NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|156523966|ref|NP_001095940|]
View 

alcohol dehydrogenase 6 isoform 1 [Homo sapiens]

Protein Classification

MDR/zinc-dependent alcohol dehydrogenase-like family protein; zinc-binding alcohol dehydrogenase family protein( domain architecture ID 10169721)

medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family protein may catalyze the reversible NAD(P)(H)-dependent conversion of an alcohol to its corresponding aldehyde; zinc-binding alcohol dehydrogenase family protein similar to Escherichia coli L-galactonate-5-dehydrogenase that catalyzes the oxidation of L-galactonate to D-tagaturonate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
3-375 0e+00

class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group includes alcohol dehydrogenases corresponding to mammalian classes I, II, IV. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


:

Pssm-ID: 176259 [Multi-domain]  Cd Length: 373  Bit Score: 703.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966   3 TTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKhLDLLYPTILGHEGAGIVESIGEGV 82
Cdd:cd08299    1 TAGKVIKCKAAVLWEPKKPFSIEEIEVAPPKAHEVRIKIVATGICRSDDHVVSGK-LVTPFPVILGHEAAGIVESVGEGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  83 STVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSK-TQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKI 161
Cdd:cd08299   80 TTVKPGDKVIPLFVPQCGKCRACLNPESNLCLKNDLGKpQGLMQDGTSRFTCKGKPIHHFLGTSTFSEYTVVDEIAVAKI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 162 DAVAPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATEC 241
Cdd:cd08299  160 DAAAPLEKVCLIGCGFSTGYGAAVNTAKVTPGSTCAVFGLGGVGLSAIMGCKAAGASRIIAVDINKDKFAKAKELGATEC 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 242 LNPQDLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASVQLKISGQLFFSGRSLKGSVFG 321
Cdd:cd08299  240 INPQDYKKPIQEVLTEMTDGGVDFSFEVIGRLDTMKAALASCHEGYGVSVIVGVPPSSQNLSINPMLLLTGRTWKGAVFG 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156523966 322 GWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCILLL 375
Cdd:cd08299  320 GWKSKDSVPKLVADYMAKKFNLDPLITHTLPFEKINEGFDLLRSGKSIRTVLTF 373
 
Name Accession Description Interval E-value
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
3-375 0e+00

class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group includes alcohol dehydrogenases corresponding to mammalian classes I, II, IV. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176259 [Multi-domain]  Cd Length: 373  Bit Score: 703.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966   3 TTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKhLDLLYPTILGHEGAGIVESIGEGV 82
Cdd:cd08299    1 TAGKVIKCKAAVLWEPKKPFSIEEIEVAPPKAHEVRIKIVATGICRSDDHVVSGK-LVTPFPVILGHEAAGIVESVGEGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  83 STVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSK-TQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKI 161
Cdd:cd08299   80 TTVKPGDKVIPLFVPQCGKCRACLNPESNLCLKNDLGKpQGLMQDGTSRFTCKGKPIHHFLGTSTFSEYTVVDEIAVAKI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 162 DAVAPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATEC 241
Cdd:cd08299  160 DAAAPLEKVCLIGCGFSTGYGAAVNTAKVTPGSTCAVFGLGGVGLSAIMGCKAAGASRIIAVDINKDKFAKAKELGATEC 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 242 LNPQDLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASVQLKISGQLFFSGRSLKGSVFG 321
Cdd:cd08299  240 INPQDYKKPIQEVLTEMTDGGVDFSFEVIGRLDTMKAALASCHEGYGVSVIVGVPPSSQNLSINPMLLLTGRTWKGAVFG 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156523966 322 GWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCILLL 375
Cdd:cd08299  320 GWKSKDSVPKLVADYMAKKFNLDPLITHTLPFEKINEGFDLLRSGKSIRTVLTF 373
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
19-374 2.01e-151

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 431.04  E-value: 2.01e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  19 GAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLgSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQ 98
Cdd:COG1062    1 GGPLEIEEVELDEPRPGEVLVRIVAAGLCHSDLHVR-DGDLPVPLPAVLGHEGAGVVEEVGPGVTGVAPGDHVVLSFIPS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  99 CGECTSCLNSEGNFCIQFKQSKTQ-LMSDGTSRFTCK-GKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLEKVCLISCG 176
Cdd:COG1062   80 CGHCRYCASGRPALCEAGAALNGKgTLPDGTSRLSSAdGEPVGHFFGQSSFAEYAVVPERSVVKVDKDVPLELAALLGCG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 177 FSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDlkKPIQEVLF 256
Cdd:COG1062  160 VQTGAGAVLNTAKVRPGDTVAVFGLGGVGLSAVQGARIAGASRIIAVDPVPEKLELARELGATHTVNPAD--EDAVEAVR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 257 DMTDAGIDFCFEAIGNLDVLAAALASCNeSYGVCVVVGVLPASVQLKIS-GQLFFSGRSLKGSVFGGWKSRQHIPKLVAD 335
Cdd:COG1062  238 ELTGGGVDYAFETTGNPAVIRQALEALR-KGGTVVVVGLAPPGAEISLDpFQLLLTGRTIRGSYFGGAVPRRDIPRLVDL 316
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 156523966 336 YMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCILL 374
Cdd:COG1062  317 YRAGRLPLDELITRRYPLDEINEAFDDLRSGEVIRPVIV 355
PLN02740 PLN02740
Alcohol dehydrogenase-like
1-375 5.19e-146

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 418.43  E-value: 5.19e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966   1 MSTTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVL-GSKHLDLLYPTILGHEGAGIVESIG 79
Cdd:PLN02740   2 SETQGKVITCKAAVAWGPGEPLVMEEIRVDPPQKMEVRIKILYTSICHTDLSAWkGENEAQRAYPRILGHEAAGIVESVG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  80 EGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQS--KTQLMSDGTSRFTCK--GKSIYHFGNTSTFCEYTVIKE 155
Cdd:PLN02740  82 EGVEDLKAGDHVIPIFNGECGDCRYCKRDKTNLCETYRVDpfKSVMVNDGKTRFSTKgdGQPIYHFLNTSTFTEYTVLDS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 156 ISVAKIDAVAPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQE 235
Cdd:PLN02740 162 ACVVKIDPNAPLKKMSLLSCGVSTGVGAAWNTANVQAGSSVAIFGLGAVGLAVAEGARARGASKIIGVDINPEKFEKGKE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 236 LGATECLNPQDLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASVQLKISGQLFFSGRSL 315
Cdd:PLN02740 242 MGITDFINPKDSDKPVHERIREMTGGGVDYSFECAGNVEVLREAFLSTHDGWGLTVLLGIHPTPKMLPLHPMELFDGRSI 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 316 KGSVFGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCILLL 375
Cdd:PLN02740 322 TGSVFGDFKGKSQLPNLAKQCMQGVVNLDGFITHELPFEKINEAFQLLEDGKALRCLLHL 381
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
203-323 2.09e-23

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 94.21  E-value: 2.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  203 GVGLSVVMGCKAAGAaRIIGVDVNKEKFKKAQELGATECLNPQDLKkpIQEVLFDMTDA-GIDFCFEAIGNLDVLAAALA 281
Cdd:pfam00107   1 GVGLAAIQLAKAAGA-KVIAVDGSEEKLELAKELGADHVINPKETD--LVEEIKELTGGkGVDVVFDCVGSPATLEQALK 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 156523966  282 SCNEsYGVCVVVGVLPASVQLKIsGQLFFSGRSLKGSVFGGW 323
Cdd:pfam00107  78 LLRP-GGRVVVVGLPGGPLPLPL-APLLLKELTILGSFLGSP 117
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
39-95 7.60e-06

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 47.00  E-value: 7.60e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966    39 IKVVATGLCGTE-MKVLGskhldlLYP--TILGHEGAGIVESIGEGVSTVKPGDKVITLF 95
Cdd:smart00829   1 IEVRAAGLNFRDvLIALG------LYPgeAVLGGECAGVVTRVGPGVTGLAVGDRVMGLA 54
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
194-229 8.65e-03

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 37.98  E-value: 8.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523966  194 STCAVFGLGGVGLsVVMGCKAAGAARIIGVDVNKEK 229
Cdd:TIGR03026   1 MKIAVIGLGYVGL-PLAALLADLGHDVTGVDIDQEK 35
 
Name Accession Description Interval E-value
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
3-375 0e+00

class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group includes alcohol dehydrogenases corresponding to mammalian classes I, II, IV. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176259 [Multi-domain]  Cd Length: 373  Bit Score: 703.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966   3 TTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKhLDLLYPTILGHEGAGIVESIGEGV 82
Cdd:cd08299    1 TAGKVIKCKAAVLWEPKKPFSIEEIEVAPPKAHEVRIKIVATGICRSDDHVVSGK-LVTPFPVILGHEAAGIVESVGEGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  83 STVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSK-TQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKI 161
Cdd:cd08299   80 TTVKPGDKVIPLFVPQCGKCRACLNPESNLCLKNDLGKpQGLMQDGTSRFTCKGKPIHHFLGTSTFSEYTVVDEIAVAKI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 162 DAVAPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATEC 241
Cdd:cd08299  160 DAAAPLEKVCLIGCGFSTGYGAAVNTAKVTPGSTCAVFGLGGVGLSAIMGCKAAGASRIIAVDINKDKFAKAKELGATEC 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 242 LNPQDLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASVQLKISGQLFFSGRSLKGSVFG 321
Cdd:cd08299  240 INPQDYKKPIQEVLTEMTDGGVDFSFEVIGRLDTMKAALASCHEGYGVSVIVGVPPSSQNLSINPMLLLTGRTWKGAVFG 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156523966 322 GWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCILLL 375
Cdd:cd08299  320 GWKSKDSVPKLVADYMAKKFNLDPLITHTLPFEKINEGFDLLRSGKSIRTVLTF 373
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
8-373 0e+00

class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176260 [Multi-domain]  Cd Length: 368  Bit Score: 531.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966   8 IRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKP 87
Cdd:cd08300    1 ITCKAAVAWEAGKPLSIEEVEVAPPKAGEVRIKILATGVCHTDAYTLSGADPEGLFPVILGHEGAGIVESVGEGVTSVKP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  88 GDKVITLFLPQCGECTSCLNSEGNFC--IQFKQSKTqLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVA 165
Cdd:cd08300   81 GDHVIPLYTPECGECKFCKSGKTNLCqkIRATQGKG-LMPDGTSRFSCKGKPIYHFMGTSTFSEYTVVAEISVAKINPEA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 166 PLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQ 245
Cdd:cd08300  160 PLDKVCLLGCGVTTGYGAVLNTAKVEPGSTVAVFGLGAVGLAVIQGAKAAGASRIIGIDINPDKFELAKKFGATDCVNPK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 246 DLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASVQlkISGQLF--FSGRSLKGSVFGGW 323
Cdd:cd08300  240 DHDKPIQQVLVEMTDGGVDYTFECIGNVKVMRAALEACHKGWGTSVIIGVAAAGQE--ISTRPFqlVTGRVWKGTAFGGW 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 156523966 324 KSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCIL 373
Cdd:cd08300  318 KSRSQVPKLVEDYMKGKIKVDEFITHTMPLDEINEAFDLMHAGKSIRTVV 367
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
8-373 0e+00

Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176238 [Multi-domain]  Cd Length: 365  Bit Score: 529.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966   8 IRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLlYPTILGHEGAGIVESIGEGVSTVKP 87
Cdd:cd08277    1 IKCKAAVAWEAGKPLVIEEIEVAPPKANEVRIKMLATSVCHTDILAIEGFKATL-FPVILGHEGAGIVESVGEGVTNLKP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  88 GDKVITLFLPQCGECTSCLNSEGNFCIQFKQSKTQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPL 167
Cdd:cd08277   80 GDKVIPLFIGQCGECSNCRSGKTNLCQKYRANESGLMPDGTSRFTCKGKKIYHFLGTSTFSQYTVVDENYVAKIDPAAPL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 168 EKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDL 247
Cdd:cd08277  160 EHVCLLGCGFSTGYGAAWNTAKVEPGSTVAVFGLGAVGLSAIMGAKIAGASRIIGVDINEDKFEKAKEFGATDFINPKDS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 248 KKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVlPASVQLKISGQLFFSGRSLKGSVFGGWKSRQ 327
Cdd:cd08277  240 DKPVSEVIREMTGGGVDYSFECTGNADLMNEALESTKLGWGVSVVVGV-PPGAELSIRPFQLILGRTWKGSFFGGFKSRS 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 156523966 328 HIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCIL 373
Cdd:cd08277  319 DVPKLVSKYMNKKFDLDELITHVLPFEEINKGFDLMKSGECIRTVI 364
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
10-373 0e+00

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: 526.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  10 CKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKhLDLLYPTILGHEGAGIVESIGEGVSTVKPGD 89
Cdd:cd05279    1 CKAAVLWEKGKPLSIEEIEVAPPKAGEVRIKVVATGVCHTDLHVIDGK-LPTPLPVILGHEGAGIVESIGPGVTTLKPGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  90 KVITLFLPQCGECTSCLNSEGNFCIQFKQSKTQ-LMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLE 168
Cdd:cd05279   80 KVIPLFGPQCGKCKQCLNPRPNLCSKSRGTNGRgLMSDGTSRFTCKGKPIHHFLGTSTFAEYTVVSEISLAKIDPDAPLE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 169 KVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDLK 248
Cdd:cd05279  160 KVCLIGCGFSTGYGAAVNTAKVTPGSTCAVFGLGGVGLSVIMGCKAAGASRIIAVDINKDKFEKAKQLGATECINPRDQD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 249 KPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASVQLKISGQLFFSGRSLKGSVFGGWKSRQH 328
Cdd:cd05279  240 KPIVEVLTEMTDGGVDYAFEVIGSADTLKQALDATRLGGGTSVVVGVPPSGTEATLDPNDLLTGRTIKGTVFGGWKSKDS 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 156523966 329 IPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCIL 373
Cdd:cd05279  320 VPKLVALYRQKKFPLDELITHVLPFEEINDGFDLMRSGESIRTIL 364
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
8-373 4.85e-171

Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176261 [Multi-domain]  Cd Length: 369  Bit Score: 481.41  E-value: 4.85e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966   8 IRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKP 87
Cdd:cd08301    1 ITCKAAVAWEAGKPLVIEEVEVAPPQAMEVRIKILHTSLCHTDVYFWEAKGQTPLFPRILGHEAAGIVESVGEGVTDLKP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  88 GDKVITLFLPQCGECTSCLNSEGNFC--IQFKQSKTQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVA 165
Cdd:cd08301   81 GDHVLPVFTGECKECRHCKSEKSNMCdlLRINTDRGVMINDGKSRFSINGKPIYHFVGTSTFSEYTVVHVGCVAKINPEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 166 PLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQ 245
Cdd:cd08301  161 PLDKVCLLSCGVSTGLGAAWNVAKVKKGSTVAIFGLGAVGLAVAEGARIRGASRIIGVDLNPSKFEQAKKFGVTEFVNPK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 246 DLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASVQLKISGQLFFSGRSLKGSVFGGWKS 325
Cdd:cd08301  241 DHDKPVQEVIAEMTGGGVDYSFECTGNIDAMISAFECVHDGWGVTVLLGVPHKDAVFSTHPMNLLNGRTLKGTLFGGYKP 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 156523966 326 RQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCIL 373
Cdd:cd08301  321 KTDLPNLVEKYMKKELELEKFITHELPFSEINKAFDLLLKGECLRCIL 368
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
19-374 2.01e-151

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 431.04  E-value: 2.01e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  19 GAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLgSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQ 98
Cdd:COG1062    1 GGPLEIEEVELDEPRPGEVLVRIVAAGLCHSDLHVR-DGDLPVPLPAVLGHEGAGVVEEVGPGVTGVAPGDHVVLSFIPS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  99 CGECTSCLNSEGNFCIQFKQSKTQ-LMSDGTSRFTCK-GKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLEKVCLISCG 176
Cdd:COG1062   80 CGHCRYCASGRPALCEAGAALNGKgTLPDGTSRLSSAdGEPVGHFFGQSSFAEYAVVPERSVVKVDKDVPLELAALLGCG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 177 FSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDlkKPIQEVLF 256
Cdd:COG1062  160 VQTGAGAVLNTAKVRPGDTVAVFGLGGVGLSAVQGARIAGASRIIAVDPVPEKLELARELGATHTVNPAD--EDAVEAVR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 257 DMTDAGIDFCFEAIGNLDVLAAALASCNeSYGVCVVVGVLPASVQLKIS-GQLFFSGRSLKGSVFGGWKSRQHIPKLVAD 335
Cdd:COG1062  238 ELTGGGVDYAFETTGNPAVIRQALEALR-KGGTVVVVGLAPPGAEISLDpFQLLLTGRTIRGSYFGGAVPRRDIPRLVDL 316
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 156523966 336 YMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCILL 374
Cdd:COG1062  317 YRAGRLPLDELITRRYPLDEINEAFDDLRSGEVIRPVIV 355
PLN02740 PLN02740
Alcohol dehydrogenase-like
1-375 5.19e-146

