgqsgrcakggLFGYAGSPNLDGAQaeyvrvpfadgtLLKLPDGLSDEAALLlgDILPT-GY 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 127 KGVLKLNLRQDEKVLITGMGVIGLLACYFLKYYvGVEHVDVVEPNKNRKDFAKKFGAKNIYDSEEKIIET 196
Cdd:cd08284   158 FGAKRAQVRPGDTVAVIGCGPVGLCAVLSAQVL-GAARVFAVDPVPERLERAAALGAEPINFEDAEPVER 226
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 64-250 2.42e-10

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: 60.34  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  64 GYESYGEVIQVGNKVTHVNVGDKVVSFY------------GHET---------IGIVKGY---------KVIRVPSSIQP 113
Cdd:cd08254    61 GHEIAGTVVEVGAGVTNFKVGDRVAVPAvipcgacalcrrGRGNlclnqgmpgLGIDGGFaeyivvparALVPVPDGVPF 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 114 KVAllSILScDA----------AKGVlklnlRQDEKVLITGMGVIGLLACYFLKYYVGveHVDVVEPNKNRKDFAKKFGA 183
Cdd:cd08254   141 AQA--AVAT-DAvltpyhavvrAGEV-----KPGETVLVIGLGGLGLNAVQIAKAMGA--AVIAVDIKEEKLELAKELGA 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1264919701 184 KNIYDSEEKIIETYNYG---------FECSATNSGFHTLQKALKTNGEICILSDGNiEELTL-IANFYQKELQIIGS 250
Cdd:cd08254   211 DEVLNSLDDSPKDKKAAglgggfdviFDFVGTQPTFEDAQKAVKPGGRIVVVGLGR-DKLTVdLSDLIARELRIIGS 286
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 20-227 1.45e-09

Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)- dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria) and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 58.01  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  20 EIKDIQDDEIIVKTIAGAISiGAELPQYNGSDVTDTNPFYPRKTGYESYGEVIQVGNKVTHVNVGDKVvSFYGH------ 93
Cdd:cd05281    19 PVPKPGPGEVLIKVLAASIC-GTDVHIYEWDEWAQSRIKPPLIFGHEFAGEVVEVGEGVTRVKVGDYV-SAETHivcgkc 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  94 --------------ETIGI-----------VKGYKVIRVPSSIQPKVAllSILS--CDAAKGVLKLNLRqDEKVLITGMG 146
Cdd:cd05281    97 yqcrtgnyhvcqntKILGVdtdgcfaeyvvVPEENLWKNDKDIPPEIA--SIQEplGNAVHTVLAGDVS-GKSVLITGCG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 147 VIGLLACYFLKYyVGVEHVDVVEPNKNRKDFAKKFGAKNIYDSEEK----IIETYNYG-----FECS----ATNSGFhtl 213
Cdd:cd05281   174 PIGLMAIAVAKA-AGASLVIASDPNPYRLELAKKMGADVVINPREEdvveVKSVTDGTgvdvvLEMSgnpkAIEQGL--- 249

                         250
                  ....*....|....
gi 1264919701 214 qKALKTNGEICILS 227
Cdd:cd05281   250 -KALTPGGRVSILG 262
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 6-210 5.77e-09

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: 56.50  E-value: 5.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   6 LIVKGPKQLEWETNEIKDIQDDEIIVKTIAGAISiGAELPQYNGSDVTDTNPFYPrktGYESYGEVIQVGNKVT------ 79
Cdd:cd08231     5 VLTGPGKPLEIREVPLPDLEPGAVLVRVRLAGVC-GSDVHTVAGRRPRVPLPIIL---GHEGVGRVVALGGGVTtdvage 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  80 HVNVGDKVVS------------------------FYGHET--------------IGIVKGYKVIRVPSSIQPKVALLSil 121
Cdd:cd08231    81 PLKVGDRVTWsvgapcgrcyrclvgdptkcenrkKYGHEAscddphlsggyaehIYLPPGTAIVRVPDNVPDEVAAPA-- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 122 SC---DAAKGVLKLNLRQ-DEKVLITGMGVIGLLACYFLKYyVGVEHVDVVEPNKNRKDFAKKFGAKNIYDSEE------ 191
Cdd:cd08231   159 NCalaTVLAALDRAGPVGaGDTVVVQGAGPLGLYAVAAAKL-AGARRVIVIDGSPERLELAREFGADATIDIDElpdpqr 237

                         250       260
                  ....*....|....*....|....*.
gi 1264919701 192 -KIIE--TYNYG----FECSATNSGF 210
Cdd:cd08231   238 rAIVRdiTGGRGadvvIEASGHPAAV 263
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 6-223 6.28e-09

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: 56.10  E-value: 6.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   6 LIVKGPKQLEWETNEIKDIQD-DEIIVKTIAGAISiGAELPQYNGsDVTDTNPfyPRKTGYESYGEVIQVGNKVTHVNVG 84
Cdd:cd08286     4 LVYHGPGKISWEDRPKPTIQEpTDAIVKMLKTTIC-GTDLHILKG-DVPTVTP--GRILGHEGVGVVEEVGSAVTNFKVG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  85 DKVV---------------SFYGH-ETIGIVKGYKV-----------------IRVPSSIQPKVAL-LS-ILSCDAAKGV 129
Cdd:cd08286    80 DRVLiscisscgtcgycrkGLYSHcESGGWILGNLIdgtqaeyvriphadnslYKLPEGVDEEAAVmLSdILPTGYECGV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 130 LKLNLRQDEKVLITGMGVIGLLACYFLKYYvGVEHVDVVEPNKNRKDFAKKFGA-KNIYDSEEKIIE-----TYNYGF-- 201
Cdd:cd08286   160 LNGKVKPGDTVAIVGAGPVGLAALLTAQLY-SPSKIIMVDLDDNRLEVAKKLGAtHTVNSAKGDAIEqvlelTDGRGVdv 238