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 418.43  E-value: 5.19e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966   1 MSTTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVL-GSKHLDLLYPTILGHEGAGIVESIG 79
Cdd:PLN02740   2 SETQGKVITCKAAVAWGPGEPLVMEEIRVDPPQKMEVRIKILYTSICHTDLSAWkGENEAQRAYPRILGHEAAGIVESVG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  80 EGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQS--KTQLMSDGTSRFTCK--GKSIYHFGNTSTFCEYTVIKE 155
Cdd:PLN02740  82 EGVEDLKAGDHVIPIFNGECGDCRYCKRDKTNLCETYRVDpfKSVMVNDGKTRFSTKgdGQPIYHFLNTSTFTEYTVLDS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 156 ISVAKIDAVAPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQE 235
Cdd:PLN02740 162 ACVVKIDPNAPLKKMSLLSCGVSTGVGAAWNTANVQAGSSVAIFGLGAVGLAVAEGARARGASKIIGVDINPEKFEKGKE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 236 LGATECLNPQDLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASVQLKISGQLFFSGRSL 315
Cdd:PLN02740 242 MGITDFINPKDSDKPVHERIREMTGGGVDYSFECAGNVEVLREAFLSTHDGWGLTVLLGIHPTPKMLPLHPMELFDGRSI 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 316 KGSVFGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCILLL 375
Cdd:PLN02740 322 TGSVFGDFKGKSQLPNLAKQCMQGVVNLDGFITHELPFEKINEAFQLLEDGKALRCLLHL 381
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
11-374 1.94e-135

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: 390.75  E-value: 1.94e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLgSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDK 90
Cdd:cd08279    2 RAAVLHEVGKPLEIEEVELDDPGPGEVLVRIAAAGLCHSDLHVV-TGDLPAPLPAVLGHEGAGVVEEVGPGVTGVKPGDH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  91 VITLFLPQCGECTSCLNSEGNFCIQFKQSKTQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLEKV 170
Cdd:cd08279   81 VVLSWIPACGTCRYCSRGQPNLCDLGAGILGGQLPDGTRRFTADGEPVGAMCGLGTFAEYTVVPEASVVKIDDDIPLDRA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 171 CLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDlKKP 250
Cdd:cd08279  161 ALLGCGVTTGVGAVVNTARVRPGDTVAVIGCGGVGLNAIQGARIAGASRIIAVDPVPEKLELARRFGATHTVNASE-DDA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 251 IQEVLfDMTDA-GIDFCFEAIGNLDVLAAALASCNESyGVCVVVGVLPASVQLKISGQ-LFFSGRSLKGSVFGGWKSRQH 328
Cdd:cd08279  240 VEAVR-DLTDGrGADYAFEAVGRAATIRQALAMTRKG-GTAVVVGMGPPGETVSLPALeLFLSEKRLQGSLYGSANPRRD 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 156523966 329 IPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCILL 374
Cdd:cd08279  318 IPRLLDLYRAGRLKLDELVTRRYSLDEINEAFADMLAGENARGVIV 363
PLN02827 PLN02827
Alcohol dehydrogenase-like
2-373 5.11e-126

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 367.69  E-value: 5.11e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966   2 STTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLdllYPTILGHEGAGIVESIGEG 81
Cdd:PLN02827   5 ISQPNVITCRAAVAWGAGEALVMEEVEVSPPQPLEIRIKVVSTSLCRSDLSAWESQAL---FPRIFGHEASGIVESIGEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  82 VSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSKTQLM-SDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAK 160
Cdd:PLN02827  82 VTEFEKGDHVLTVFTGECGSCRHCISGKSNMCQVLGLERKGVMhSDQKTRFSIKGKPVYHYCAVSSFSEYTVVHSGCAVK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 161 IDAVAPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATE 240
Cdd:PLN02827 162 VDPLAPLHKICLLSCGVAAGLGAAWNVADVSKGSSVVIFGLGTVGLSVAQGAKLRGASQIIGVDINPEKAEKAKTFGVTD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 241 CLNPQDLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASVQLKISGQLFFSGRSLKGSVF 320
Cdd:PLN02827 242 FINPNDLSEPIQQVIKRMTGGGADYSFECVGDTGIATTALQSCSDGWGLTVTLGVPKAKPEVSAHYGLFLSGRTLKGSLF 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 156523966 321 GGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCIL 373
Cdd:PLN02827 322 GGWKPKSDLPSLVDKYMNKEIMIDEFITHNLSFDEINKAFELMREGKCLRCVI 374
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
8-374 1.55e-104

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: 312.13  E-value: 1.55e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966   8 IRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMkVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKP 87
Cdd:cd08278    1 MKTTAAVVREPGGPFVLEDVELDDPRPDEVLVRIVATGICHTDL-VVRDGGLPTPLPAVLGHEGAGVVEAVGSAVTGLKP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  88 GDKVItLFLPQCGECTSCLNSEGNFCIQFkqskTQL-----MSDGTSRFT-CKGKSIY-HFGNTSTFCEYTVIKEISVAK 160
Cdd:cd08278   80 GDHVV-LSFASCGECANCLSGHPAYCENF----FPLnfsgrRPDGSTPLSlDDGTPVHgHFFGQSSFATYAVVHERNVVK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 161 IDAVAPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATE 240
Cdd:cd08278  155 VDKDVPLELLAPLGCGIQTGAGAVLNVLKPRPGSSIAVFGAGAVGLAAVMAAKIAGCTTIIAVDIVDSRLELAKELGATH 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 241 CLNPQDLKkpIQEVLFDMTDAGIDFCFEAIGNLDVLAAALAsCNESYGVCVVVGVLPASVQLKIS-GQLFFSGRSLKGSV 319
Cdd:cd08278  235 VINPKEED--LVAAIREITGGGVDYALDTTGVPAVIEQAVD-ALAPRGTLALVGAPPPGAEVTLDvNDLLVSGKTIRGVI 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156523966 320 FGGWKSRQHIPKLVADYMAEKLNLDPLIThTLNLDKINEAVELMKTGKCIRCILL 374
Cdd:cd08278  312 EGDSVPQEFIPRLIELYRQGKFPFDKLVT-FYPFEDINQAIADSESGKVIKPVLR 365
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
11-374 7.81e-98

Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group contains members identified as zinc dependent alcohol dehydrogenases (ADH), and class III ADG (aka formaldehyde dehydrogenase, FDH). Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also know as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to the corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176241 [Multi-domain]  Cd Length: 371  Bit Score: 295.44  E-value: 7.81e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGA--------PFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVL-GSKHLDLlyPTILGHEGAGIVESIGEG 81
Cdd:cd08281    2 RAAVLRETGAptpyadsrPLVIEEVELDPPGPGEVLVKIAAAGLCHSDLSVInGDRPRPL--PMALGHEAAGVVVEVGEG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  82 VSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSKTQ-LMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAK 160
Cdd:cd08281   80 VTDLEVGDHVVLVFVPSCGHCRPCAEGRPALCEPGAAANGAgTLLSGGRRLRLRGGEINHHLGVSAFAEYAVVSRRSVVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 161 IDAVAPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATE 240
Cdd:cd08281  160 IDKDVPLEIAALFGCAVLTGVGAVVNTAGVRPGQSVAVVGLGGVGLSALLGAVAAGASQVVAVDLNEDKLALARELGATA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 241 CLNPQDlkKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALaSCNESYGVCVVVGVLPASVQLKISG-QLFFSGRSLKGSV 319
Cdd:cd08281  240 TVNAGD--PNAVEQVRELTGGGVDYAFEMAGSVPALETAY-EITRRGGTTVTAGLPDPEARLSVPAlSLVAEERTLKGSY 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156523966 320 FGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCILL 374
Cdd:cd08281  317 MGSCVPRRDIPRYLALYLSGRLPVDKLLTHRLPLDEINEGFDRLAAGEAVRQVIL 371
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
11-374 3.24e-78

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


Pssm-ID: 176224 [Multi-domain]  Cd Length: 367  Bit Score: 244.97  E-value: 3.24e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKhLDLLYPTILGHEGAGIVESIGEGV---STVKP 87
Cdd:cd08263    2 KAAVLKGPNPPLTIEEIPVPRPKEGEILIRVAACGVCHSDLHVLKGE-LPFPPPFVLGHEISGEVVEVGPNVenpYGLSV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  88 GDKVITLFLPQCGECTSCLNSEGNFCIQF---KQSKTQLMsDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAV 164
Cdd:cd08263   81 GDRVVGSFIMPCGKCRYCARGKENLCEDFfayNRLKGTLY-DGTTRLFRLDGGPVYMYSMGGLAEYAVVPATALAPLPES 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 165 APLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNP 244
Cdd:cd08263  160 LDYTESAVLGCAGFTAYGALKHAADVRPGETVAVIGVGGVGSSAIQLAKAFGASPIIAVDVRDEKLAKAKELGATHTVNA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 245 --QDLKKPIQEVLFDMtdaGIDFCFEAIGNLDVLAAALASCNESyGVCVVVGVLPASVQLKISGQLFFS-GRSLKGSvFG 321
Cdd:cd08263  240 akEDAVAAIREITGGR---GVDVVVEALGKPETFKLALDVVRDG-GRAVVVGLAPGGATAEIPITRLVRrGIKIIGS-YG 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 156523966 322 GwKSRQHIPKLVAdyMAE--KLNLDPLITHTLNLDKINEAVELMKTGKC-IRCILL 374
Cdd:cd08263  315 A-RPRQDLPELVG--LAAsgKLDPEALVTHKYKLEEINEAYENLRKGLIhGRAIVE 367
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
11-367 1.41e-72

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: 229.64  E-value: 1.41e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGaPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDK 90
Cdd:COG1063    2 KALVLHGPG-DLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  91 VITLFLPQCGECTSCLNSEGNFCiqfkqSKTQLMsdGTSRftckgksiYHFGntstFCEYTVIKEISVAKIDAVAPLEKV 170
Cdd:COG1063   81 VVVEPNIPCGECRYCRRGRYNLC-----ENLQFL--GIAG--------RDGG----FAEYVRVPAANLVKVPDGLSDEAA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 171 CLI---SCGFstgfgAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDl 247
Cdd:COG1063  142 ALVeplAVAL-----HAVERAGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARELGADAVVNPRE- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 248 kKPIQEVLFDMTD-AGIDFCFEAIGNLDVLAAALASCNeSYGVCVVVGVLPASVQLKIsGQLFFSGRSLKGSVFGGwksR 326
Cdd:COG1063  216 -EDLVEAVRELTGgRGADVVIEAVGAPAALEQALDLVR-PGGTVVLVGVPGGPVPIDL-NALVRKELTLRGSRNYT---R 289
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 156523966 327 QHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGK 367
Cdd:COG1063  290 EDFPEALELLASGRIDLEPLITHRFPLDDAPEAFEAAADRA 330
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
36-333 5.65e-70

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: 220.66  E-value: 5.65e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  36 EVRIKVVATGLCGTEMKVL-GSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQCGECTSCLNsegnfci 114
Cdd:cd05188    1 EVLVRVEAAGLCGTDLHIRrGGYPPPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNLGCGTCELCRE------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 115 qfkqsktqlmsdgtsrfTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLEKVCLISCGFSTGFGAAINTAKVTPGS 194
Cdd:cd05188   74 -----------------LCPGGGILGEGLDGGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVLKPGD 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 195 TCAVFGLGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGATECLNPQDlkKPIQEVLFDMTDAGIDFCFEAIGNLD 274
Cdd:cd05188  137 TVLVLGAGGVGLLAAQLAKAAG-ARVIVTDRSDEKLELAKELGADHVIDYKE--EDLEEELRLTGGGGADVVIDAVGGPE 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 156523966 275 VLAAALASCNeSYGVCVVVGVLPASVQLKISGQLFFSGRSLKGSVFGGWKSRQHIPKLV 333
Cdd:cd05188  214 TLAQALRLLR-PGGRIVVVGGTSGGPPLDDLRRLLFKELTIIGSTGGTREDFEEALDLL 271
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
11-367 7.02e-69

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 219.60  E-value: 7.02e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDK 90
Cdd:COG1064    2 KAAVLTEPGGPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGVTGFKVGDR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  91 VITLFLPQCGECTSCLNSEGNFCIQFKQsktqlmsDGtsrftckgksIYHFGntsTFCEYTVIKEISVAKIDAVAPLEKV 170
Cdd:COG1064   82 VGVGWVDSCGTCEYCRSGRENLCENGRF-------TG----------YTTDG---GYAEYVVVPARFLVKLPDGLDPAEA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 171 CLISCGFSTGFgAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGATECLNPQDlKKP 250
Cdd:COG1064  142 APLLCAGITAY-RALRRAGVGPGDRVAVIGAGGLGHLAVQIAKALG-AEVIAVDRSPEKLELARELGADHVVNSSD-EDP 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 251 IQEVlfdMTDAGIDFCFEAIGNLDVLAAALASCNeSYGVCVVVGVLPASVQLKIsGQLFFSGRSLKGSVFGGwksRQHIP 330
Cdd:COG1064  219 VEAV---RELTGADVVIDTVGAPATVNAALALLR-RGGRLVLVGLPGGPIPLPP-FDLILKERSIRGSLIGT---RADLQ 290
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 156523966 331 KLVAdyMAEKLNLDPlITHTLNLDKINEAVELMKTGK 367
Cdd:COG1064  291 EMLD--LAAEGKIKP-EVETIPLEEANEALERLRAGK 324
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
11-367 2.40e-53

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: 179.73  E-value: 2.40e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGApFSIEEVEVAPPKAKEVRIKVVATGLCGTE---MKVLGSKHldllYPTILGHEGAGIVESIGEGVSTVKP 87
Cdd:cd08236    2 KALVLTGPGD-LRYEDIPKPEPGPGEVLVKVKACGICGSDiprYLGTGAYH----PPLVLGHEFSGTVEEVGSGVDDLAV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  88 GDKV-ITLFLPqCGECTSCLNSEGNFCiqfkqskTQLMSDGTSRFTCkgksiyhfgntstFCEYTVIKEISVAKIDAVAP 166
Cdd:cd08236   77 GDRVaVNPLLP-CGKCEYCKKGEYSLC-------SNYDYIGSRRDGA-------------FAEYVSVPARNLIKIPDHVD 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 167 LEKVCLI---SCGFStgfgaAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLN 243
Cdd:cd08236  136 YEEAAMIepaAVALH-----AVRLAGITLGDTVVVIGAGTIGLLAIQWLKILGAKRVIAVDIDDEKLAVARELGADDTIN 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 244 PqdlKKPIQEVLFDMTDA-GIDFCFEAIGNLDVLAAALASCNeSYGVCVVVGVLPASVQL--KISGQLFFSGRSLKGS-- 318
Cdd:cd08236  211 P---KEEDVEKVRELTEGrGADLVIEAAGSPATIEQALALAR-PGGKVVLVGIPYGDVTLseEAFEKILRKELTIQGSwn 286
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 156523966 319 ----VFGG--WKSrqhipklVADYMAE-KLNLDPLITHTLNLDKINEAVELMKTGK 367
Cdd:cd08236  287 sysaPFPGdeWRT-------ALDLLASgKIKVEPLITHRLPLEDGPAAFERLADRE 335
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
11-367 1.49e-49

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: 169.73  E-value: 1.49e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAP-FSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVL-GSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPG 88
Cdd:cd08254    2 KAWRFHKGSKGlLVLEEVPVPEPGPGEVLVKVKAAGVCHSDLHILdGGVPTLTKLPLTLGHEIAGTVVEVGAGVTNFKVG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  89 DKVITLFLPQCGECTSCLNSEGNFCIqfKQSKTQLMSDGtsrftckgksiyhfgntsTFCEYTVIKEISVAKIDAVAPLE 168
Cdd:cd08254   82 DRVAVPAVIPCGACALCRRGRGNLCL--NQGMPGLGIDG------------------GFAEYIVVPARALVPVPDGVPFA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 169 KVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAArIIGVDVNKEKFKKAQELGATECLNPQDlK 248
Cdd:cd08254  142 QAAVATDAVLTPYHAVVRAGEVKPGETVLVIGLGGLGLNAVQIAKAMGAA-VIAVDIKEEKLELAKELGADEVLNSLD-D 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 249 KPIQEVLFDmTDAGIDFCFEAIGNLDVLAAALaSCNESYGVCVVVGVLPASVQLKISgQLFFSGRSLKGSvFGGwkSRQH 328
Cdd:cd08254  220 SPKDKKAAG-LGGGFDVIFDFVGTQPTFEDAQ-KAVKPGGRIVVVGLGRDKLTVDLS-DLIARELRIIGS-FGG--TPED 293
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 156523966 329 IPKlVADYMAEKLnLDPLItHTLNLDKINEAVELMKTGK 367
Cdd:cd08254  294 LPE-VLDLIAKGK-LDPQV-ETRPLDEIPEVLERLHKGK 329
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
11-373 3.14e-48

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: 166.21  E-value: 3.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGApFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDK 90
Cdd:cd08261    2 KALVCEKPGR-LEVVDIPEPVPGAGEVLVRVKRVGICGSDLHIYHGRNPFASYPRILGHELSGEVVEVGEGVAGLKVGDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  91 VItlFLP--QCGECTSCLNSEGNFCiqfkqSKTQLM---SDGTsrftckgksiyhfgntstFCEYTVIKEISVAKIDAVa 165
Cdd:cd08261   81 VV--VDPyiSCGECYACRKGRPNCC-----ENLQVLgvhRDGG------------------FAEYIVVPADALLVPEGL- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 166 PLEKVCLISCgFSTGFgAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGATECLNPQ 245
Cdd:cd08261  135 SLDQAALVEP-LAIGA-HAVRRAGVTAGDTVLVVGAGPIGLGVIQVAKARG-ARVIVVDIDDERLEFARELGADDTINVG 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 246 DlkKPIQEVLFDMTDA-GIDFCFEAIGNLDVLAAAL---ASCnesyGVCVVVGVLPASVQLKisgQLFFSGRSLkgSVFG 321
Cdd:cd08261  212 D--EDVAARLRELTDGeGADVVIDATGNPASMEEAVelvAHG----GRVVLVGLSKGPVTFP---DPEFHKKEL--TILG 280
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 156523966 322 gwkSR----QHIPKlVADYMAE-KLNLDPLITHTLNLDKINEAVELMKT--GKCIRCIL 373
Cdd:cd08261  281 ---SRnatrEDFPD-VIDLLESgKVDPEALITHRFPFEDVPEAFDLWEAppGGVIKVLI 335
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
11-374 6.82e-48

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: 165.46  E-value: 6.82e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGApFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDK 90
Cdd:cd08235    2 KAAVLHGPND-VRLEEVPVPEPGPGEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGDGVTGFKVGDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  91 VITL-FLPqCGECTSCLNSEGNFCIQFKQsktqlmsdgtsrftckgksiyhFGNTST--FCEYTVIKEISVA-----KID 162
Cdd:cd08235   81 VFVApHVP-CGECHYCLRGNENMCPNYKK----------------------FGNLYDggFAEYVRVPAWAVKrggvlKLP 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 163 AVAPLEKVCLI---SCGFstgfgAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGAT 239
Cdd:cd08235  138 DNVSFEEAALVeplACCI-----NAQRKAGIKPGDTVLVIGAGPIGLLHAMLAKASGARKVIVSDLNEFRLEFAKKLGAD 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 240 ECLNPqdLKKPIQEVLFDMTD-AGIDFCFEAIGNLDVLAAALaSCNESYGVCVVVGVLPASVQLKI-SGQLFFSGRSLKG 317
Cdd:cd08235  213 YTIDA--AEEDLVEKVRELTDgRGADVVIVATGSPEAQAQAL-ELVRKGGRILFFGGLPKGSTVNIdPNLIHYREITITG 289
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 156523966 318 SvFGGwkSRQHIpKLVADYMAE-KLNLDPLITHTLNLDKINEAVELMKTGKCIRCILL 374
Cdd:cd08235  290 S-YAA--SPEDY-KEALELIASgKIDVKDLITHRFPLEDIEEAFELAADGKSLKIVIT 343
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
11-363 3.58e-47

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 163.54  E-value: 3.58e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDK 90
Cdd:cd08260    2 RAAVYEEFGEPLEIREVPDPEPPPDGVVVEVEACGVCRSDWHGWQGHDPDVTLPHVPGHEFAGVVVEVGEDVSRWRVGDR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  91 VITLFLPQCGECTSCLNSEGNfciqfkqsktqlmsdgtsrfTCKGKSIYHFGNTSTFCEYTVIKEisvAKIDAVA----- 165
Cdd:cd08260   82 VTVPFVLGCGTCPYCRAGDSN--------------------VCEHQVQPGFTHPGSFAEYVAVPR---ADVNLVRlpddv 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 166 PLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGATECLNPQ 245
Cdd:cd08260  139 DFVTAAGLGCRFATAFRALVHQARVKPGEWVAVHGCGGVGLSAVMIASALG-ARVIAVDIDDDKLELARELGAVATVNAS 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 246 DLKKPIQEVLfDMTDAGIDFCFEAIGNLDVLAAALASCnESYGVCVVVGVL---PASVQLK----ISGQLFFSGrslkgs 318
Cdd:cd08260  218 EVEDVAAAVR-DLTGGGAHVSVDALGIPETCRNSVASL-RKRGRHVQVGLTlgeEAGVALPmdrvVARELEIVG------ 289
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 156523966 319 VFGGWKSR-QHIPKLVAdymAEKLNLDPLITHTLNLDKINEAVELM 363
Cdd:cd08260  290 SHGMPAHRyDAMLALIA---SGKLDPEPLVGRTISLDEAPDALAAM 332
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
11-358 1.50e-46

(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: 162.32  E-value: 1.50e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGaPFSIEEVEVAPPKAKEVRIKVVATGLCGTE----------MKVLGSKHL-DLLYPTILGHEGAGIVESIG 79
Cdd:cd08233    2 KAARYHGRK-DIRVEEVPEPPVKPGEVKIKVAWCGICGSDlheyldgpifIPTEGHPHLtGETAPVTLGHEFSGVVVEVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  80 EGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCiqfkqskTQLMSDGTSrftckgksiyhfGNTSTFCEYTVIKEISVA 159
Cdd:cd08233   81 SGVTGFKVGDRVVVEPTIKCGTCGACKRGLYNLC-------DSLGFIGLG------------GGGGGFAEYVVVPAYHVH 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 160 KIDAVAPLEKVCLI---SCGFStgfgaAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQEL 236
Cdd:cd08233  142 KLPDNVPLEEAALVeplAVAWH-----AVRRSGFKPGDTALVLGAGPIGLLTILALKAAGASKIIVSEPSEARRELAEEL 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 237 GATECLNPqdLKKPIQEVLFDMTD-AGIDFCFEAIGNLDVLAAALASCnESYGVCVVVGVLPASVQLKISgQLFFSGRSL 315
Cdd:cd08233  217 GATIVLDP--TEVDVVAEVRKLTGgGGVDVSFDCAGVQATLDTAIDAL-RPRGTAVNVAIWEKPISFNPN-DLVLKEKTL 292
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 156523966 316 KGSvfggWKSRQHIPKLVADYMAE-KLNLDPLITHTLNLDKINE 358
Cdd:cd08233  293 TGS----ICYTREDFEEVIDLLASgKIDAEPLITSRIPLEDIVE 332
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
11-374 1.78e-45

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: 159.02  E-value: 1.78e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDK 90
Cdd:cd08259    2 KAAILHKPNKPLQIEEVPDPEPGPGEVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVGEGVERFKPGDR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  91 VITLFLPQCGECTSCLNSEGNFciqfkqsktqlmsdgtsrftCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLEKV 170
Cdd:cd08259   82 VILYYYIPCGKCEYCLSGEENL--------------------CRNRAEYGEEVDGGFAEYVKVPERSLVKLPDNVSDESA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 171 CLISCGFSTGFGAAiNTAKVTPGST-CAVFGLGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGATECLNPQDLKK 249
Cdd:cd08259  142 ALAACVVGTAVHAL-KRAGVKKGDTvLVTGAGGGVGIHAIQLAKALG-ARVIAVTRSPEKLKILKELGADYVIDGSKFSE 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 250 PIQEVLfdmtdaGIDFCFEAIGNlDVLAAALASCNESyGVCVVVG-VLPASVQLKIsGQLFFSGRSLKGSVFGGWKSRQH 328
Cdd:cd08259  220 DVKKLG------GADVVIELVGS-PTIEESLRSLNKG-GRLVLIGnVTPDPAPLRP-GLLILKEIRIIGSISATKADVEE 290
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 156523966 329 IPKLVADYMAEklnldPLITHTLNLDKINEAVELMKTGKCIRCILL 374
Cdd:cd08259  291 ALKLVKEGKIK-----PVIDRVVSLEDINEALEDLKSGKVVGRIVL 331
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
11-370 9.38e-45

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: 156.92  E-value: 9.38e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGApFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVL----GSKhldllYPTILGHEGAGIVESIGEGVSTVK 86
Cdd:cd08234    2 KALVYEGPGE-LEVEEVPVPEPGPDEVLIKVAACGICGTDLHIYegefGAA-----PPLVPGHEFAGVVVAVGSKVTGFK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  87 PGDKV-----ITlflpqCGECTSCLNSEGNFCiqfkqsktqlmsdgtsrftckgKSIYHFGNTST--FCEYTVIKEISVA 159
Cdd:cd08234   76 VGDRVavdpnIY-----CGECFYCRRGRPNLC----------------------ENLTAVGVTRNggFAEYVVVPAKQVY 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 160 KI-DAVAPLEKVCL--ISCgfstgfgAA--INTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQ 234
Cdd:cd08234  129 KIpDNLSFEEAALAepLSC-------AVhgLDLLGIKPGDSVLVFGAGPIGLLLAQLLKLNGASRVTVAEPNEEKLELAK 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 235 ELGATECLNPQDLKKPIQEvlfDMTDAGIDFCFEAIGNLDVLAAALASCNESyGVCVVVGVLPASVQLKISGQLFFsGRS 314
Cdd:cd08234  202 KLGATETVDPSREDPEAQK---EDNPYGFDVVIEATGVPKTLEQAIEYARRG-GTVLVFGVYAPDARVSISPFEIF-QKE 276
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 156523966 315 LKgsVFGGWKSRQHIPKlVADYMAE-KLNLDPLITHTLNLDKINEAVELMKTGKCIR 370
Cdd:cd08234  277 LT--IIGSFINPYTFPR-AIALLESgKIDVKGLVSHRLPLEEVPEALEGMRSGGALK 330
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
23-375 1.24e-44

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: 156.71  E-value: 1.24e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  23 SIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTIL-GHEGAGIVESIGEGVSTVKPGDKVITLFLPQCGE 101
Cdd:cd08239   13 ELREFPVPVPGPGEVLLRVKASGLCGSDLHYYYHGHRAPAYQGVIpGHEPAGVVVAVGPGVTHFRVGDRVMVYHYVGCGA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 102 CTSCLNSEGNFCiqfkqsKTQLMSDGTSRftckgksiyHFGNTstfcEYTVIKEISVAKIDAVAPLEKVCLISCGFSTGf 181
Cdd:cd08239   93 CRNCRRGWMQLC------TSKRAAYGWNR---------DGGHA----EYMLVPEKTLIPLPDDLSFADGALLLCGIGTA- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 182 GAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDLKkpIQEVLFDMTDA 261
Cdd:cd08239  153 YHALRRVGVSGRDTVLVVGAGPVGLGALMLARALGAEDVIGVDPSPERLELAKALGADFVINSGQDD--VQEIRELTSGA 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 262 GIDFCFEAIGNLDVLAAALASCNEsYGVCVVVGVlPASVQLKISGQLFFSGRSLKGS-VFGGWKSRQhIPKLVADYmaeK 340
Cdd:cd08239  231 GADVAIECSGNTAARRLALEAVRP-WGRLVLVGE-GGELTIEVSNDLIRKQRTLIGSwYFSVPDMEE-CAEFLARH---K 304
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 156523966 341 LNLDPLITHTLNLDKINEAVELMKTGKCIRCILLL 375
Cdd:cd08239  305 LEVDRLVTHRFGLDQAPEAYALFAQGESGKVVFVF 339
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
10-373 4.72e-44

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 155.88  E-value: 4.72e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  10 CKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVST----- 84
Cdd:cd08231    1 ARAAVLTGPGKPLEIREVPLPDLEPGAVLVRVRLAGVCGSDVHTVAGRRPRVPLPIILGHEGVGRVVALGGGVTTdvage 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  85 -VKPGDKVITLFLPQCGECTSCLNSEGNFCiqfkQSKTQLmsdGTSRFTCKGksiyhfGNTSTFCEYTVIK-EISVAKID 162
Cdd:cd08231   81 pLKVGDRVTWSVGAPCGRCYRCLVGDPTKC----ENRKKY---GHEASCDDP------HLSGGYAEHIYLPpGTAIVRVP 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 163 AVAPLEKVCLISCGFSTGFgAAINTA-KVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATEC 241
Cdd:cd08231  148 DNVPDEVAAPANCALATVL-AALDRAgPVGAGDTVVVQGAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAREFGADAT 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 242 LNPQDLKKP-IQEVLFDMTDA-GIDFCFEAIGNLDVLAAALASCNESyGVCVVVGVLPASVQLKISGQLF-FSGRSLKGS 318
Cdd:cd08231  227 IDIDELPDPqRRAIVRDITGGrGADVVIEASGHPAAVPEGLELLRRG-GTYVLVGSVAPAGTVPLDPERIvRKNLTIIGV 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156523966 319 VFGGWKSRQHIPKLVADYmAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCIL 373
Cdd:cd08231  306 HNYDPSHLYRAVRFLERT-QDRFPFAELVTHRYPLEDINEALELAESGTALKVVI 359
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
24-373 1.17e-43

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: 154.35  E-value: 1.17e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  24 IEEVEVAPPKAKEVR---IKVVATGLCGTEM-----KVLGSKHldllyPTILGHEGAGIVESIGEGVSTVKPGDKVITLF 95
Cdd:cd05278   12 IGLEEVPDPKIQGPHdaiVRVTATSICGSDLhiyrgGVPGAKH-----GMILGHEFVGEVVEVGSDVKRLKPGDRVSVPC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  96 LPQCGECTSCLNSEGNFCIqfkqsktqlmsdgtsrftcKGKSIYHFGN--TSTFCEYTVIKE--ISVAKIDAVAPLEKVC 171
Cdd:cd05278   87 ITFCGRCRFCRRGYHAHCE-------------------NGLWGWKLGNriDGGQAEYVRVPYadMNLAKIPDGLPDEDAL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 172 LISCGFSTGFGAAINtAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDlKKPI 251
Cdd:cd05278  148 MLSDILPTGFHGAEL-AGIKPGSTVAVIGAGPVGLCAVAGARLLGAARIIAVDSNPERLDLAKEAGATDIINPKN-GDIV 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 252 QEVLFDMTDAGIDFCFEAIGNLDVLAAALAsCNESYGVCVVVGVLPASVQLKISGQLFFSGRSLKGsvfGGWKSRQHIPK 331
Cdd:cd05278  226 EQILELTGGRGVDCVIEAVGFEETFEQAVK-VVRPGGTIANVGVYGKPDPLPLLGEWFGKNLTFKT---GLVPVRARMPE 301
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 156523966 332 LVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGK--CIRCIL 373
Cdd:cd05278  302 LLDLIEEGKIDPSKLITHRFPLDDILKAYRLFDNKPdgCIKVVI 345
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
12-367 7.19e-43

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: 152.26  E-value: 7.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  12 AAILWKPGApFSIEEVEVAPPKAKEVRIKVVATGLCGTemkvlgskhlDLLY-------------PTILGHEGAGIVESI 78
Cdd:cd05285    1 AAVLHGPGD-LRLEERPIPEPGPGEVLVRVRAVGICGS----------DVHYykhgrigdfvvkePMVLGHESAGTVVAV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  79 GEGVSTVKPGDKV-ITLFLPqCGECTSCLNSEGNFC--IQFkqsktqlMS----DGTsrftckgksiyhfgntstFCEYT 151
Cdd:cd05285   70 GSGVTHLKVGDRVaIEPGVP-CRTCEFCKSGRYNLCpdMRF-------AAtppvDGT------------------LCRYV 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 152 VIKEISVAKI-DAV-----APLE--KVCLiscgfstgfgAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGV 223
Cdd:cd05285  124 NHPADFCHKLpDNVsleegALVEplSVGV----------HACRRAGVRPGDTVLVFGAGPIGLLTAAVAKAFGATKVVVT 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 224 DVNKEKFKKAQELGATECLNP--QDLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESyGVCVVVGVLPASVQ 301
Cdd:cd05285  194 DIDPSRLEFAKELGATHTVNVrtEDTPESAEKIAELLGGKGPDVVIECTGAESCIQTAIYATRPG-GTVVLVGMGKPEVT 272
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156523966 302 LKISgqlFFSGR--SLKGsVF---GGWKsrqHIPKLVAdymAEKLNLDPLITHTLNLDKINEAVELMKTGK 367
Cdd:cd05285  273 LPLS---AASLReiDIRG-VFryaNTYP---TAIELLA---SGKVDVKPLITHRFPLEDAVEAFETAAKGK 333
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
11-373 1.65e-42