                         250       260
                  ....*....|....*....|....
gi 1264919701 202 --ECSATNSGFHTLQKALKTNGEI 223
Cdd:cd08286   239 viEAVGIPATFELCQELVAPGGHI 262
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 7-197 1.00e-07

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 52.73  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   7 IVKGPKQ-LEWETNEIKDIQDDEIIVKTIAGAISIgAELPQYNGsdvtdtnpFYPRKT-----GYESYGEVIQVGNKVTH 80
Cdd:PRK13771    5 ILPGFKQgYRIEEVPDPKPGKDEVVIKVNYAGLCY-RDLLQLQG--------FYPRMKypvilGHEVVGTVEEVGENVKG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  81 VNVGDKVVSF------------------------YGHETIGI------VKGYKVIRVPSSIQPKVAllSILSCDAA---K 127
Cdd:PRK13771   76 FKPGDRVASLlyapdgtceycrsgeeaycknrlgYGEELDGFfaeyakVKVTSLVKVPPNVSDEGA--VIVPCVTGmvyR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1264919701 128 GVLKLNLRQDEKVLITGMGviGllacyflkyYVGVEHVDVvepnknrkdfAKKFGAKNI----YDSEEKIIETY 197
Cdd:PRK13771  154 GLRRAGVKKGETVLVTGAG--G---------GVGIHAIQV----------AKALGAKVIavtsSESKAKIVSKY 206
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 10-251 1.18e-07

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: 52.46  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  10 GPKQLEWETNEIKDIQDDEIIVKTIAGAIsigaelpqyNGSDV------TDTNPFYPRKTGYESYGEVIQVGNKVTHVNV 83
Cdd:COG0604    11 GPEVLELEEVPVPEPGPGEVLVRVKAAGV---------NPADLlirrglYPLPPGLPFIPGSDAAGVVVAVGEGVTGFKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  84 GDKVVSFYGH----ETIgIVKGYKVIRVPSSIQPKVAllSILSCDA--AKGVL--KLNLRQDEKVLITGM-GVIGLLACY 154
Cdd:COG0604    82 GDRVAGLGRGggyaEYV-VVPADQLVPLPDGLSFEEA--AALPLAGltAWQALfdRGRLKPGETVLVHGAaGGVGSAAVQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 155 FLKYYvGVeHVDVVEPNKNRKDFAKKFGAKNIYDSEEK----------IIETYNYGFEcSATNSGFHTLQKALKTNGEIC 224
Cdd:COG0604   159 LAKAL-GA-RVIATASSPEKAELLRALGADHVIDYREEdfaervraltGGRGVDVVLD-TVGGDTLARSLRALAPGGRLV 235

                         250       260
                  ....*....|....*....|....*....
gi 1264919701 225 I--LSDGNIEELTLiANFYQKELQIIGSS 251
Cdd:COG0604   236 SigAASGAPPPLDL-APLLLKGLTLTGFT 263
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 10-158 1.25e-07

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: 52.06  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  10 GPKQLEWETNEIKDIQDDEIIVK-TIAGAisigaelpqyNGSDVTDTNPFYPRKT----GYESYGEVIQVGNKVTHVNVG 84
Cdd:cd05286    10 GPEVLEYEDVPVPEPGPGEVLVRnTAIGV----------NFIDTYFRSGLYPLPLpfvlGVEGAGVVEAVGPGVTGFKVG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  85 DKVVSF-----YGHETigIVKGYKVIRVPSSIQPKVA---LL-----SILSCDAAKgvlklnLRQDEKVLITG--MGViG 149
Cdd:cd05286    80 DRVAYAgppgaYAEYR--VVPASRLVKLPDGISDETAaalLLqgltaHYLLRETYP------VKPGDTVLVHAaaGGV-G 150


                  ....*....
gi 1264919701 150 LLACYFLKY 158
Cdd:cd05286   151 LLLTQWAKA 159
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 20-253 1.28e-07

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: 52.35  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  20 EIKDIQD-----DEIIVK-TIAGAISIgaelpQYNGSDVTDTNPFyPRKTGYESYGEVIQVGNKVTHVNVGDKVVSF--- 90
Cdd:cd08264    15 KVEDVKDpkpgpGEVLIRvKMAGVNPV-----DYNVINAVKVKPM-PHIPGAEFAGVVEEVGDHVKGVKKGDRVVVYnrv 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  91 ---------YGHET-------IGIVK--GYK---------VIRVPSSIQPKVAL-LSILSCDAAKGVLKLNLRQDEKVLI 142
Cdd:cd08264    89 fdgtcdmclSGNEMlcrnggiIGVVSngGYAeyivvpeknLFKIPDSISDELAAsLPVAALTAYHALKTAGLGPGETVVV 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 143 TGM-GVIGLLACYFLKYYVGveHVDVVepnkNRKDFAKKFGAKNIYDSEEkIIETYNYGFEC------SATNSGFHTLQK 215
Cdd:cd08264   169 FGAsGNTGIFAVQLAKMMGA--EVIAV----SRKDWLKEFGADEVVDYDE-VEEKVKEITKMadvvinSLGSSFWDLSLS 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1264919701 216 ALKTNGEIC---ILSDGNIEelTLIANFYQKELQIIGSSDG 253
Cdd:cd08264   242 VLGRGGRLVtfgTLTGGEVK--LDLSDLYSKQISIIGSTGG 280
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 13-229 1.30e-07

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 52.28  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  13 QLEWETNEIKDIQDDEIIVKTIAGAIS------IGAELPqyngsdvtdtNPFYPRKTGYESYGEVIQVGNKVTHVNVGDK 86
Cdd:cd08271    14 QLTLEEIEIPGPGAGEVLVKVHAAGLNpvdwkvIAWGPP----------AWSYPHVPGVDGAGVVVAVGAKVTGWKVGDR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  87 VVsfyGHETIG---------IVKGYKVIRVPSSIQPKVAllSILSCdAAKGVL-----KLNLRQDEKVLITG-MGVIGLL 151
Cdd:cd08271    84 VA---YHASLArggsfaeytVVDARAVLPLPDSLSFEEA--AALPC-AGLTAYqalfkKLRIEAGRTILITGgAGGVGSF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 152 ACYFLKYYvgVEHVDVVEPNKNRkDFAKKFGAKNIYDSE-----EKIIE-TYNYGFECS-ATNSGFH--TLQKALKTNGE 222
Cdd:cd08271   158 AVQLAKRA--GLRVITTCSKRNF-EYVKSLGADHVIDYNdedvcERIKEiTGGRGVDAVlDTVGGETaaALAPTLAFNGH 234


                  ....*..
gi 1264919701 223 ICILSDG 229
Cdd:cd08271   235 LVCIQGR 241
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 6-226 1.48e-07

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: 52.12  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   6 LIVKGPKQ-LEWETNEIKDIQDDEIIVKTIAGAI--------SIGAELPqyngsdvtdtnpfYPRKTGYESYGEVIQVGN 76
Cdd:cd08278     6 AVVREPGGpFVLEDVELDDPRPDEVLVRIVATGIchtdlvvrDGGLPTP-------------LPAVLGHEGAGVVEAVGS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  77 KVTHVNVGDKVV-SF--------------------------------------YGHETIG-------------IVKGYKV 104
Cdd:cd08278    73 AVTGLKPGDHVVlSFascgecanclsghpaycenffplnfsgrrpdgstplslDDGTPVHghffgqssfatyaVVHERNV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 105 IRVPSSIQPkvALLSILSC---DAAKGVL-KLNLRQDEKVLITGMGVIGLLACYFLKyYVGVEHVDVVEPNKNRKDFAKK 180
Cdd:cd08278   153 VKVDKDVPL--ELLAPLGCgiqTGAGAVLnVLKPRPGSSIAVFGAGAVGLAAVMAAK-IAGCTTIIAVDIVDSRLELAKE 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1264919701 181 FGAKNIYDS-EEKIIETY--------NYGFECSATNSGFHTLQKALKTNGEICIL 226
Cdd:cd08278   230 LGATHVINPkEEDLVAAIreitgggvDYALDTTGVPAVIEQAVDALAPRGTLALV 284
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 55-152 2.73e-07

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: 51.27  E-value: 2.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  55 TNPFYPRKTGYESYGEVIQVGNKVTHVNVGDKVVSFYG-----HETIGIVKGYKVIRVPSSIQ-------PKVALLSIls 122
Cdd:cd08251    33 TMPPYPFTPGFEASGVVRAVGPHVTRLAVGDEVIAGTGesmggHATLVTVPEDQVVRKPASLSfeeacalPVVFLTVI-- 110

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1264919701 123 cDAAKgvlKLNLRQDEKVLI-TGMGVIGLLA 152
Cdd:cd08251   111 -DAFA---RAGLAKGEHILIqTATGGTGLMA 137
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
148-265 4.50e-07

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 47.99  E-value: 4.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 148 IGLLACYFLKYYvGVEhVDVVEPNKNRKDFAKKFGAKNIYDSE-----EKIIE-TYNYG----FECSATNSGFHTLQKAL 217
Cdd:pfam00107   2 VGLAAIQLAKAA-GAK-VIAVDGSEEKLELAKELGADHVINPKetdlvEEIKElTGGKGvdvvFDCVGSPATLEQALKLL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1264919701 218 KTNGEICILsdGNIEELT--LIANFYQKELQIIGS--SDGYDYQKHADWFFK 265
Cdd:pfam00107  80 RPGGRVVVV--GLPGGPLplPLAPLLLKELTILGSflGSPEEFPEALDLLAS 129
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 6-250 4.53e-07

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. 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: 50.39  E-value: 4.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   6 LIVKGPKQLEWETNEIKDIQDDEIIVKTIAGAISiGAELPQYNGsdvtdtnpFYPRKT-----GYESYGEVIQVGNKVTH 80
Cdd:cd08259     5 ILHKPNKPLQIEEVPDPEPGPGEVLIKVKAAGVC-YRDLLFWKG--------FFPRGKyplilGHEIVGTVEEVGEGVER 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  81 VNVGDKVVS------------------------FYGHETIG------IVKGYKVIRVPSSIQPKVAllSILSCDAAKGVL 130
Cdd:cd08259    76 FKPGDRVILyyyipcgkceyclsgeenlcrnraEYGEEVDGgfaeyvKVPERSLVKLPDNVSDESA--ALAACVVGTAVH 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 131 KLN---LRQDEKVLITG-MGVIGLLACYFLKYYvGVEhVDVVEPNKNRKDFAKKFGAKNIYDSEEKIIETYNYG-----F 201
Cdd:cd08259   154 ALKragVKKGDTVLVTGaGGGVGIHAIQLAKAL-GAR-VIAVTRSPEKLKILKELGADYVIDGSKFSEDVKKLGgadvvI 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1264919701 202 ECSATNSGFHTLqKALKTNGEICIL--SDGNIEELTLiANFYQKELQIIGS 250
Cdd:cd08259   232 ELVGSPTIEESL-RSLNKGGRLVLIgnVTPDPAPLRP-GLLILKEIRIIGS 280
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 6-227 6.18e-07