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: 151.23  E-value: 1.65e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMkvlgskHLD---------LLYPTILGHEGAGIVESIGEG 81
Cdd:cd05281    2 KAIVKTKAGPGAELVEVPVPKPGPGEVLIKVLAASICGTDV------HIYewdewaqsrIKPPLIFGHEFAGEVVEVGEG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  82 VSTVKPGDKVITLFLPQCGECTSCLNSEGNFCiqfkqSKTQLMsdGTSRFTCkgksiyhfgntstFCEYTVIKEISVAKI 161
Cdd:cd05281   76 VTRVKVGDYVSAETHIVCGKCYQCRTGNYHVC-----QNTKIL--GVDTDGC-------------FAEYVVVPEENLWKN 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 162 DAVAPLEKVCLIScgfstGFGAAINTAKVTP--GSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGAT 239
Cdd:cd05281  136 DKDIPPEIASIQE-----PLGNAVHTVLAGDvsGKSVLITGCGPIGLMAIAVAKAAGASLVIASDPNPYRLELAKKMGAD 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 240 ECLNPqdLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESyGVCVVVGVLPASVQLKISGQLFFSGRSLKG-- 317
Cdd:cd05281  211 VVINP--REEDVVEVKSVTDGTGVDVVLEMSGNPKAIEQGLKALTPG-GRVSILGLPPGPVDIDLNNLVIFKGLTVQGit 287
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 156523966 318 --SVFGGWKSRQHIPKlvadymAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCIL 373
Cdd:cd05281  288 grKMFETWYQVSALLK------SGKVDLSPVITHKLPLEDFEEAFELMRSGKCGKVVL 339
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
11-365 2.08e-38

NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol dehydrogenases; they exist as tetramers and exhibit specificity for NADP(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like other zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric ADHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains; however, they do not have and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 140.45  E-value: 2.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGApFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDK 90
Cdd:cd08285    2 KAFAMLGIGK-VGWIEKPIPVCGPNDAIVRPTAVAPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGSEVKDFKPGDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  91 VITLFLPQCGECTSCLNSEgnfciqfkQSKTQLMSDGtsrftckgksiYHFGNT--STFCEYTVIKE--ISVAKIDAVAP 166
Cdd:cd08285   81 VIVPAITPDWRSVAAQRGY--------PSQSGGMLGG-----------WKFSNFkdGVFAEYFHVNDadANLAPLPDGLT 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 167 LEKVCLISCGFSTGFGAAINtAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQD 246
Cdd:cd08285  142 DEQAVMLPDMMSTGFHGAEL-ANIKLGDTVAVFGIGPVGLMAVAGARLRGAGRIIAVGSRPNRVELAKEYGATDIVDYKN 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 247 lKKPIQEVLfDMTD-AGIDFCFEAIGNLDVLAAALAsCNESYGVCVVVGVLPASVQLKISGQLFFSG---RSLKGSVFGG 322
Cdd:cd08285  221 -GDVVEQIL-KLTGgKGVDAVIIAGGGQDTFEQALK-VLKPGGTISNVNYYGEDDYLPIPREEWGVGmghKTINGGLCPG 297
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 156523966 323 WKSRqhIPKLVADYMAEKLNLDPLITH-TLNLDKINEAVELMKT 365
Cdd:cd08285  298 GRLR--MERLASLIEYGRVDPSKLLTHhFFGFDDIEEALMLMKD 339
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
10-367 3.44e-38

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 139.59  E-value: 3.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  10 CKAAILWKPG-APFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKV-LGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKP 87
Cdd:cd08297    1 MKAAVVEEFGeKPYEVKDVPVPEPGPGEVLVKLEASGVCHTDLHAaLGDWPVKPKLPLIGGHEGAGVVVAVGPGVSGLKV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  88 GDKV-ITLFLPQCGECTSCLNSEGNFCIqfKQSKTQLMSDGtsrftckgksiyhfgntsTFCEYTVIKEISVAKI----- 161
Cdd:cd08297   81 GDRVgVKWLYDACGKCEYCRTGDETLCP--NQKNSGYTVDG------------------TFAEYAIADARYVTPIpdgls 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 162 -DAVAPlekvclISCGFSTGFGaAINTAKVTPGSTCAVFGLGG-VGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGAT 239
Cdd:cd08297  141 fEQAAP------LLCAGVTVYK-ALKKAGLKPGDWVVISGAGGgLGHLGVQYAKAMG-LRVIAIDVGDEKLELAKELGAD 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 240 ECLNPQDlKKPIQEVLFDMTDAGIDfcfEAIgnldVLAAALASCNESY------GVCVVVGvLPASVQLKIS-GQLFFSG 312
Cdd:cd08297  213 AFVDFKK-SDDVEAVKELTGGGGAH---AVV----VTAVSAAAYEQALdylrpgGTLVCVG-LPPGGFIPLDpFDLVLRG 283
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156523966 313 RSLKGSVFGgwkSRQHIPKLVaDYMAEKLnLDPLIThTLNLDKINEAVELMKTGK 367
Cdd:cd08297  284 ITIVGSLVG---TRQDLQEAL-EFAARGK-VKPHIQ-VVPLEDLNEVFEKMEEGK 332
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
13-373 1.92e-37

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: 137.77  E-value: 1.92e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  13 AILWKPgaPFSIEEVEVAPPK---AKEVRIKVVATGLCGTEMKVL-GskHLDLLYPTILGHEGAGIVESIGEGVSTVKPG 88
Cdd:cd08284    3 AVVFKG--PGDVRVEEVPIPQiqdPTDAIVKVTAAAICGSDLHIYrG--HIPSTPGFVLGHEFVGEVVEVGPEVRTLKVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  89 DKVITLFLPQCGECTSCLNSEGNFCiqfkqSKTQLmsdgtsrFTCKGKSIYHFGNTstfcEYTVI--KEISVAKIDAVAP 166
Cdd:cd08284   79 DRVVSPFTIACGECFYCRRGQSGRC-----AKGGL-------FGYAGSPNLDGAQA----EYVRVpfADGTLLKLPDGLS 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 167 LEKVCLISCGFSTGFGAAINtAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGAtECLNPQD 246
Cdd:cd08284  143 DEAALLLGDILPTGYFGAKR-AQVRPGDTVAVIGCGPVGLCAVLSAQVLGAARVFAVDPVPERLERAAALGA-EPINFED 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 247 LkKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCnESYGVCVVVGVlPASVQLKISGQLFFSgRSLKGSvFGGWKSR 326
Cdd:cd08284  221 A-EPVERVREATEGRGADVVLEAVGGAAALDLAFDLV-RPGGVISSVGV-HTAEEFPFPGLDAYN-KNLTLR-FGRCPVR 295
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 156523966 327 QHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCIL 373
Cdd:cd08284  296 SLFPELLPLLESGRLDLEFLIDHRMPLEEAPEAYRLFDKRKVLKVVL 342
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
11-367 3.87e-37

D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related alcohol dehydrogenases. AraDH is a member of the medium chain dehydrogenase/reductase family and catalyzes the NAD(P)-dependent oxidation of D-arabinose and other pentoses, the initial step in the metabolism of d-arabinose into 2-oxoglutarate. Like the alcohol dehydrogenases, AraDH binds a zinc in the catalytic cleft as well as a distal structural zinc. AraDH forms homotetramers as a dimer of dimers. AraDH replaces a conserved catalytic His with replace with Arg, compared to the canonical ADH site. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176187 [Multi-domain]  Cd Length: 340  Bit Score: 136.92  E-value: 3.87e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGS---KHLDLLYPTILGHEGAGIVESIGEGVSTVKP 87
Cdd:cd05284    2 KAARLYEYGKPLRLEDVPVPEPGPGQVLVRVGGAGVCHSDLHVIDGvwgGILPYKLPFTLGHENAGWVEEVGSGVDGLKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  88 GDKVItLFLPQ-CGECTSCLNSEGNFCiqFKQSKTQLMSDGTsrftckgksiyhfgntstFCEYTVIKEISVAK-IDAVA 165
Cdd:cd05284   82 GDPVV-VHPPWgCGTCRYCRRGEENYC--ENARFPGIGTDGG------------------FAEYLLVPSRRLVKlPRGLD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 166 PLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQ 245
Cdd:cd05284  141 PVEAAPLADAGLTAYHAVKKALPYLDPGSTVVVIGVGGLGHIAVQILRALTPATVIAVDRSEEALKLAERLGADHVLNAS 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 246 DlkKPIQEVLfDMT-----DAGIDFcfeaIGNLDVLAAAlASCNESYGVCVVVGvlpasvqLKISGQLFFSGRSLKGSVF 320
Cdd:cd05284  221 D--DVVEEVR-ELTggrgaDAVIDF----VGSDETLALA-AKLLAKGGRYVIVG-------YGGHGRLPTSDLVPTEISV 285
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 156523966 321 GG--WKSRQHIPKLVAdyMAEKLNLDPLITHTLnLDKINEAVELMKTGK 367
Cdd:cd05284  286 IGslWGTRAELVEVVA--LAESGKVKVEITKFP-LEDANEALDRLREGR 331
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
11-367 6.02e-37

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: 136.05  E-value: 6.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAP--FSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVL-GSKHLDLLYPTILGHEGAGIVESIGEGVSTVKP 87
Cdd:COG0604    2 KAIVITEFGGPevLELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRrGLYPLPPGLPFIPGSDAAGVVVAVGEGVTGFKV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  88 GDKVITLFlpqcgectsclnsegnfciqfkqsktqlmsdgtsrftckgksiyHFGntsTFCEYTVIKEISVAKIDAVAPL 167
Cdd:COG0604   82 GDRVAGLG--------------------------------------------RGG---GYAEYVVVPADQLVPLPDGLSF 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 168 EKVCLISCGFSTGFGAAINTAKVTPGSTCAVFG-LGGVGLSVVMGCKAAGAaRIIGVDVNKEKFKKAQELGATECLN--P 244
Cdd:COG0604  115 EEAAALPLAGLTAWQALFDRGRLKPGETVLVHGaAGGVGSAAVQLAKALGA-RVIATASSPEKAELLRALGADHVIDyrE 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 245 QDLKKPIQEVLfdmTDAGIDFCFEAIGNlDVLAAALASCNEsYGVCVVVGVLP-ASVQLKIsGQLFFSGRSLKGSVFGGW 323
Cdd:COG0604  194 EDFAERVRALT---GGRGVDVVLDTVGG-DTLARSLRALAP-GGRLVSIGAASgAPPPLDL-APLLLKGLTLTGFTLFAR 267
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 156523966 324 KSRQHIPKL--VADYMAEKlNLDPLITHTLNLDKINEAVELMKTGK 367
Cdd:COG0604  268 DPAERRAALaeLARLLAAG-KLRPVIDRVFPLEEAAEAHRLLESGK 312
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
24-373 2.24e-36

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: 136.13  E-value: 2.24e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  24 IEEVEVAPPK---AKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQCG 100
Cdd:cd08283   12 VRVEEVPDPKiedPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGPEVRNLKVGDRVVVPFTIACG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 101 ECTSCLNSEGNFCIQFKQSKTQLMSDGTSrftckGKSIyhFGNTSTF-------CEYTVI--KEISVAKIDAVAPLEKVC 171
Cdd:cd08283   92 ECFYCKRGLYSQCDNTNPSAEMAKLYGHA-----GAGI--FGYSHLTggyaggqAEYVRVpfADVGPFKIPDDLSDEKAL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 172 LISCGFSTGFGAAINtAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDLKKPI 251
Cdd:cd08283  165 FLSDILPTGYHAAEL-AEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLGAETINFEEVDDVV 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 252 QEVLfDMTD-AGIDFCFEAIG---------------------NLDVLAAALASCNEsYGVCVVVGVLPASVQLKISGQLF 309
Cdd:cd08283  244 EALR-ELTGgRGPDVCIDAVGmeahgsplhkaeqallkletdRPDALREAIQAVRK-GGTVSIIGVYGGTVNKFPIGAAM 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156523966 310 FSGRSLKGsvfGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELM--KTGKCIRCIL 373
Cdd:cd08283  322 NKGLTLRM---GQTHVQRYLPRLLELIESGELDPSFIITHRLPLEDAPEAYKIFdkKEDGCIKVVL 384
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
11-373 6.93e-36

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: 133.89  E-value: 6.93e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKV------LGSKHLDLL------YPTILGHEGAGIVESI 78
Cdd:cd08240    2 KAAAVVEPGKPLEEVEIDTPKPPGTEVLVKVTACGVCHSDLHIwdggydLGGGKTMSLddrgvkLPLVLGHEIVGEVVAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  79 GEGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCiqfkqsktqlmsdgtsrftCKGKS--IYHFGNtstFCEYTVIK-E 155
Cdd:cd08240   82 GPDAADVKVGDKVLVYPWIGCGECPVCLAGDENLC-------------------AKGRAlgIFQDGG---YAEYVIVPhS 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 156 ISVAKIDAVaPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQE 235
Cdd:cd08240  140 RYLVDPGGL-DPALAATLACSGLTAYSAVKKLMPLVADEPVVIIGAGGLGLMALALLKALGPANIIVVDIDEAKLEAAKA 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 236 LGATECLNPQDL--KKPIQEVLFDMTDAGIDFcfeaIGNLDVLAAALaSCNESYGVCVVVGVLPASVQLKISGqLFFSGR 313
Cdd:cd08240  219 AGADVVVNGSDPdaAKRIIKAAGGGVDAVIDF----VNNSATASLAF-DILAKGGKLVLVGLFGGEATLPLPL-LPLRAL 292
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156523966 314 SLKGSVFGgwkSRQHIPKLVAdyMAEKLNLDPLITHTLNLDKINEAVELMKTGKCI-RCIL 373
Cdd:cd08240  293 TIQGSYVG---SLEELRELVA--LAKAGKLKPIPLTERPLSDVNDALDDLKAGKVVgRAVL 348
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
11-367 4.99e-35

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: 130.90  E-value: 4.99e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDK 90
Cdd:cd08245    1 KAAVVHAAGGPLEPEEVPVPEPGPGEVLIKIEACGVCHTDLHAAEGDWGGSKYPLVPGHEIVGEVVEVGAGVEGRKVGDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  91 V-ITLFLPQCGECTSCLNSEGNFCIqfKQSKTQLMSDGtsrftckgksiyhfgntsTFCEYTVIKEISVAKIDAVAPLEK 169
Cdd:cd08245   81 VgVGWLVGSCGRCEYCRRGLENLCQ--KAVNTGYTTQG------------------GYAEYMVADAEYTVLLPDGLPLAQ 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 170 VCLISCGFSTGFgAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGAteclnpqdlkk 249
Cdd:cd08245  141 AAPLLCAGITVY-SALRDAGPRPGERVAVLGIGGLGHLAVQYARAMG-FETVAITRSPDKRELARKLGA----------- 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 250 piqEVLFDMTDAGIDfcFEAIGNLDVL---AAALASCNESY------GVCVVVGVLPASVQLKISGQLFFSGRSLKGSVF 320
Cdd:cd08245  208 ---DEVVDSGAELDE--QAAAGGADVIlvtVVSGAAAEAALgglrrgGRIVLVGLPESPPFSPDIFPLIMKRQSIAGSTH 282
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 156523966 321 GGWKSRQHIPKLVAdymaeKLNLDPlITHTLNLDKINEAVELMKTGK 367
Cdd:cd08245  283 GGRADLQEALDFAA-----EGKVKP-MIETFPLDQANEAYERMEKGD 323
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
11-373 9.59e-34

formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol dehydrogenases and glutathione-dependant formaldehyde dehydrogenases (FDH) of the zinc-dependent/medium chain alcohol dehydrogenase family. The MDR family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176247 [Multi-domain]  Cd Length: 345  Bit Score: 127.81  E-value: 9.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGApFSIEEVevapPKAKEVR-----IKVVATGLCGTemkvlgskhlDLLY---------PTILGHEGAGIVE 76
Cdd:cd08287    2 RATVIHGPGD-IRVEEV----PDPVIEEptdavIRVVATCVCGS----------DLWPyrgvsptraPAPIGHEFVGVVE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  77 SIGEGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSKTQlmSDGtsrftCKGKSIyhfgnTSTFCEYTVIK-- 154
Cdd:cd08287   67 EVGSEVTSVKPGDFVIAPFAISDGTCPFCRAGFTTSCVHGGFWGAF--VDG-----GQGEYV-----RVPLADGTLVKvp 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 155 ---EISVAKIDAVAPLEKVcliscgFSTGFGAAInTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFK 231
Cdd:cd08287  135 gspSDDEDLLPSLLALSDV------MGTGHHAAV-SAGVRPGSTVVVVGDGAVGLCAVLAAKRLGAERIIAMSRHEDRQA 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 232 KAQELGATECLnPQDLKKPIQEVLfDMTDA-GIDFCFEAIGNLDVLAAALASCNESyGVCVVVGVLPASVQLKIsGQLFF 310
Cdd:cd08287  208 LAREFGATDIV-AERGEEAVARVR-ELTGGvGADAVLECVGTQESMEQAIAIARPG-GRVGYVGVPHGGVELDV-RELFF 283
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156523966 311 SGRSLKGsvfGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCIL 373
Cdd:cd08287  284 RNVGLAG---GPAPVRRYLPELLDDVLAGRINPGRVFDLTLPLDEVAEGYRAMDERRAIKVLL 343
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
11-361 3.28e-33