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: 50.27  E-value: 6.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   6 LIVKGPKQLEWETNEIK--DIQDDEIIVKTIAGAIsigaelpqyNGSDV----TDTNPFYPRKTGYESYGEVIQVGNKVT 79
Cdd:cd08249     4 AVLTGPGGGLLVVVDVPvpKPGPDEVLVKVKAVAL---------NPVDWkhqdYGFIPSYPAILGCDFAGTVVEVGSGVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  80 HVNVGDKVVSF-----YGHETIG------IVKGYKVIRVPSSIQPK------VALLSilscdAAKGV---LKLNLR---- 135
Cdd:cd08249    75 RFKVGDRVAGFvhggnPNDPRNGafqeyvVADADLTAKIPDNISFEeaatlpVGLVT-----AALALfqkLGLPLPppkp 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 136 ----QDEKVLITGmG--VIGLLACYFLKYYvGVEHVDVVEPnKNrKDFAKKFGAKNIYDS------EEKIIETYN---YG 200
Cdd:cd08249   150 spasKGKPVLIWG-GssSVGTLAIQLAKLA-GYKVITTASP-KN-FDLVKSLGADAVFDYhdpdvvEDIRAATGGklrYA 225

                         250       260
                  ....*....|....*....|....*..
gi 1264919701 201 FECSATNSGFHTLQKALKTNGEICILS 227
Cdd:cd08249   226 LDCISTPESAQLCAEALGRSGGGKLVS 252
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 27-88 8.77e-07

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: 46.83  E-value: 8.77e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1264919701  27 DEIIVKTIAGAIsigaelpqyNGSD---VTDTNPF--YPRKTGYESYGEVIQVGNKVTHVNVGDKVV 88
Cdd:pfam08240   1 GEVLVKVKAAGI---------CGSDlhiYKGGNPPvkLPLILGHEFAGEVVEVGPGVTGLKVGDRVV 58
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 56-299 1.17e-06

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: 49.24  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  56 NPFYPRKTGYESYGEVIQVGNKVTHVNVGDKV-------------------------------VSFYGHETIGIVKGYKV 104
Cdd:cd08245    50 GSKYPLVPGHEIVGEVVEVGAGVEGRKVGDRVgvgwlvgscgrceycrrglenlcqkavntgyTTQGGYAEYMVADAEYT 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 105 IRVPSSIQpkVALLSILSC---DAAKGVLKLNLRQDEKVLITGMGVIGLLACYFLKyYVGVeHVDVVEPNKNRKDFAKKF 181
Cdd:cd08245   130 VLLPDGLP--LAQAAPLLCagiTVYSALRDAGPRPGERVAVLGIGGLGHLAVQYAR-AMGF-ETVAITRSPDKRELARKL 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 182 GAKNIYDS-EEKIIETYNYGFE----CSATNSGFHTLQKALKTNGEI-CILSDGNIEELTLIANFYQKELQIIGSSDG-- 253
Cdd:cd08245   206 GADEVVDSgAELDEQAAAGGADvilvTVVSGAAAEAALGGLRRGGRIvLVGLPESPPFSPDIFPLIMKRQSIAGSTHGgr 285

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1264919701 254 YDYQKHADwFFKEIGKTPFIEEIFQHEIHytsliECFDELSLGIIK 299
Cdd:cd08245   286 ADLQEALD-FAAEGKVKPMIETFPLDQAN-----EAYERMEKGDVR 325
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 10-196 1.19e-06

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: 49.46  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  10 GPKQLEWETNEIKDIQD-DEIIVKTIAGAISiGAELPQYNGSdVTDTNPfyPRKTGYESYGEVIQVGNKVTHVNVGDKVV 88
Cdd:cd08283     8 GKGDVRVEEVPDPKIEDpTDAIVRVTATAIC-GSDLHLYHGY-IPGMKK--GDILGHEFMGVVEEVGPEVRNLKVGDRVV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  89 -SF------------------------------YGHETIGIVkGY---------------KV-------IRVPSSIQP-K 114
Cdd:cd08283    84 vPFtiacgecfyckrglysqcdntnpsaemaklYGHAGAGIF-GYshltggyaggqaeyvRVpfadvgpFKIPDDLSDeK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 115 VALLSILSCDAAKGVLKLNLRQDEKVLITGMGVIGLLACYFLKyYVGVEHVDVVEPNKNRKDFAKKF-GAKNI-YDSEEK 192
Cdd:cd08283   163 ALFLSDILPTGYHAAELAEVKPGDTVAVWGCGPVGLFAARSAK-LLGAERVIAIDRVPERLEMARSHlGAETInFEEVDD 241


                  ....
gi 1264919701 193 IIET 196
Cdd:cd08283   242 VVEA 245
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 10-188 2.26e-06

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


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 48.35  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  10 GPKQLEWETNEIKDIQDDEIIVKTIAGAIsigaelpqyNGSDVT------DTNPFYPRKTGYESYGEVIQVGNKVTHVNV 83
Cdd:cd08275    10 GLDKLKVEKEALPEPSSGEVRVRVEACGL---------NFADLMarqglyDSAPKPPFVPGFECAGTVEAVGEGVKDFKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  84 GDKV---VSFYGHETIGIVKGYKVIRVPSSIQ-PKVALLSILSCDAAKGVLKL-NLRQDEKVLI--TGMGViGLLACYFL 156
Cdd:cd08275    81 GDRVmglTRFGGYAEVVNVPADQVFPLPDGMSfEEAAAFPVNYLTAYYALFELgNLRPGQSVLVhsAAGGV-GLAAGQLC 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1264919701 157 KYyvgVEHVDVV-EPNKNRKDFAKKFGAKNIYD 188
Cdd:cd08275   160 KT---VPNVTVVgTASASKHEALKENGVTHVID 189
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 59-250 3.09e-06

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: 47.88  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  59 YPRKTGYESYGEVIQVGNKVTHVNVGDKV---------------------------VSFYGHETIG-----------IVK 100
Cdd:cd05283    53 YPLVPGHEIVGIVVAVGSKVTKFKVGDRVgvgcqvdscgtceqcksgeeqycpkgvVTYNGKYPDGtitqggyadhiVVD 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 101 GYKVIRVPSSIQPKVA--LL-------SILscdaakgvLKLNLRQDEKVLITGMGVIGLLACYFLKyYVGVEhVDVVEPN 171
Cdd:cd05283   133 ERFVFKIPEGLDSAAAapLLcagitvySPL--------KRNGVGPGKRVGVVGIGGLGHLAVKFAK-ALGAE-VTAFSRS 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 172 KNRKDFAKKFGAKNIYDS-EEKIIETYNYGFE----CSATNSGFHTLQKALKTNGEICILSDGNIEELTLIANFYQKELQ 246
Cdd:cd05283   203 PSKKEDALKLGADEFIATkDPEAMKKAAGSLDliidTVSASHDLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGRKS 282


                  ....
gi 1264919701 247 IIGS 250
Cdd:cd05283   283 VAGS 286
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 59-210 3.72e-06

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: 48.00  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  59 YPRKTGYESYGEVIQVGNKVTHVNVGDKVVSF------------YGHETI------------G------IVKGYKVIRVP 108
Cdd:cd08240    66 LPLVLGHEIVGEVVAVGPDAADVKVGDKVLVYpwigcgecpvclAGDENLcakgralgifqdGgyaeyvIVPHSRYLVDP 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 109 SSIQPKVAllSILSCD---AAKGVLKLNLR-QDEKVLITGMGVIGLLACYFLKYYVGVEHVdVVEPNKNRKDFAKKFGAK 184
Cdd:cd08240   146 GGLDPALA--ATLACSgltAYSAVKKLMPLvADEPVVIIGAGGLGLMALALLKALGPANII-VVDIDEAKLEAAKAAGAD 222

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1264919701 185 NIYDSEE-----KIIEtynygfecsATNSGF 210
Cdd:cd08240   223 VVVNGSDpdaakRIIK---------AAGGGV 244
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 13-226 1.43e-05

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: 45.97  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  13 QLEWETNEIKDIQDDEIIVKTIAGAISigaelpqynGSDV----TDTNPF--------YPRKTGYESYGEVIQVGNKVTH 80
Cdd:cd08265    38 ELRVEDVPVPNLKPDEILIRVKACGIC---------GSDIhlyeTDKDGYilypglteFPVVIGHEFSGVVEKTGKNVKN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  81 VNVGDKVVS---------------FYGH-ETIGIVkGYKV-------IRVPSSIQPKV----------------ALLSIL 121
Cdd:cd08265   109 FEKGDPVTAeemmwcgmcracrsgSPNHcKNLKEL-GFSAdgafaeyIAVNARYAWEInelreiysedkafeagALVEPT 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 122 SCdAAKGVLKL--NLRQDEKVLITGMGVIGLLACYFLKyYVGVEHVDVVEPNKNRKDFAKKFGAKNIYD--------SEE 191
Cdd:cd08265   188 SV-AYNGLFIRggGFRPGAYVVVYGAGPIGLAAIALAK-AAGASKVIAFEISEERRNLAKEMGADYVFNptkmrdclSGE 265

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1264919701 192 KIIE-TYNYG--FECSATNSGFHT---LQKALKTNGEICIL 226
Cdd:cd08265   266 KVMEvTKGWGadIQVEAAGAPPATipqMEKSIAINGKIVYI 306
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 64-183 1.58e-05

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: 45.76  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  64 GYESYGEVIQVGNKVTH-VNVGDKVVS--------------FYGHETIGivkGY---------KVIRVPSSIQPK-VALL 118
Cdd:cd08262    68 GHEFCGEVVDYGPGTERkLKVGTRVTSlplllcgqgascgiGLSPEAPG---GYaeymllseaLLLRVPDGLSMEdAALT 144

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1264919701 119 SILSCdAAKGVLKLNLRQDEKVLITGMGVIGLLACYFLKYYvGVEHVDVVEPNKNRKDFAKKFGA 183
Cdd:cd08262   145 EPLAV-GLHAVRRARLTPGEVALVIGCGPIGLAVIAALKAR-GVGPIVASDFSPERRALALAMGA 207
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 9-88 1.60e-05

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: 46.05  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   9 KGPKQLEwetneIKDIQDDEI------IVKTIAGAISiGAELPQYNGSdvtdTNPFYPRKTGYESYGEVIQVGNKVTHVN 82
Cdd:cd08282     7 GGPGNVA-----VEDVPDPKIehptdaIVRITTTAIC-GSDLHMYRGR----TGAEPGLVLGHEAMGEVEEVGSAVESLK 76