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: 126.60  E-value: 3.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGApfsIEEVEVAPPKAKE---VRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKP 87
Cdd:cd08286    2 KALVYHGPGK---ISWEDRPKPTIQEptdAIVKMLKTTICGTDLHILKGDVPTVTPGRILGHEGVGVVEEVGSAVTNFKV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  88 GDKVITLFLPQCGECTSClnsegnfciqfkqsKTQLMSDgtsrftCKGKSiYHFGNT--STFCEYTVI--KEISVAKIDA 163
Cdd:cd08286   79 GDRVLISCISSCGTCGYC--------------RKGLYSH------CESGG-WILGNLidGTQAEYVRIphADNSLYKLPE 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 164 VAPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLN 243
Cdd:cd08286  138 GVDEEAAVMLSDILPTGYECGVLNGKVKPGDTVAIVGAGPVGLAALLTAQLYSPSKIIMVDLDDNRLEVAKKLGATHTVN 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 244 PQDLKkpIQEVLFDMTDA-GIDFCFEAIG-------NLDVLAAAlascnesyGVCVVVGVLPASVQLKISgQLFFSGRSL 315
Cdd:cd08286  218 SAKGD--AIEQVLELTDGrGVDVVIEAVGipatfelCQELVAPG--------GHIANVGVHGKPVDLHLE-KLWIKNITI 286
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 156523966 316 KgsvfGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVE 361
Cdd:cd08286  287 T----TGLVDTNTTPMLLKLVSSGKLDPSKLVTHRFKLSEIEKAYD 328
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
17-368 7.10e-33

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: 125.30  E-value: 7.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  17 KPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKV-ITLF 95
Cdd:cd05283    7 DASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDRVgVGCQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  96 LPQCGECTSCLNSEGNFCiqfkqsktqlmsdgtSRFTCKGKSIYHFGNTST--FCEYTVIKEISVAKI------DAVAPL 167
Cdd:cd05283   87 VDSCGTCEQCKSGEEQYC---------------PKGVVTYNGKYPDGTITQggYADHIVVDERFVFKIpegldsAAAAPL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 168 ekvcliSCGFSTGFgAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGATECL---NP 244
Cdd:cd05283  152 ------LCAGITVY-SPLKRNGVGPGKRVGVVGIGGLGHLAVKFAKALG-AEVTAFSRSPSKKEDALKLGADEFIatkDP 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 245 QDLKKPIQEVLFDMTDAGIDFCFEAIgnLDVLAaalascneSYGVCVVVGVLPASVQLKiSGQLFFSGRSLKGSVFGGwk 324
Cdd:cd05283  224 EAMKKAAGSLDLIIDTVSASHDLDPY--LSLLK--------PGGTLVLVGAPEEPLPVP-PFPLIFGRKSVAGSLIGG-- 290
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 156523966 325 sRQHIPKLVaDYMAEKlNLDPLIThTLNLDKINEAVELMKTGKC 368
Cdd:cd05283  291 -RKETQEML-DFAAEH-GIKPWVE-VIPMDGINEALERLEKGDV 330
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
17-373 1.36e-32

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 124.55  E-value: 1.36e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  17 KPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMkvlgskHLdllY------------PTILGHEGAGIVESIGEGVST 84
Cdd:PRK05396   8 KAEPGLWLTDVPVPEPGPNDVLIKVKKTAICGTDV------HI---YnwdewaqktipvPMVVGHEFVGEVVEVGSEVTG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  85 VKPGDKV-----ITlflpqCGECTSCLNSEGNFCIqfkqsKTQLMsdGTSRFTCkgksiyhfgntstFCEYTVIKEISVA 159
Cdd:PRK05396  79 FKVGDRVsgeghIV-----CGHCRNCRAGRRHLCR-----NTKGV--GVNRPGA-------------FAEYLVIPAFNVW 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 160 KIDAVAPLEkvclISCGFSTgFGAAINTAKVTP--GSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELG 237
Cdd:PRK05396 134 KIPDDIPDD----LAAIFDP-FGNAVHTALSFDlvGEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELARKMG 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 238 ATECLNP--QDLKKPIQEvlFDMTDaGIDFCFEAIGNLDVLAAALASCNESyGVCVVVGVLPASVQLKIsGQLFFSGRSL 315
Cdd:PRK05396 209 ATRAVNVakEDLRDVMAE--LGMTE-GFDVGLEMSGAPSAFRQMLDNMNHG-GRIAMLGIPPGDMAIDW-NKVIFKGLTI 283
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156523966 316 KG----SVFGGWKSrqhipklVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKCIRCIL 373
Cdd:PRK05396 284 KGiygrEMFETWYK-------MSALLQSGLDLSPIITHRFPIDDFQKGFEAMRSGQSGKVIL 338
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
11-374 1.62e-32

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 124.38  E-value: 1.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCgtemkvlgskHLDLL----------YPTILGHEGAGIVESIGE 80
Cdd:PRK13771   2 KAVILPGFKQGYRIEEVPDPKPGKDEVVIKVNYAGLC----------YRDLLqlqgfyprmkYPVILGHEVVGTVEEVGE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  81 GVSTVKPGDKVITLFLPQCGECTSCLNSEGNFciqfkqsktqlmsdgtsrftCKGKSIYHFGNTSTFCEYTVIKEISVAK 160
Cdd:PRK13771  72 NVKGFKPGDRVASLLYAPDGTCEYCRSGEEAY--------------------CKNRLGYGEELDGFFAEYAKVKVTSLVK 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 161 IDAVAPLEKVCLISCGFSTGFgAAINTAKVTPGSTCAVFGL-GGVGLSVVMGCKAAGaARIIGVDVNKEKFK---KAQEL 236
Cdd:PRK13771 132 VPPNVSDEGAVIVPCVTGMVY-RGLRRAGVKKGETVLVTGAgGGVGIHAIQVAKALG-AKVIAVTSSESKAKivsKYADY 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 237 GATECLNPQDLKKPiqevlfdmtdAGIDFCFEAIGNlDVLAAALASCNESYGVCVVVGVLPASV-QLKIsGQLFFSGRSL 315
Cdd:PRK13771 210 VIVGSKFSEEVKKI----------GGADIVIETVGT-PTLEESLRSLNMGGKIIQIGNVDPSPTySLRL-GYIILKDIEI 277
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 156523966 316 KGSVFGGWKSRQHIPKLVAdymaeKLNLDPLITHTLNLDKINEAVELMKTGKCIRCILL 374
Cdd:PRK13771 278 IGHISATKRDVEEALKLVA-----EGKIKPVIGAEVSLSEIDKALEELKDKSRIGKILV 331
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
22-363 1.52e-31

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: 121.31  E-value: 1.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  22 FSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVL--GSKHL-DLLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLflpq 98
Cdd:cd08269    7 FEVEEHPRPTPGPGQVLVRVEGCGVCGSDLPAFnqGRPWFvYPAEPGGPGHEGWGRVVALGPGVRGLAVGDRVAGL---- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  99 cgectsclnsegnfciqfkqsktqlmsdgtsrftckgksiyhfgNTSTFCEYTVIKEISVAKIDAVA-----PLEKVcli 173
Cdd:cd08269   83 --------------------------------------------SGGAFAEYDLADADHAVPLPSLLdgqafPGEPL--- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 174 SCGFStgfgaAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATEClnPQDLKKPIQE 253
Cdd:cd08269  116 GCALN-----VFRRGWIRAGKTVAVIGAGFIGLLFLQLAAAAGARRVIAIDRRPARLALARELGATEV--VTDDSEAIVE 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 254 VLFDMTD-AGIDFCFEAIGNLDVLAAALASCNESyGVCVVVGV---LPASVQLkisGQLFFSGRSLKGSVFGGWK-SRQH 328
Cdd:cd08269  189 RVRELTGgAGADVVIEAVGHQWPLDLAGELVAER-GRLVIFGYhqdGPRPVPF---QTWNWKGIDLINAVERDPRiGLEG 264
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 156523966 329 IPKLVADYMAEKLNLDPLITHTLNLDKINEAVELM 363
Cdd:cd08269  265 MREAVKLIADGRLDLGSLLTHEFPLEELGDAFEAA 299
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
24-362 3.54e-31

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays a broad range of activities and are distinguished from the smaller short chain dehydrogenases(~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 120.80  E-value: 3.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  24 IEEVEVAPPKAKEVRIKVVATGLCGTemkvlgskhlDLLY-------------PTILGHEGAGIVESIGEGVSTVKPGDK 90
Cdd:cd08232   11 VEERPAPEPGPGEVRVRVAAGGICGS----------DLHYyqhggfgtvrlrePMVLGHEVSGVVEAVGPGVTGLAPGQR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  91 V-ITLFLPqCGECTSCLNSEGNFCiqfkqsktqlmsdGTSRFtckgksiyhFGNTST-------FCEYTVIKEISVAKID 162
Cdd:cd08232   81 VaVNPSRP-CGTCDYCRAGRPNLC-------------LNMRF---------LGSAMRfphvqggFREYLVVDASQCVPLP 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 163 AVAPLEK--------VCLiscgfstgfgAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQ 234
Cdd:cd08232  138 DGLSLRRaalaeplaVAL----------HAVNRAGDLAGKRVLVTGAGPIGALVVAAARRAGAAEIVATDLADAPLAVAR 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 235 ELGATECLNPQDlkkpiQEVLFDMTDAG-IDFCFEAIGNldvlAAALASCNESY---GVCVVVGVLPASVQLKISGQLff 310
Cdd:cd08232  208 AMGADETVNLAR-----DPLAAYAADKGdFDVVFEASGA----PAALASALRVVrpgGTVVQVGMLGGPVPLPLNALV-- 276
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156523966 311 sGRSLkgSVFGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVEL 362
Cdd:cd08232  277 -AKEL--DLRGSFRFDDEFAEAVRLLAAGRIDVRPLITAVFPLEEAAEAFAL 325
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
11-367 1.10e-30

Alcohol dehydrogenases of the MDR family; This group contains proteins related to the zinc-dependent alcohol dehydrogenases. However, while the group has structural zinc site characteristic of these enzymes, it lacks the consensus site for a catalytic zinc. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 119.67  E-value: 1.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAP--FSIEEVEVAPPKAKEVRIKVVATGLcgtemkvlgsKHLDLL-----------YPTILGHEGAGIVES 77
Cdd:cd08266    2 KAVVIRGHGGPevLEYGDLPEPEPGPDEVLVRVKAAAL----------NHLDLWvrrgmpgiklpLPHILGSDGAGVVEA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  78 IGEGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKqsktqlmsdgtsrftckgksIYHFGNTSTFCEYTVIKEIS 157
Cdd:cd08266   72 VGPGVTNVKPGQRVVIYPGISCGRCEYCLAGRENLCAQYG--------------------ILGEHVDGGYAEYVAVPARN 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 158 VAKIDAVAPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLG-GVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQEL 236
Cdd:cd08266  132 LLPIPDNLSFEEAAAAPLTFLTAWHMLVTRARLRPGETVLVHGAGsGVGSAAIQIAKLFG-ATVIATAGSEDKLERAKEL 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 237 GATECLNPQdlKKPIQEVLFDMTDA-GIDFCFEAIG------NLDVLA--AALASCNESYGVcvvvgvlpaSVQLKISgQ 307
Cdd:cd08266  211 GADYVIDYR--KEDFVREVRELTGKrGVDVVVEHVGaatwekSLKSLArgGRLVTCGATTGY---------EAPIDLR-H 278
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 308 LFFSGRSLKGSVFGGWKSRQHIPKLVadymaEKLNLDPLITHTLNLDKINEAVELMKTGK 367
Cdd:cd08266  279 VFWRQLSILGSTMGTKAELDEALRLV-----FRGKLKPVIDSVFPLEEAAEAHRRLESRE 333
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
11-280 1.09e-28

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


Pssm-ID: 176219 [Multi-domain]  Cd Length: 306  Bit Score: 113.56  E-value: 1.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGaPFSIEEVEVAPPKA--KEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPG 88
Cdd:cd08258    2 KALVKTGPG-PGNVELREVPEPEPgpGEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEVGPDVEGWKVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  89 DKVI--TLFLpQCGECTSCLNSEGNFCiqfkqsktqlmsdgTSRftcKGksiyhFGNT--STFCEYTVIKEISVAKIDAV 164
Cdd:cd08258   81 DRVVseTTFS-TCGRCPYCRRGDYNLC--------------PHR---KG-----IGTQadGGFAEYVLVPEESLHELPEN 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 165 APLEKVCL---ISCGFStgfgAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARII-GVDVNKEKFKKAQELGATE 240
Cdd:cd08258  138 LSLEAAALtepLAVAVH----AVAERSGIRPGDTVVVFGPGPIGLLAAQVAKLQGATVVVvGTEKDEVRLDVAKELGADA 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 156523966 241 C-LNPQDLKKPIQEvlfdMTDA-GIDFCFEAIGNLDVLAAAL 280
Cdd:cd08258  214 VnGGEEDLAELVNE----ITDGdGADVVIECSGAVPALEQAL 251
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
22-362 1.17e-28

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: 114.92  E-value: 1.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  22 FSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGS-KHLDLLY------PTILGHEGAGIVESIGEGVSTVKPGDKVITL 94
Cdd:cd08265   39 LRVEDVPVPNLKPDEILIRVKACGICGSDIHLYETdKDGYILYpgltefPVVIGHEFSGVVEKTGKNVKNFEKGDPVTAE 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  95 FLPQCGECTSCLNSEGNFCIQFKQskTQLMSDGTsrftckgksiyhfgntstFCEYTVIKEISVAKI------------- 161
Cdd:cd08265  119 EMMWCGMCRACRSGSPNHCKNLKE--LGFSADGA------------------FAEYIAVNARYAWEInelreiysedkaf 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 162 DAVAPLEKVcliSCGFSTGFgaaINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATEC 241
Cdd:cd08265  179 EAGALVEPT---SVAYNGLF---IRGGGFRPGAYVVVYGAGPIGLAAIALAKAAGASKVIAFEISEERRNLAKEMGADYV 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 242 LNPQDLKK--PIQEVLFDMTDAGIDFCFEAIGnldVLAAALASCNESYGV-CVVVGVLPASVQLKISGQLFFSGRslkGS 318
Cdd:cd08265  253 FNPTKMRDclSGEKVMEVTKGWGADIQVEAAG---APPATIPQMEKSIAInGKIVYIGRAATTVPLHLEVLQVRR---AQ 326
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 156523966 319 VFGgwkSRQH-----IPKLVADYMAEKLNLDPLITHTLNLDKINEAVEL 362
Cdd:cd08265  327 IVG---AQGHsghgiFPSVIKLMASGKIDMTKIITARFPLEGIMEAIKA 372
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
19-271 2.43e-26

Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. PFDH converts 2 molecules of aldehydes to corresponding carboxylic acid and alcohol. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176242 [Multi-domain]  Cd Length: 375  Bit Score: 108.06  E-value: 2.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  19 GAPFSIEEVEVAPPKAKE---VRIKVVATGLCGTemkvlgskhlDL-LY--------PTILGHEGAGIVESIGEGVSTVK 86
Cdd:cd08282    7 GGPGNVAVEDVPDPKIEHptdAIVRITTTAICGS----------DLhMYrgrtgaepGLVLGHEAMGEVEEVGSAVESLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  87 PGDKVITLFLPQCGECTSCLNSEGNFCiqfkqsktqlmSDGTSRFTCKGKSIYHFGN-TSTFCEYTVI--KEISVAKI-- 161
Cdd:cd08282   77 VGDRVVVPFNVACGRCRNCKRGLTGVC-----------LTVNPGRAGGAYGYVDMGPyGGGQAEYLRVpyADFNLLKLpd 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 162 --DAVAPLEKVCLiSCGFSTGFgAAINTAKVTPGSTCAVFGLGGVGLsvvMGCKAA---GAARIIGVDVNKEKFKKAQEL 236
Cdd:cd08282  146 rdGAKEKDDYLML-SDIFPTGW-HGLELAGVQPGDTVAVFGAGPVGL---MAAYSAilrGASRVYVVDHVPERLDLAESI 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 156523966 237 GATeclnPQDLKK--PIQEVL---FDMTDAGIDfC--FEAIG 271
Cdd:cd08282  221 GAI----PIDFSDgdPVEQILglePGGVDRAVD-CvgYEARD 257
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
11-367 4.44e-26

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: 106.43  E-value: 4.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAP-PKAK-EVRIKVVATGLCgtemkvlgskHLDLLY-----------PTILGHEGAGIVES 77
Cdd:cd08241    2 KAVVCKELGGPEDLVLEEVPPePGAPgEVRIRVEAAGVN----------FPDLLMiqgkyqvkpplPFVPGSEVAGVVEA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  78 IGEGVSTVKPGDKVITLflpqcgectsclnsegnfciqfkqsktqlmsdgtsrftckgksiyhfGNTSTFCEYTVIKEIS 157
Cdd:cd08241   72 VGEGVTGFKVGDRVVAL-----------------------------------------------TGQGGFAEEVVVPAAA 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 158 VAKI-DAVAPLEKVCLIsCGFSTGFGAAINTAKVTPGSTCAVFGL-GGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQE 235
Cdd:cd08241  105 VFPLpDGLSFEEAAALP-VTYGTAYHALVRRARLQPGETVLVLGAaGGVGLAAVQLAKALG-ARVIAAASSEEKLALARA 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 236 LGATECLNPQDlkKPIQEVLFDMTD-AGIDFCFEAIGnLDVLAAALASCNESyGVCVVVG-------VLPASVqlkisgq 307
Cdd:cd08241  183 LGADHVIDYRD--PDLRERVKALTGgRGVDVVYDPVG-GDVFEASLRSLAWG-GRLLVIGfasgeipQIPANL------- 251
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156523966 308 LFFSGRSLKGSVFGGWksRQHIPKLVADYMAEKLNL------DPLITHTLNLDKINEAVELMKTGK 367
Cdd:cd08241  252 LLLKNISVVGVYWGAY--ARREPELLRANLAELFDLlaegkiRPHVSAVFPLEQAAEALRALADRK 315
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
11-367 1.01e-25

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176258 [Multi-domain]  Cd Length: 329  Bit Score: 105.73  E-value: 1.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGA----PFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVK 86
Cdd:cd08298    2 KAMVLEKPGPieenPLRLTEVPVPEPGPGEVLIKVEACGVCRTDLHIVEGDLPPPKLPLIPGHEIVGRVEAVGPGVTRFS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  87 PGDKV-ITLFLPQCGECTSCLNSEGNFCIQFkqsktqlmsdgtsRFTckGKSIyHFGntstFCEYTVIKEISVAKIDAVA 165
Cdd:cd08298   82 VGDRVgVPWLGSTCGECRYCRSGRENLCDNA-------------RFT--GYTV-DGG----YAEYMVADERFAYPIPEDY 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 166 PLEKVCLISCGFSTGFGaAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGATECLNPQ 245
Cdd:cd08298  142 DDEEAAPLLCAGIIGYR-ALKLAGLKPGQRLGLYGFGASAHLALQIARYQG-AEVFAFTRSGEHQELARELGADWAGDSD 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 246 DLK-KPIqevlfdmtDAGIDFCfeAIGnlDVLAAALASCNEsyGVCVVVGVLPASVQLKISGQLFFSGRSLKGSVFGgwk 324
Cdd:cd08298  220 DLPpEPL--------DAAIIFA--PVG--ALVPAALRAVKK--GGRVVLAGIHMSDIPAFDYELLWGEKTIRSVANL--- 282
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 156523966 325 SRQHIPKLVAdyMAEKLNLDPlITHTLNLDKINEAVELMKTGK 367
Cdd:cd08298  283 TRQDGEEFLK--LAAEIPIKP-EVETYPLEEANEALQDLKEGR 322
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
11-367 4.34e-25

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 103.96  E-value: 4.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVlgsKHLDLLYPT--ILGHEGAGIVESIGEGVSTVKPG 88
Cdd:PRK09422   2 KAAVVNKDHTGDVVVEKTLRPLKHGEALVKMEYCGVCHTDLHV---ANGDFGDKTgrILGHEGIGIVKEVGPGVTSLKVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  89 DKV-ITLFLPQCGECTSCLNSEGNFCIQFKQSktqlmsdgtsrftckGKSIYhfGNTSTFCeyTVIKEISVAKIDAVAPL 167
Cdd:PRK09422  79 DRVsIAWFFEGCGHCEYCTTGRETLCRSVKNA---------------GYTVD--GGMAEQC--IVTADYAVKVPEGLDPA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 168 EKVClISCGFSTGFgAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNP--- 244
Cdd:PRK09422 140 QASS-ITCAGVTTY-KAIKVSGIKPGQWIAIYGAGGLGNLALQYAKNVFNAKVIAVDINDDKLALAKEVGADLTINSkrv 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 245 QDLKKPIQEvlfdmTDAGIDfcfeaigNLDVLAAALASCNESY------GVCVVVGVLPASVQLKISgQLFFSGRSLKGS 318
Cdd:PRK09422 218 EDVAKIIQE-----KTGGAH-------AAVVTAVAKAAFNQAVdavragGRVVAVGLPPESMDLSIP-RLVLDGIEVVGS 284
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 156523966 319 VFGgwkSRQHIpKLVADYMAEKLnLDPLIThTLNLDKINEAVELMKTGK 367
Cdd:PRK09422 285 LVG---TRQDL-EEAFQFGAEGK-VVPKVQ-LRPLEDINDIFDEMEQGK 327
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
11-367 2.45e-24

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


Pssm-ID: 176256 [Multi-domain]  Cd Length: 333  Bit Score: 101.94  E-value: 2.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDK 90
Cdd:cd08296    2 KAVQVTEPGGPLELVERDVPLPGPGEVLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVGEGVSRWKVGDR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  91 V-ITLFLPQCGECTSClnSEGNFciqfkqsktqlmsdgtsrFTCKGKSI----YHFGntstFCEYTVIKEISVAKI-DAV 164
Cdd:cd08296   82 VgVGWHGGHCGTCDAC--RRGDF------------------VHCENGKVtgvtRDGG----YAEYMLAPAEALARIpDDL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 165 APLEKVCLISCGFSTgFGaAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGATECLN- 243
Cdd:cd08296  138 DAAEAAPLLCAGVTT-FN-ALRNSGAKPGDLVAVQGIGGLGHLAVQYAAKMG-FRTVAISRGSDKADLARKLGAHHYIDt 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 244 -PQDLKKPIQE------VLFDMTDAgidfcfEAIgnldvlaAALASCNESYGVCVVVGVLPASVQLkISGQLFFSGRSLK 316
Cdd:cd08296  215 sKEDVAEALQElggaklILATAPNA------KAI-------SALVGGLAPRGKLLILGAAGEPVAV-SPLQLIMGRKSIH 280
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 156523966 317 GSVFGgwksrqhIPKLVADYMAEKLNLD--PLItHTLNLDKINEAVELMKTGK 367
Cdd:cd08296  281 GWPSG-------TALDSEDTLKFSALHGvrPMV-ETFPLEKANEAYDRMMSGK 325
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
203-323 2.09e-23

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 94.21  E-value: 2.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  203 GVGLSVVMGCKAAGAaRIIGVDVNKEKFKKAQELGATECLNPQDLKkpIQEVLFDMTDA-GIDFCFEAIGNLDVLAAALA 281
Cdd:pfam00107   1 GVGLAAIQLAKAAGA-KVIAVDGSEEKLELAKELGADHVINPKETD--LVEEIKELTGGkGVDVVFDCVGSPATLEQALK 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 156523966  282 SCNEsYGVCVVVGVLPASVQLKIsGQLFFSGRSLKGSVFGGW 323
Cdd:pfam00107  78 LLRP-GGRVVVVGLPGGPLPLPL-APLLLKELTILGSFLGSP 117
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
11-367 6.83e-22

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


Pssm-ID: 176218 [Multi-domain]  Cd Length: 350  Bit Score: 95.17  E-value: 6.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGaPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVL-------GSKHLD--LLYPTILGHEGAGIVESIGEG 81
Cdd:cd08256    2 RAVVCHGPQ-DYRLEEVPVPRPGPGEILVKVEACGICAGDIKCYhgapsfwGDENQPpyVKPPMIPGHEFVGRVVELGEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  82 VST--VKPGDKVITLFLPQCGECTSClnSEGNFciqfkqsktqlmsdgtsrFTCKGKSIYHFGNTST--FCEYTVI-KEI 156
Cdd:cd08256   81 AEErgVKVGDRVISEQIVPCWNCRFC--NRGQY------------------WMCQKHDLYGFQNNVNggMAEYMRFpKEA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 157 SVAKIDAVAPLEKVCLI---SCGFStgfgaAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKA 233
Cdd:cd08256  141 IVHKVPDDIPPEDAILIeplACALH-----AVDRANIKFDDVVVLAGAGPLGLGMIGAARLKNPKKLIVLDLKDERLALA 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 234 QELGATECLNPQdlKKPIQEVLFDMTDA-GIDFCFEAIGNLDVLAAALASCNEsYGVCVVVGVL--PASVQLKISG---Q 307
Cdd:cd08256  216 RKFGADVVLNPP--EVDVVEKIKELTGGyGCDIYIEATGHPSAVEQGLNMIRK-LGRFVEFSVFgdPVTVDWSIIGdrkE 292
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156523966 308 LffsgrSLKGSVFGgwksrQHIPKLVADYMAE-KLNLDPLITHTLNLDKINEAVELMKTGK 367
Cdd:cd08256  293 L-----DVLGSHLG-----PYCYPIAIDLIASgRLPTDGIVTHQFPLEDFEEAFELMARGD 343
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
11-366 9.67e-22

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: 94.59  E-value: 9.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAP--FSIEEVEVAPPKAKEVRIKVVATGLCGTE-MKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKP 87
Cdd:cd08268    2 RAVRFHQFGGPevLRIEELPVPAPGAGEVLIRVEAIGLNRADaMFRRGAYIEPPPLPARLGYEAAGVVEAVGAGVTGFAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  88 GDKVITL--FLPQCGectsclnsegnfciqfkqsktqlmsdgtsrftckgksiyhfgntSTFCEYTVIKEISVAKI-DAV 164
Cdd:cd08268   82 GDRVSVIpaADLGQY--------------------------------------------GTYAEYALVPAAAVVKLpDGL 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 165 APLEKV-CLIScgFSTGFGAAINTAKVTPGSTCAVFGL-GGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGATECL 242
Cdd:cd08268  118 SFVEAAaLWMQ--YLTAYGALVELAGLRPGDSVLITAAsSSVGLAAIQIANAAG-ATVIATTRTSEKRDALLALGAAHVI 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 243 N--PQDLKKpiqEVLFDMTDAGIDFCFEAIGNLDV--LAAALAscneSYGVCVVVGVL---PASVQLKIsgqLFFSGRSL 315
Cdd:cd08268  195 VtdEEDLVA---EVLRITGGKGVDVVFDPVGGPQFakLADALA----PGGTLVVYGALsgePTPFPLKA---ALKKSLTF 264
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156523966 316 KG-SVFGGWKSRQHIPKLVA--DYMAEKLNLDPLITHTLNLDKINEAVELMKTG 366
Cdd:cd08268  265 RGySLDEITLDPEARRRAIAfiLDGLASGALKPVVDRVFPFDDIVEAHRYLESG 318
PRK10083 PRK10083
putative oxidoreductase; Provisional
11-375 1.76e-21

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 94.04  E-value: 1.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGApFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDK 90
Cdd:PRK10083   2 KSIVIEKPNS-LAIEERPIPQPAAGEVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGEGVDAARIGER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  91 VITLFLPQCGECTSCLNSEGNFCiqfkqskTQLMSDGTSRftckgksiyhfgnTSTFCEYTVIKEISVAKIDAVAPLEKV 170
Cdd:PRK10083  81 VAVDPVISCGHCYPCSIGKPNVC-------TSLVVLGVHR-------------DGGFSEYAVVPAKNAHRIPDAIADQYA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 171 CLIScgfstGFGAAINT---AKVTPGSTCAVFGLGGVGLSVVMGCKAA-GAARIIGVDVNKEKFKKAQELGATECLNpqD 246
Cdd:PRK10083 141 VMVE-----PFTIAANVtgrTGPTEQDVALIYGAGPVGLTIVQVLKGVyNVKAVIVADRIDERLALAKESGADWVIN--N 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 247 LKKPIQEVLfdmTDAGID--FCFEAIGNLDVL--AAALAScneSYGVCVVVGVLP---ASVQLKISGQ--LFFSGRsLKG 317
Cdd:PRK10083 214 AQEPLGEAL---EEKGIKptLIIDAACHPSILeeAVTLAS---PAARIVLMGFSSepsEIVQQGITGKelSIFSSR-LNA 286
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 318 SVFggwksrqhipKLVADYMAEKLnLDP--LITHTLNLDKINEAVELMKTGKCIRCILLL 375
Cdd:PRK10083 287 NKF----------PVVIDWLSKGL-IDPekLITHTFDFQHVADAIELFEKDQRHCCKVLL 335
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
36-255 1.95e-21

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 94.13  E-value: 1.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  36 EVRIKVVATGLCGTEMKVLgSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQ 115
Cdd:PRK10309  27 DVLVKVASSGLCGSDIPRI-FKNGAHYYPITLGHEFSGYVEAVGSGVDDLHPGDAVACVPLLPCFTCPECLRGFYSLCAK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 116 FkqsktQLMsdGTSRFtckgksiyhfgntSTFCEYTVIKEISVAKIDAVAPLEKVCLIScGFSTGFgAAINTAKVTPGST 195
Cdd:PRK10309 106 Y-----DFI--GSRRD-------------GGNAEYIVVKRKNLFALPTDMPIEDGAFIE-PITVGL-HAFHLAQGCEGKN 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156523966 196 CAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDLKKP-IQEVL 255
Cdd:PRK10309 164 VIIIGAGTIGLLAIQCAVALGAKSVTAIDINSEKLALAKSLGAMQTFNSREMSAPqIQSVL 224
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
36-160 1.35e-20

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: 85.74  E-value: 1.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966   36 EVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIq 115
Cdd:pfam08240   2 EVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYNLCP- 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 156523966  116 fKQSKTQLMSDGtsrftckgksiyhfgntsTFCEYTVIKEISVAK 160
Cdd:pfam08240  81 -NGRFLGYDRDG------------------GFAEYVVVPERNLVP 106
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
11-367 1.47e-20

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: 91.22  E-value: 1.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILwkPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEM-----------KVLGSKHLDLLYPTILGHEGAGIVESIG 79
Cdd:cd08262    2 RAAVF--RDGPLVVRDVPDPEPGPGQVLVKVLACGICGSDLhatahpeamvdDAGGPSLMDLGADIVLGHEFCGEVVDYG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  80 EGVS-TVKPGDKVITLFLPQCGECTSCLnsegnfciqfkqsktqlmsdgtsrftcKGKSIYHFGNtstFCEYTVIKEISV 158
Cdd:cd08262   80 PGTErKLKVGTRVTSLPLLLCGQGASCG---------------------------IGLSPEAPGG---YAEYMLLSEALL 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 159 AKIDAVAPLEKVCLIScGFSTGFGAAiNTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGA 238
Cdd:cd08262  130 LRVPDGLSMEDAALTE-PLAVGLHAV-RRARLTPGEVALVIGCGPIGLAVIAALKARGVGPIVASDFSPERRALALAMGA 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 239 TECLNP-QDLkkPIQevLFDMTDAGI-----DFCFEAIGNLDVLAAALASCnESYGVCVVVGVLPASVQ----LKISGQL 308
Cdd:cd08262  208 DIVVDPaADS--PFA--AWAAELARAggpkpAVIFECVGAPGLIQQIIEGA-PPGGRIVVVGVCMESDNiepaLAIRKEL 282
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 309 ffsgrSLKgsvFGGWKSRQHIpKLVADYMAE-KLNLDPLITHTLNLDKINEAVELMKTGK 367
Cdd:cd08262  283 -----TLQ---FSLGYTPEEF-ADALDALAEgKVDVAPMVTGTVGLDGVPDAFEALRDPE 333
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
11-374 3.41e-20

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


Pssm-ID: 176215 [Multi-domain]  Cd Length: 325  Bit Score: 89.95  E-value: 3.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAP--FSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLY-PTILGHEGAGIVESIGEGVSTVKP 87
Cdd:cd08253    2 RAIRYHEFGAPdvLRLGDLPVPTPGPGEVLVRVHASGVNPVDTYIRAGAYPGLPPlPYVPGSDGAGVVEAVGEGVDGLKV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  88 GDKVitlflpqcgectsclnsegnfciqfkqsktqlmsdgtsrFTCKGKSIYHFGntsTFCEYTVIKEISVAKI-DAVAP 166
Cdd:cd08253   82 GDRV---------------------------------------WLTNLGWGRRQG---TAAEYVVVPADQLVPLpDGVSF 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 167 LEKVCLISCGFsTGFGAAINTAKVTPGSTCAVFG-LGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGATECLNPQ 245
Cdd:cd08253  120 EQGAALGIPAL-TAYRALFHRAGAKAGETVLVHGgSGAVGHAAVQLARWAG-ARVIATASSAEGAELVRQAGADAVFNYR 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 246 DlKKPIQEVLfDMTDA-GIDFCFE--AIGNLDVLAAALAscneSYGVCVVVGVLPASVQLKIsGQLFFSGRSLKG-SVFG 321
Cdd:cd08253  198 A-EDLADRIL-AATAGqGVDVIIEvlANVNLAKDLDVLA----PGGRIVVYGSGGLRGTIPI-NPLMAKEASIRGvLLYT 270
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156523966 322 GWKS-RQHIPKLVADYMAEKlNLDPLITHTLNLDKINEAVELMKTGKCIRCILL 374
Cdd:cd08253  271 ATPEeRAAAAEAIAAGLADG-ALRPVIAREYPLEEAAAAHEAVESGGAIGKVVL 323
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
25-370 1.29e-19