                  ....*.
gi 1264919701  83 VGDKVV 88
Cdd:cd08282    77 VGDRVV 82
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 64-189 1.93e-05

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 45.46  E-value: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701   64 GYESYGEVIQVGNKVTHVNVGDKVVSFY--GHETIGIVKGYKVIRVPSSIQ-------PKVALLSILS-CDAAkgvlklN 133
Cdd:smart00829  27 GGECAGVVTRVGPGVTGLAVGDRVMGLApgAFATRVVTDARLVVPIPDGWSfeeaatvPVVFLTAYYAlVDLA------R 100

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  134 LRQDEKVLI-TGMGVIGLLACYFLKyYVGVE-HVDVVEPNKnrKDFAKKFG--AKNIYDS 189
Cdd:smart00829 101 LRPGESVLIhAAAGGVGQAAIQLAR-HLGAEvFATAGSPEK--RDFLRALGipDDHIFSS 157
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 24-188 2.56e-05

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: 45.24  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  24 IQDDEIIVKTIAGAISiGAELPQYNGSDVTDTNPFYPRKTGYESYGEVIQVGNKVTHVNVGDKVVSFYGHETIG------ 97
Cdd:cd05289    25 PGPGEVLVKVHAAGVN-PVDLKIREGLLKAAFPLTLPLIPGHDVAGVVVAVGPGVTGFKVGDEVFGMTPFTRGGayaeyv 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  98 IVKGYKVIRVPSSIQPKVA---LLSILScdAAKGVLKL-NLRQDEKVLITGM-GVIGLLACYFLKYYvGVeHVDVVEPNK 172
Cdd:cd05289   104 VVPADELALKPANLSFEEAaalPLAGLT--AWQALFELgGLKAGQTVLIHGAaGGVGSFAVQLAKAR-GA-RVIATASAA 179

                         170
                  ....*....|....*.
gi 1264919701 173 NRkDFAKKFGAKNIYD 188
Cdd:cd05289   180 NA-DFLRSLGADEVID 194
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 69-221 3.60e-05

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: 44.91  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  69 GEVIQVGNKVTHVNVGDKV---VSFYGH----ETIgIVKGYKVIRVPSSIQ-------PKVALLSILSCDAAKGVLKLNL 134
Cdd:cd08248    83 GVVVDIGSGVKSFEIGDEVwgaVPPWSQgthaEYV-VVPENEVSKKPKNLSheeaaslPYAGLTAWSALVNVGGLNPKNA 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 135 RqDEKVLITG-MGVIGLLACYFLKYYVGveHVDVVEPNKNRkDFAKKFGAKNIYD-----SEEKIIET--YNYGFECsaT 206
Cdd:cd08248   162 A-GKRVLILGgSGGVGTFAIQLLKAWGA--HVTTTCSTDAI-PLVKSLGADDVIDynnedFEEELTERgkFDVILDT--V 235

                         170
                  ....*....|....*.
gi 1264919701 207 NSGFHT-LQKALKTNG 221
Cdd:cd08248   236 GGDTEKwALKLLKKGG 251
PRK10754 PRK10754
NADPH:quinone reductase;
57-157 4.45e-05

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 44.34  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  57 PFYPRKTGYESYGEVIQVGNKVTHVNVGDKVVsfYGHETIGI------VKGYKVIRVPSSIQPKVALLSILscdaaKG-- 128
Cdd:PRK10754   55 PSLPSGLGTEAAGVVSKVGSGVKHIKVGDRVV--YAQSALGAyssvhnVPADKAAILPDAISFEQAAASFL-----KGlt 127

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1264919701 129 VLKLnLRQ------DEKVLI-TGMGVIGLLACYFLK 157
Cdd:PRK10754  128 VYYL-LRKtyeikpDEQFLFhAAAGGVGLIACQWAK 162
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 52-152 7.70e-05

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: 43.71  E-value: 7.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  52 VTDTNPFYPRKTGYESYGEVIQVGNKVTHVNVGDKVVSFYGHE--TIGIVKGYKVIRVPSSIQPKVA-------LLSILS 122
Cdd:cd05195    20 ALGLLPGDETPLGLECSGIVTRVGSGVTGLKVGDRVMGLAPGAfaTHVRVDARLVVKIPDSLSFEEAatlpvayLTAYYA 99

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1264919701 123 -CDAAkgvlklNLRQDEKVLIT-GMGVIGLLA 152
Cdd:cd05195   100 lVDLA------RLQKGESVLIHaAAGGVGQAA 125
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
 14-188 9.75e-05

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


Pssm-ID: 176209 [Multi-domain]  Cd Length: 352  Bit Score: 43.41  E-value: 9.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  14 LEWETNEI---KDIQDDEIIVKTIAGAISiGAELPQYNGsdvTDTNPFYPRKT-GYESYGEVIQVGNKV-THVNVGDKVV 88
Cdd:cd08247    13 LTITTIKLplpNCYKDNEIVVKVHAAALN-PVDLKLYNS---YTFHFKVKEKGlGRDYSGVIVKVGSNVaSEWKVGDEVC 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  89 SFYGHetIGIVKG--------------YKVIRVPSSI---QPKVALLSILSCDAAKGVLKLNLRQDEKVLITGMGV-IGL 150
Cdd:cd08247    89 GIYPH--PYGGQGtlsqyllvdpkkdkKSITRKPENIsleEAAAWPLVLGTAYQILEDLGQKLGPDSKVLVLGGSTsVGR 166

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1264919701 151 LACYFLKYYVGVEHVdVVEPNKNRKDFAKKFGAKNIYD 188
Cdd:cd08247   167 FAIQLAKNHYNIGTV-VGTCSSRSAELNKKLGADHFID 203
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 48-143 1.95e-04

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: 42.63  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  48 NGSDVTDTNPFYPRKT------GYESYGEVIQVGNKVTHVNVGDKVV--SFYGHETIGIVKGYKVIRVPsSIQPKVaLLS 119
Cdd:cd08250    43 NASDINFTAGRYDPGVkppfdcGFEGVGEVVAVGEGVTDFKVGDAVAtmSFGAFAEYQVVPARHAVPVP-ELKPEV-LPL 120

                          90       100
                  ....*....|....*....|....*.
gi 1264919701 120 ILSCDAAKGVLK--LNLRQDEKVLIT 143
Cdd:cd08250   121 LVSGLTASIALEevGEMKSGETVLVT 146
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 10-150 3.65e-04

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: 41.48  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  10 GPKQLEWETNEIKDIQDDEIIVKTIAGAISigaelpqynGSDV---------TDTNPFYPrktGYESYGEVIQVGNKVTH 80
Cdd:cd08273    11 GPEVLKVVEADLPEPAAGEVVVKVEASGVS---------FADVqmrrglypdQPPLPFTP---GYDLVGRVDALGSGVTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  81 VNVGDKVVSFYghetigIVKGY---------KVIRVPSSIQPKVALLSILSCDAAKGVLKL--NLRQDEKVLITG-MGVI 148
Cdd:cd08273    79 FEVGDRVAALT------RVGGNaeyinldakYLVPVPEGVDAAEAVCLVLNYVTAYQMLHRaaKVLTGQRVLIHGaSGGV 152


                  ..
gi 1264919701 149 GL 150
Cdd:cd08273   153 GQ 154
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 12-92 5.16e-04

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: 41.27  E-value: 5.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  12 KQLEWETNEIKDIQDDEIIVKTIAGAISigaelpqynGSDVTDTNPFYPRK----TGYESYGEVIQVGNKVTHVNVGDKV 87
Cdd:cd05279    11 KPLSIEEIEVAPPKAGEVRIKVVATGVC---------HTDLHVIDGKLPTPlpviLGHEGAGIVESIGPGVTTLKPGDKV 81


                  ....*
gi 1264919701  88 VSFYG 92
Cdd:cd05279    82 IPLFG 86
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
 61-196 5.70e-04

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 41.17  E-value: 5.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  61 RKTGYESYGEVIQVGNKVTHVNVGDKV--VSFY-----------GHETI-GIVK--GYKV---------------IRVPS 109
Cdd:PRK09422   55 RILGHEGIGIVKEVGPGVTSLKVGDRVsiAWFFegcghceycttGRETLcRSVKnaGYTVdggmaeqcivtadyaVKVPE 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 110 SIQPKVAllSILSCDAA---KGVLKLNLRQDEKVLITGMGVIGLLACYFLKYYVGVeHVDVVEPNKNRKDFAKKFGA--- 183
Cdd:PRK09422  135 GLDPAQA--SSITCAGVttyKAIKVSGIKPGQWIAIYGAGGLGNLALQYAKNVFNA-KVIAVDINDDKLALAKEVGAdlt 211

                         170
                  ....*....|....*.
gi 1264919701 184 ---KNIYDSEEKIIET 196
Cdd:PRK09422  212 insKRVEDVAKIIQEK 227
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 10-191 8.12e-04

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: 40.66  E-value: 8.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  10 GPKQLEWETNEIKDIQDDEIIVKTIAGAISiGAELPQYNGSDVTDTNPfyPRKTGYESYGEVIQVGNKVTHVNVGDKVVS 89
Cdd:cd08268    11 GPEVLRIEELPVPAPGAGEVLIRVEAIGLN-RADAMFRRGAYIEPPPL--PARLGYEAAGVVEAVGAGVTGFAVGDRVSV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  90 FYGH---------ETIgIVKGYKVIRVPSSIQPKVALLSILSCDAAKGVL--KLNLRQDEKVLITGM-GVIGlLACYFLK 157
Cdd:cd08268    88 IPAAdlgqygtyaEYA-LVPAAAVVKLPDGLSFVEAAALWMQYLTAYGALveLAGLRPGDSVLITAAsSSVG-LAAIQIA 165

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1264919701 158 YYVGVeHVDVVEPNKNRKDFAKKFGAKNIYDSEE 191
Cdd:cd08268   166 NAAGA-TVIATTRTSEKRDALLALGAAHVIVTDE 198
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
 24-88 1.13e-03

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: 39.98  E-value: 1.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1264919701  24 IQDDEIIVKTIAGAISiGAELPQYNGsdVTDTNPfyPRKTGYESYGEVIQVGNKVTHVNVGDKVV 88
Cdd:cd08287    23 EEPTDAVIRVVATCVC-GSDLWPYRG--VSPTRA--PAPIGHEFVGVVEEVGSEVTSVKPGDFVI 82
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 64-250 1.18e-03

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: 39.92  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  64 GYESYGEVIQVGNK-------VTHVNVGDKVVSF-----YGH----ETIGIVK--G----YKVIR------VPSSI---- 111
Cdd:cd08242    55 GHEFVGIVEEGPEAelvgkrvVGEINIACGRCEYcrrglYTHcpnrTVLGIVDrdGafaeYLTLPlenlhvVPDLVpdeq 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 112 ----QPKVALLSILScdaakgvlKLNLRQDEKVLITGMGVIGLLACYFLKYYvGVEHVdVVEPNKNRKDFAKKFGAKNIY 187
Cdd:cd08242   135 avfaEPLAAALEILE--------QVPITPGDKVAVLGDGKLGLLIAQVLALT-GPDVV-LVGRHSEKLALARRLGVETVL 204