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


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 88.75  E-value: 1.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  25 EEVEVAPPKAKEVRIKVVATGLcgtemkvlgsKHLDLL-----YPT------ILGHEGAGIVESIGEGVSTVKPGDKVIT 93
Cdd:cd08276   18 VEEPVPEPGPGEVLVRVHAVSL----------NYRDLLilngrYPPpvkdplIPLSDGAGEVVAVGEGVTRFKVGDRVVP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  94 LFLPqcgectsclnseGNFCIQFKQSKTQLM----SDGTSRftckgksiyhfgntstfcEYTVIKEISVAKIDAVAPLEK 169
Cdd:cd08276   88 TFFP------------NWLDGPPTAEDEASAlggpIDGVLA------------------EYVVLPEEGLVRAPDHLSFEE 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 170 VCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGATECLNPQDLKK 249
Cdd:cd08276  138 AATLPCAGLTAWNALFGLGPLKPGDTVLVQGTGGVSLFALQFAKAAG-ARVIATSSSDEKLERAKALGADHVINYRTTPD 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 250 PIQEVLfDMT-DAGIDFCFEaIGNLDVLAAALASCNeSYGVCVVVGVLPASVQLKISGQLFFSGRSLKGSVFGgwkSRQH 328
Cdd:cd08276  217 WGEEVL-KLTgGRGVDHVVE-VGGPGTLAQSIKAVA-PGGVISLIGFLSGFEAPVLLLPLLTKGATLRGIAVG---SRAQ 290
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 156523966 329 IPKLVAdyMAEKLNLDPLITHTLNLDKINEAVELMKTGK-----CIR 370
Cdd:cd08276  291 FEAMNR--AIEAHRIRPVIDRVFPFEEAKEAYRYLESGShfgkvVIR 335
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
15-368 1.45e-19

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


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 88.04  E-value: 1.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  15 LWKPGAPFSIEEVEVAPPKAK--EVRIKVVATGLCGTEMKVL-GSKHLDLL--YPTILGHEGAGIVESIGEGVSTVKPGD 89
Cdd:cd08267    5 RYGSPEVLLLLEVEVPIPTPKpgEVLVKVHAASVNPVDWKLRrGPPKLLLGrpFPPIPGMDFAGEVVAVGSGVTRFKVGD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  90 KVI-TLFLPQCGectsclnsegnfciqfkqsktqlmsdgtsrftckgksiyhfgntsTFCEYTVIKEISVAKI-DAVAPL 167
Cdd:cd08267   85 EVFgRLPPKGGG---------------------------------------------ALAEYVVAPESGLAKKpEGVSFE 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 168 EKVCLISCGfSTGFGAAINTAKVTPGSTcaVF---GLGGVGLSVVMGCKAAGaARIIGVDvNKEKFKKAQELGATECLnp 244
Cdd:cd08267  120 EAAALPVAG-LTALQALRDAGKVKPGQR--VLingASGGVGTFAVQIAKALG-AHVTGVC-STRNAELVRSLGADEVI-- 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 245 qDLKKpiQEVLFDMTDAG-IDFCFEAIGNLDVLAAALASCNESYGVCV-VVGVLPASVQLKISGQLFFSGRSLKGSVFGG 322
Cdd:cd08267  193 -DYTT--EDFVALTAGGEkYDVIFDAVGNSPFSLYRASLALKPGGRYVsVGGGPSGLLLVLLLLPLTLGGGGRRLKFFLA 269
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 156523966 323 WKSRQHIPKLvADYMAEKlNLDPLITHTLNLDKINEAVELMKTGKC 368
Cdd:cd08267  270 KPNAEDLEQL-AELVEEG-KLKPVIDSVYPLEDAPEAYRRLKSGRA 313
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
11-367 3.48e-18

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: 84.15  E-value: 3.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAPPKAK--EVRIKVVATGLCGTEMKV---LGSKHLDLLYPTILGHEGAGIVESIGEGVSTV 85
Cdd:cd05289    2 KAVRIHEYGGPEVLELADVPTPEPGpgEVLVKVHAAGVNPVDLKIregLLKAAFPLTLPLIPGHDVAGVVVAVGPGVTGF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  86 KPGDKVItlflpqcgectsclnsegnfciqfkqsktqlmsdGTSRFTCKGksiyhfgntsTFCEYTVIKEISVAKID--- 162
Cdd:cd05289   82 KVGDEVF----------------------------------GMTPFTRGG----------AYAEYVVVPADELALKPanl 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 163 -----AVAPLekVCLiscgfsTGFGAAINTAKVTPGSTcaVF---GLGGVGLSVVMGCKAAGaARIIGVdVNKEKFKKAQ 234
Cdd:cd05289  118 sfeeaAALPL--AGL------TAWQALFELGGLKAGQT--VLihgAAGGVGSFAVQLAKARG-ARVIAT-ASAANADFLR 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 235 ELGATECLNPQDlkkpiQEVLFDMTDAGIDFCFEAIGNlDVLAAALAscnesygvCV-----VVGVLPASVQLKISGQlf 309
Cdd:cd05289  186 SLGADEVIDYTK-----GDFERAAAPGGVDAVLDTVGG-ETLARSLA--------LVkpggrLVSIAGPPPAEQAAKR-- 249
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 156523966 310 fsgRSLKGSVFGGWKSRQHIPKLVAdyMAEKLNLDPLITHTLNLDKINEAVELMKTGK 367
Cdd:cd05289  250 ---RGVRAGFVFVEPDGEQLAELAE--LVEAGKLRPVVDRVFPLEDAAEAHERLESGH 302
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
11-367 3.72e-18

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: 84.56  E-value: 3.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGA-PFSIEEVEVAPPKAKEVRIKVVATGLCGTEmkvlgSKHLDLL----YPTILGHEGAGIVESIGEGVSTV 85
Cdd:cd08249    2 KAAVLTGPGGgLLVVVDVPVPKPGPDEVLVKVKAVALNPVD-----WKHQDYGfipsYPAILGCDFAGTVVEVGSGVTRF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  86 KPGDKVitlflpqCGECTSclnsegnfciqfkqsktqlmsdGTSRFTCKGksiyhfgntsTFCEYTVIKEISVAKIDAVA 165
Cdd:cd08249   77 KVGDRV-------AGFVHG----------------------GNPNDPRNG----------AFQEYVVADADLTAKIPDNI 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 166 PLEKVCLISCGFST---------GFGA-AINTAKVTPGSTCAVFGlGG--VGLSVVMGCKAAGaARIIGVdVNKEKFKKA 233
Cdd:cd08249  118 SFEEAATLPVGLVTaalalfqklGLPLpPPKPSPASKGKPVLIWG-GSssVGTLAIQLAKLAG-YKVITT-ASPKNFDLV 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 234 QELGATECLnpqDLKKP-IQEVLFDMTDAGIDFCFEAIGN---LDVLAAALASCNESYgvcvVVGVLPASVQLKISGQLF 309
Cdd:cd08249  195 KSLGADAVF---DYHDPdVVEDIRAATGGKLRYALDCISTpesAQLCAEALGRSGGGK----LVSLLPVPEETEPRKGVK 267
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156523966 310 FSGRSLkGSVFGGWKSRQHIPKLVADYMAEKLNLDPLITHTL-----NLDKINEAVELMKTGK 367
Cdd:cd08249  268 VKFVLG-YTVFGEIPEDREFGEVFWKYLPELLEEGKLKPHPVrvvegGLEGVQEGLDLLRKGK 329
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
10-366 4.49e-18

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 83.86  E-value: 4.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  10 CKAAILWKPGAP--FSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKP 87
Cdd:cd08271    1 MKAWVLPKPGAAlqLTLEEIEIPGPGAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTGWKV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  88 GDKVItlflpqcgectsclnsegnfciqFKQSktqLMSDGtsrftckgksiyhfgntsTFCEYTVIKEISVAKI-DAVAP 166
Cdd:cd08271   81 GDRVA-----------------------YHAS---LARGG------------------SFAEYTVVDARAVLPLpDSLSF 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 167 LEKVCLISCGFsTGFGAAINTAKVTPGSTcaVF---GLGGVGLSVVMGCKAAGaARIIgVDVNKEKFKKAQELGATECLN 243
Cdd:cd08271  117 EEAAALPCAGL-TAYQALFKKLRIEAGRT--ILitgGAGGVGSFAVQLAKRAG-LRVI-TTCSKRNFEYVKSLGADHVID 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 244 PQDlkKPIQEVLFDMTDA-GIDFCFEAIG--NLDVLAAALASCNEsygVCVVVGVLPASVQLKISGQLFFSGRSLKGSVF 320
Cdd:cd08271  192 YND--EDVCERIKEITGGrGVDAVLDTVGgeTAAALAPTLAFNGH---LVCIQGRPDASPDPPFTRALSVHEVALGAAHD 266
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 156523966 321 GGwkSRQHIPKLVadYMAEKL-------NLDPLITHTLNLDKINEAVELMKTG 366
Cdd:cd08271  267 HG--DPAAWQDLR--YAGEELlellaagKLEPLVIEVLPFEQLPEALRALKDR 315
PLN02702 PLN02702
L-idonate 5-dehydrogenase
24-366 9.00e-18

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 83.67  E-value: 9.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  24 IEEVEVAPPKAKEVRIKVVATGLCGTE---MKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQCG 100
Cdd:PLN02702  31 IQPFKLPPLGPHDVRVRMKAVGICGSDvhyLKTMRCADFVVKEPMVIGHECAGIIEEVGSEVKHLVVGDRVALEPGISCW 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 101 ECTSCLNSEGNFCIQFKQSKTQlmsdgtsrfTCKGKSIYHFGNTSTFCeYTVIKEISVAKIDAVAPLekvcliscgfSTG 180
Cdd:PLN02702 111 RCNLCKEGRYNLCPEMKFFATP---------PVHGSLANQVVHPADLC-FKLPENVSLEEGAMCEPL----------SVG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 181 FGAAiNTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECL----NPQDLKKPIQEVLF 256
Cdd:PLN02702 171 VHAC-RRANIGPETNVLVMGAGPIGLVTMLAARAFGAPRIVIVDVDDERLSVAKQLGADEIVlvstNIEDVESEVEEIQK 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 257 DMTdAGIDFCFEAIGNLDVLAAALASCNESYGVCvVVGVLPASVQLKISgqlffSGRSLKGSVFGGWKSRQHIPKLVADY 336
Cdd:PLN02702 250 AMG-GGIDVSFDCVGFNKTMSTALEATRAGGKVC-LVGMGHNEMTVPLT-----PAAAREVDVVGVFRYRNTWPLCLEFL 322
                        330       340       350
                 ....*....|....*....|....*....|..
gi 156523966 337 MAEKLNLDPLITH--TLNLDKINEAVELMKTG 366
Cdd:PLN02702 323 RSGKIDVKPLITHrfGFSQKEVEEAFETSARG 354
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
61-367 4.32e-17

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: 80.39  E-value: 4.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  61 LLYPTILGHEGAGIVESIGEGVSTVKPGDKVitlflpqcgectsclnsegnFCiqfkqsktqlmsdgtsrftckgksiyh 140
Cdd:cd08255   18 LPLPLPPGYSSVGRVVEVGSGVTGFKPGDRV--------------------FC--------------------------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 141 FGNTSTFceYTVIKEISVAKIDAVAPLEKVCLISCgfSTgfgaAINT---AKVTPGSTCAVFGLGGVGLSVVMGCKAAGA 217
Cdd:cd08255   51 FGPHAER--VVVPANLLVPLPDGLPPERAALTALA--AT----ALNGvrdAEPRLGERVAVVGLGLVGLLAAQLAKAAGA 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 218 ARIIGVDVNKEKFKKAQELGATECLNpqdlkkpiQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNEsYGVCVVVGVLP 297
Cdd:cd08255  123 REVVGVDPDAARRELAEALGPADPVA--------ADTADEIGGRGADVVIEASGSPSALETALRLLRD-RGRVVLVGWYG 193
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156523966 298 ASVqLKISGQLFFSGRSLKGSVFGG---------WKSRQHIpKLVADYMAEKLnLDPLITHTLNLDKINEAVELMKTGK 367
Cdd:cd08255  194 LKP-LLLGEEFHFKRLPIRSSQVYGigrydrprrWTEARNL-EEALDLLAEGR-LEALITHRVPFEDAPEAYRLLFEDP 269
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
11-367 1.82e-16

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 79.53  E-value: 1.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAP--FSIEEVEVAPPKAKEVRIKVVATGL--CGTEMKVLGSKHLDLLyPTILGHEGAGIVESIGEGVSTVK 86
Cdd:cd08272    2 KALVLESFGGPevFELREVPRPQPGPGQVLVRVHASGVnpLDTKIRRGGAAARPPL-PAILGCDVAGVVEAVGEGVTRFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  87 PGDKVItlflpqcgectsclnsegnFCIQfkqsktqlmsdgtsrftckgksiyHFGNTS-TFCEYTVIKEISVAK----- 160
Cdd:cd08272   81 VGDEVY-------------------GCAG------------------------GLGGLQgSLAEYAVVDARLLALkpanl 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 161 --IDAVA-PLekvcliscGFSTGFGAAINTAKVTPGSTCAVF-GLGGVGLSVVMGCKAAGaARIIGVdVNKEKFKKAQEL 236
Cdd:cd08272  118 smREAAAlPL--------VGITAWEGLVDRAAVQAGQTVLIHgGAGGVGHVAVQLAKAAG-ARVYAT-ASSEKAAFARSL 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 237 GATECLNPqdlKKPIQEVLFDMTD-AGIDFCFEAIG--NLD--VLAAALascnesYGVcVVVGVLPASVQLKisgQLFFS 311
Cdd:cd08272  188 GADPIIYY---RETVVEYVAEHTGgRGFDVVFDTVGgeTLDasFEAVAL------YGR-VVSILGGATHDLA---PLSFR 254
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156523966 312 GRSLKGsVF------GGWKSRQHIPKL-VADYMAEKLNLDPLI-THTLNLDKINEAVELMKTGK 367
Cdd:cd08272  255 NATYSG-VFtllpllTGEGRAHHGEILrEAARLVERGQLRPLLdPRTFPLEEAAAAHARLESGS 317
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
11-277 5.00e-16

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: 77.87  E-value: 5.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAP--FSIEEVEVAPPKAKEVRIKVVATGLcgtemkvlgsKHLDL-----LY----PTILGHEGAGIVESIG 79
Cdd:cd05286    1 KAVRIHKTGGPevLEYEDVPVPEPGPGEVLVRNTAIGV----------NFIDTyfrsgLYplplPFVLGVEGAGVVEAVG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  80 EGVSTVKPGDKVITlflpqcgectsclnsegnfciqfkqsktqlmsdgtsrftckgksiyhFGNTSTFCEYTVIkeisva 159
Cdd:cd05286   71 PGVTGFKVGDRVAY-----------------------------------------------AGPPGAYAEYRVV------ 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 160 kidavaPLEKVCLISCGFSTGFGAAI------------NTAKVTPGSTCAVFGL-GGVGLSVVMGCKAAGaARIIGVDVN 226
Cdd:cd05286   98 ------PASRLVKLPDGISDETAAALllqgltahyllrETYPVKPGDTVLVHAAaGGVGLLLTQWAKALG-ATVIGTVSS 170
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 227 KEKFKKAQELGATECLN--PQDLKKpiqEVLfDMTD-AGIDFCFEAIG------NLDVLA 277
Cdd:cd05286  171 EEKAELARAAGADHVINyrDEDFVE---RVR-EITGgRGVDVVYDGVGkdtfegSLDSLR 226
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
11-367 6.64e-16

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


Pssm-ID: 176180 [Multi-domain]  Cd Length: 323  Bit Score: 77.48  E-value: 6.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAP--FSIEEVEVAPPKAKEVRIKVVATGLCGTemkvlgskhlDLL-----YP------TILGHEGAGIVES 77
Cdd:cd05276    2 KAIVIKEPGGPevLELGEVPKPAPGPGEVLIRVAAAGVNRA----------DLLqrqglYPpppgasDILGLEVAGVVVA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  78 IGEGVSTVKPGDKVITLfLPQCGectsclnsegnfciqfkqsktqlmsdgtsrftckgksiyhfgntstFCEYTVIKEIS 157
Cdd:cd05276   72 VGPGVTGWKVGDRVCAL-LAGGG----------------------------------------------YAEYVVVPAGQ 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 158 VAKI-------DAVAPLEkvcliscGFSTGFGAAINTAKVTPGSTCAVF-GLGGVGLSVVMGCKAAGaARIIGVDVNKEK 229
Cdd:cd05276  105 LLPVpeglslvEAAALPE-------VFFTAWQNLFQLGGLKAGETVLIHgGASGVGTAAIQLAKALG-ARVIATAGSEEK 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 230 FKKAQELGATECLN--PQDLKkpiqEVLFDMTD-AGIDFCFEAIG------NLDVLAAalascnesYGVCVVVGVLP-AS 299
Cdd:cd05276  177 LEACRALGADVAINyrTEDFA----EEVKEATGgRGVDVILDMVGgdylarNLRALAP--------DGRLVLIGLLGgAK 244
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156523966 300 VQLKIsGQLFFSGRSLKGSVFggwKSR---------QHIPKLVADYMAEKLnLDPLITHTLNLDKINEAVELMKTGK 367
Cdd:cd05276  245 AELDL-APLLRKRLTLTGSTL---RSRsleekaalaAAFREHVWPLFASGR-IRPVIDKVFPLEEAAEAHRRMESNE 316
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
11-361 1.06e-14