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1264919701 188 DSEEKIIET-YNYGFECSATNSGFHTLQKALKTNGEICILSDGNIEELTLIANFYQKELQIIGS 250
Cdd:cd08242   205 PDEAESEGGgFDVVVEATGSPSGLELALRLVRPRGTVVLKSTYAGPASFDLTKAVVNEITLVGS 268
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 10-188 1.24e-03

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


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 39.89  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  10 GPKQLEWETNEIK--DIQDDEIIVKTIAGAIsigaelpqyNGSDV----TDTNPFYPRKT----GYESYGEVIQVGNKVT 79
Cdd:cd08267     8 SPEVLLLLEVEVPipTPKPGEVLVKVHAASV---------NPVDWklrrGPPKLLLGRPFppipGMDFAGEVVAVGSGVT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  80 HVNVGDKVVSFYGHETIG------IVKGYKVIRVPSSIQPKVAllsilscdAAKGV----------LKLNLRQDEKVLIT 143
Cdd:cd08267    79 RFKVGDEVFGRLPPKGGGalaeyvVAPESGLAKKPEGVSFEEA--------AALPVagltalqalrDAGKVKPGQRVLIN 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1264919701 144 G-MGVIGLLACYFLKYYVGveHVDVVEPNKNRkDFAKKFGAKNIYD 188
Cdd:cd08267   151 GaSGGVGTFAVQIAKALGA--HVTGVCSTRNA-ELVRSLGADEVID 193
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 12-88 1.48e-03

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: 39.83  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  12 KQLEWETNEIKDIQDDEIIVKTIAGAISigaelpqynGSD---VTDTNPF-YPRKTGYESYGEVIQVGNKVTHVNVGDKV 87
Cdd:cd08279    11 KPLEIEEVELDDPGPGEVLVRIAAAGLC---------HSDlhvVTGDLPApLPAVLGHEGAGVVEEVGPGVTGVKPGDHV 81


                  .
gi 1264919701  88 V 88
Cdd:cd08279    82 V 82
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 57-192 1.68e-03

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: 39.40  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  57 PFYPrktGYESYGEVIQVGNKVTHVNVGDKVVSFYGH----ETIgIVKGYKVIRVPSSIQPKVALLSILSCDAAKGVLKL 132
Cdd:cd08241    58 PFVP---GSEVAGVVEAVGEGVTGFKVGDRVVALTGQggfaEEV-VVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALVR 133

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1264919701 133 --NLRQDEKVLITGM-GVIGLLAcyflkyyvgvehVDVvepnknrkdfAKKFGAKNI--YDSEEK 192
Cdd:cd08241   134 raRLQPGETVLVLGAaGGVGLAA------------VQL----------AKALGARVIaaASSEEK 176
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
 60-91 3.26e-03

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: 38.66  E-value: 3.26e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1264919701  60 PRKTGYESYGEVIQVGNKVTHVNVGDKVvsFY 91
Cdd:cd08252    60 PKILGWDASGVVEAVGSEVTLFKVGDEV--YY 89
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 69-89 4.96e-03

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


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 38.29  E-value: 4.96e-03
                          10        20
                  ....*....|....*....|.
gi 1264919701  69 GEVIQVGNKVTHVNVGDKVVS 89
Cdd:cd08276    67 GEVVAVGEGVTRFKVGDRVVP 87
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 60-249 5.53e-03

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 38.22  E-value: 5.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  60 PRKTGYESYGEVIQVGNKVTHVNVGDKV------------------------VSFYGHETI-GIVKGYKV------IRVP 108
Cdd:PLN02702   74 PMVIGHECAGIIEEVGSEVKHLVVGDRValepgiscwrcnlckegrynlcpeMKFFATPPVhGSLANQVVhpadlcFKLP 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701 109 SSIQ-PKVALLSILSCdAAKGVLKLNLRQDEKVLITGMGVIGLLACYFLKYYvGVEHVDVVEPNKNRKDFAKKFGA---- 183
Cdd:PLN02702  154 ENVSlEEGAMCEPLSV-GVHACRRANIGPETNVLVMGAGPIGLVTMLAARAF-GAPRIVIVDVDDERLSVAKQLGAdeiv 231

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1264919701 184 ---KNIYDSEEKIIETYN-------YGFECSATNSGFHTLQKALKTNGEICILSDGNIEELTLIANFYQKELQIIG 249
Cdd:PLN02702  232 lvsTNIEDVESEVEEIQKamgggidVSFDCVGFNKTMSTALEATRAGGKVCLVGMGHNEMTVPLTPAAAREVDVVG 307
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 11-125 6.69e-03

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


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 37.58  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264919701  11 PKQ-LEWETNEI-KDIQDDEIIVKTIAGAIsigaelpqyNGSD---VTDTNPFYPRKT-------GYESYGEVIQVGNKV 78
Cdd:cd08290    12 PKEvLQLESYEIpPPGPPNEVLVKMLAAPI---------NPADinqIQGVYPIKPPTTpeppavgGNEGVGEVVKVGSGV 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1264919701  79 THVNVGDKVVSFYGH----ETIGIVKGYKVIRVPSSIQP-KVALLSILSCDA 125
Cdd:cd08290    83 KSLKPGDWVIPLRPGlgtwRTHAVVPADDLIKVPNDVDPeQAATLSVNPCTA 134
 
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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