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: 74.31  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPF-SIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLyPTILGHEGAGIVESIGEGVSTVKPGD 89
Cdd:cd08264    2 KALVFEKSGIENlKVEDVKDPKPGPGEVLIRVKMAGVNPVDYNVINAVKVKPM-PHIPGAEFAGVVEEVGDHVKGVKKGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  90 KVIT---LFlpqCGECTSCLNSEGNFciqfkqsktqlmsdgtsrftCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAP 166
Cdd:cd08264   81 RVVVynrVF---DGTCDMCLSGNEML--------------------CRNGGIIGVVSNGGYAEYIVVPEKNLFKIPDSIS 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 167 LEKVCLISCGFSTGFGAAiNTAKVTPGSTCAVFGLGG-VGLSVVMGCKAAGaARIIGVDvNKEKFKkaqELGATECLNPQ 245
Cdd:cd08264  138 DELAASLPVAALTAYHAL-KTAGLGPGETVVVFGASGnTGIFAVQLAKMMG-AEVIAVS-RKDWLK---EFGADEVVDYD 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 246 DLKKPIQEvLFDMTDAGIDfcfeAIGNldvlaaalASCNESYGVC------VVVGVLP-ASVQLKISgQLFFSGRSLKGS 318
Cdd:cd08264  212 EVEEKVKE-ITKMADVVIN----SLGS--------SFWDLSLSVLgrggrlVTFGTLTgGEVKLDLS-DLYSKQISIIGS 277
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 156523966 319 VFGgwkSRQHIPKLVAdyMAEKLNLDplITHTLNLDKINEAVE 361
Cdd:cd08264  278 TGG---TRKELLELVK--IAKDLKVK--VWKTFKLEEAKEALK 313
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
11-374 2.96e-14

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 72.76  E-value: 2.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAP--FSIEEVEVAPPKAKEVRIKVVATGLCGTEMkvlgSKHLDLLYP-----TILGHEGAGIVESIGEGVS 83
Cdd:PTZ00354   3 RAVTLKGFGGVdvLKIGESPKPAPKRNDVLIKVSAAGVNRADT----LQRQGKYPPppgssEILGLEVAGYVEDVGSDVK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  84 TVKPGDKVITLFlpqcgectsclnsegnfciqfkqsktqlmSDGtsrftckgksiyhfgntsTFCEYTVIKEISVAKIDA 163
Cdd:PTZ00354  79 RFKEGDRVMALL-----------------------------PGG------------------GYAEYAVAHKGHVMHIPQ 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 164 VAPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVF-GLGGVGLSVVMGCKAAGAARIIGVDvNKEKFKKAQELGATECL 242
Cdd:PTZ00354 112 GYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQSVLIHaGASGVGTAAAQLAEKYGAATIITTS-SEEKVDFCKKLAAIILI 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 243 NPQDLKKPIQEVLFDMTDAGIDFCFEAIG------NLDVLAAAlascnesyGVCVVVGVLP-ASVQLKISGQLFFSGRSL 315
Cdd:PTZ00354 191 RYPDEEGFAPKVKKLTGEKGVNLVLDCVGgsylseTAEVLAVD--------GKWIVYGFMGgAKVEKFNLLPLLRKRASI 262
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156523966 316 KGSVFggwKSR--QHIPKLVAD-------YMAEKLnLDPLITHTLNLDKINEAVELMKTGKCIRCILL 374
Cdd:PTZ00354 263 IFSTL---RSRsdEYKADLVASferevlpYMEEGE-IKPIVDRTYPLEEVAEAHTFLEQNKNIGKVVL 326
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
34-364 3.50e-14

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 72.91  E-value: 3.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  34 AKEVRIKVVATGLCGTEMKV----LGSKHldllYPTILGHEGAGIVESIGEGVSTVKPGDKV-ITLFLPQCGECTSCLNS 108
Cdd:PLN02514  34 PEDVVIKVIYCGICHTDLHQikndLGMSN----YPMVPGHEVVGEVVEVGSDVSKFTVGDIVgVGVIVGCCGECSPCKSD 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 109 EGNFCIQFKQSKTQLMSDGtsRFTCKGksiyhfgntstFCEYTVIKEISVAKI-DAVAPlEKVCLISCGFSTGFGAAINT 187
Cdd:PLN02514 110 LEQYCNKRIWSYNDVYTDG--KPTQGG-----------FASAMVVDQKFVVKIpEGMAP-EQAAPLLCAGVTVYSPLSHF 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 188 AKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDLKKpiqevlfdMTDAG--IDF 265
Cdd:PLN02514 176 GLKQSGLRGGILGLGGVGHMGVKIAKAMGHHVTVISSSDKKREEALEHLGADDYLVSSDAAE--------MQEAAdsLDY 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 266 CFEAIGNLDVLAAALaSCNESYGVCVVVGVLPASVQLkISGQLFFSGRSLKGSVFGGWKSRQHIpklvADYMAEKlNLDP 345
Cdd:PLN02514 248 IIDTVPVFHPLEPYL-SLLKLDGKLILMGVINTPLQF-VTPMLMLGRKVITGSFIGSMKETEEM----LEFCKEK-GLTS 320
                        330
                 ....*....|....*....
gi 156523966 346 LItHTLNLDKINEAVELMK 364
Cdd:PLN02514 321 MI-EVVKMDYVNTAFERLE 338
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
37-318 5.08e-13

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 69.33  E-value: 5.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  37 VRIKVVATGLCGTEM------KVLGS--KHldllyPTILGHEGAG-IVESIGEGVstvKPGDKVITLFLPQCGECTSCLN 107
Cdd:PRK09880  30 TLVQITRGGICGSDLhyyqegKVGNFviKA-----PMVLGHEVIGkIVHSDSSGL---KEGQTVAINPSKPCGHCKYCLS 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 108 SEGNFCiqfkqsktqlmsdGTSRFTckGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPlEKVCliscGFSTGFGAAINT 187
Cdd:PRK09880 102 HNENQC-------------TTMRFF--GSAMYFPHVDGGFTRYKVVDTAQCIPYPEKAD-EKVM----AFAEPLAVAIHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 188 AKVT---PGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDlkkpiQEVLFDMTDAG-I 263
Cdd:PRK09880 162 AHQAgdlQGKRVFVSGVGPIGCLIVAAVKTLGAAEIVCADVSPRSLSLAREMGADKLVNPQN-----DDLDHYKAEKGyF 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 156523966 264 DFCFEAIGNldvlAAALASCNE---SYGVCVVVGVLPASVQLKISgQLFFSGRSLKGS 318
Cdd:PRK09880 237 DVSFEVSGH----PSSINTCLEvtrAKGVMVQVGMGGAPPEFPMM-TLIVKEISLKGS 289
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
23-367 8.91e-13

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: 68.44  E-value: 8.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  23 SIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDL-LYPTILGHEGAGIVESIGEGVSTVKPGDKVITLflpqcge 101
Cdd:cd08273   16 KVVEADLPEPAAGEVVVKVEASGVSFADVQMRRGLYPDQpPLPFTPGYDLVGRVDALGSGVTGFEVGDRVAAL------- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 102 ctsclnsegnfciqfkqsktqLMSDGTSRFTCkgksiyhfgntstfceytvIKEISVAKI-DAVAPLEKVCLISCGfSTG 180
Cdd:cd08273   89 ---------------------TRVGGNAEYIN-------------------LDAKYLVPVpEGVDAAEAVCLVLNY-VTA 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 181 FGAAINTAKVTPGSTCAVFGL-GGVGLSVVMGCKAAGaARIIGVdVNKEKFKKAQELGATeCL--NPQDLkkpiqeVLFD 257
Cdd:cd08273  128 YQMLHRAAKVLTGQRVLIHGAsGGVGQALLELALLAG-AEVYGT-ASERNHAALRELGAT-PIdyRTKDW------LPAM 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 258 MTDAGIDFCFEAIG--NLDVLAAALAscneSYGVCVVVG-------------VLPASVQLKISGQLFFSGRSLKgsVFGG 322
Cdd:cd08273  199 LTPGGVDVVFDGVGgeSYEESYAALA----PGGTLVCYGgnssllqgrrslaALGSLLARLAKLKLLPTGRRAT--FYYV 272
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 156523966 323 WKSRQHIPKLVADYMAEKLNL------DPLITHTLNLDKINEAVELMKTGK 367
Cdd:cd08273  273 WRDRAEDPKLFRQDLTELLDLlakgkiRPKIAKRLPLSEVAEAHRLLESGK 323
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
20-361 1.91e-11

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 64.51  E-value: 1.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  20 APFSIEEVEVAPpkaKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKV-ITLFLPQ 98
Cdd:PLN02586  26 SPFHFSRRENGD---EDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGKNVKKFKEGDRVgVGVIVGS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  99 CGECTSCLNSEGNFCIQFKQSKTQLMSDGTSrftckgksiyhfgNTSTFCEYTVIKEISVAKIDAVAPLEKVCLISCGFS 178
Cdd:PLN02586 103 CKSCESCDQDLENYCPKMIFTYNSIGHDGTK-------------NYGGYSDMIVVDQHFVLRFPDNLPLDAGAPLLCAGI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 179 TGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAG-AARIIGVDVNKEKfKKAQELGATECL---NPQDLKKPIqev 254
Cdd:PLN02586 170 TVYSPMKYYGMTEPGKHLGVAGLGGLGHVAVKIGKAFGlKVTVISSSSNKED-EAINRLGADSFLvstDPEKMKAAI--- 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 255 lfdmtdAGIDFCFEAIGNLDVLAAALASCNESyGVCVVVGVLPASVQLKISGQLFfsGRSL-KGSVFGGWKSRQHIPKLV 333
Cdd:PLN02586 246 ------GTMDYIIDTVSAVHALGPLLGLLKVN-GKLITLGLPEKPLELPIFPLVL--GRKLvGGSDIGGIKETQEMLDFC 316
                        330       340
                 ....*....|....*....|....*...
gi 156523966 334 AdymaeKLNLDPLItHTLNLDKINEAVE 361
Cdd:PLN02586 317 A-----KHNITADI-ELIRMDEINTAME 338
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
11-367 1.24e-10

Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 61.86  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAP--FSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGvsTVKPG 88
Cdd:cd08243    2 KAIVIEQPGGPevLKLREIPIPEPKPGWVLIRVKAFGLNRSEIFTRQGHSPSVKFPRVLGIEAVGEVEEAPGG--TFTPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  89 DKVITLFlpqcgectsclnseGNFCIQFkqsktqlmsDGtsrftckgksiyhfgntsTFCEYTVIKEISVAKIDAVAPLE 168
Cdd:cd08243   80 QRVATAM--------------GGMGRTF---------DG------------------SYAEYTLVPNEQVYAIDSDLSWA 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 169 KVCLISCGFSTGFGAAINTAKVTPGSTCAVFG-LGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGATEC-LNPQD 246
Cdd:cd08243  119 ELAALPETYYTAWGSLFRSLGLQPGDTLLIRGgTSSVGLAALKLAKALG-ATVTATTRSPERAALLKELGADEVvIDDGA 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 247 LKKPIQEVlfdmtDAGIDFCFEAIGNLdVLAAALASCNEsYGVCVVVGVLPASVQLKISGQLFFSGRSLKGSVFGGWKSR 326
Cdd:cd08243  198 IAEQLRAA-----PGGFDKVLELVGTA-TLKDSLRHLRP-GGIVCMTGLLGGQWTLEDFNPMDDIPSGVNLTLTGSSSGD 270
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 156523966 327 ------QHIPKLVADYmaeklNLDPLITHTLNLDKINEAVELMKTGK 367
Cdd:cd08243  271 vpqtplQELFDFVAAG-----HLDIPPSKVFTFDEIVEAHAYMESNR 312
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
23-367 1.76e-10

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: 61.50  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  23 SIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTI-LGHEGAGIVESIGEGVSTVKPGDKVITLflpqcge 101
Cdd:cd08250   19 SIVDVPVPLPGPGEVLVKNRFVGINASDINFTAGRYDPGVKPPFdCGFEGVGEVVAVGEGVTDFKVGDAVATM------- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 102 ctsclnsegnfciqfkqsktqlmsdgtsrftckgksiyHFGntsTFCEYTVIKEISVAKIDAVAPlEKVCLISCGFStgf 181
Cdd:cd08250   92 --------------------------------------SFG---AFAEYQVVPARHAVPVPELKP-EVLPLLVSGLT--- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 182 gAAI---NTAKVTPGSTCAVF-GLGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGateCLNPQDLKK-PIQEVLF 256
Cdd:cd08250  127 -ASIaleEVGEMKSGETVLVTaAAGGTGQFAVQLAKLAG-CHVIGTCSSDEKAEFLKSLG---CDRPINYKTeDLGEVLK 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 257 DMTDAGIDFCFEAIGN--LDVLAAALAscneSYGVCVVVG---------VLPASVQLKISGQLFFSGRSLKGSVFGGWKS 325
Cdd:cd08250  202 KEYPKGVDVVYESVGGemFDTCVDNLA----LKGRLIVIGfisgyqsgtGPSPVKGATLPPKLLAKSASVRGFFLPHYAK 277
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 156523966 326 --RQHIPKLVADYMAEKLNL--DPliTHTLNLDKINEAVELMKTGK 367
Cdd:cd08250  278 liPQHLDRLLQLYQRGKLVCevDP--TRFRGLESVADAVDYLYSGK 321
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
11-113 3.29e-10

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


Pssm-ID: 176192 [Multi-domain]  Cd Length: 355  Bit Score: 60.70  E-value: 3.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVL---------GSKHLdllyptILGHEGAGIVESIGEG 81
Cdd:cd08230    2 KAIAVKPGKPGVRVVDIPEPEPTPGEVLVRTLEVGVCGTDREIVageygtappGEDFL------VLGHEALGVVEEVGDG 75
                         90       100       110
                 ....*....|....*....|....*....|..
gi 156523966  82 vSTVKPGDKVITLFLPQCGECTSCLNSEGNFC 113
Cdd:cd08230   76 -SGLSPGDLVVPTVRRPPGKCLNCRIGRPDFC 106
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
11-271 1.66e-09

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


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 58.75  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAP--FSIEEVEVAPPKAKEVRIKVVATGL----CgteMKVLGskhldlLY------PTILGHEGAGIVESI 78
Cdd:cd08275    1 RAVVLTGFGGLdkLKVEKEALPEPSSGEVRVRVEACGLnfadL---MARQG------LYdsapkpPFVPGFECAGTVEAV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  79 GEGVSTVKPGDKVITlfLPQCGECTSCLNSEGNFCIqfkqsktqLMSDGTsrftckgksiyhfgntsTFceytvikeisv 158
Cdd:cd08275   72 GEGVKDFKVGDRVMG--LTRFGGYAEVVNVPADQVF--------PLPDGM-----------------SF----------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 159 akIDAVAplekvclISCGFSTGFGAAINTAKVTPGSTCAVF-GLGGVGLSVVMGCKAAGAARIIGvDVNKEKFKKAQELG 237
Cdd:cd08275  114 --EEAAA-------FPVNYLTAYYALFELGNLRPGQSVLVHsAAGGVGLAAGQLCKTVPNVTVVG-TASASKHEALKENG 183
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 156523966 238 ATECL--NPQDLKKPIQEVlfdmTDAGIDFCFEAIG 271
Cdd:cd08275  184 VTHVIdyRTQDYVEEVKKI----SPEGVDIVLDALG 215
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
36-217 1.85e-09

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


Pssm-ID: 176179 [Multi-domain]  Cd Length: 293  Bit Score: 57.96  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  36 EVRIKVVATGLCGTE-MKVLGskhLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFlpqcgectsclnsegnfci 114
Cdd:cd05195    2 EVEVEVKAAGLNFRDvLVALG---LLPGDETPLGLECSGIVTRVGSGVTGLKVGDRVMGLA------------------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 115 qfkqsktqlmsdgtsrftckgksiyhfgnTSTFCEYTVIKEISVAKIDAVAPLEKVCLISCGFSTGFGAAINTAKVTPGS 194
Cdd:cd05195   60 -----------------------------PGAFATHVRVDARLVVKIPDSLSFEEAATLPVAYLTAYYALVDLARLQKGE 110
                        170       180
                 ....*....|....*....|....*.
gi 156523966 195 TcaVF---GLGGVGLSVVMGCKAAGA 217
Cdd:cd05195  111 S--VLihaAAGGVGQAAIQLAQHLGA 134
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
36-336 8.94e-09

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 56.57  E-value: 8.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  36 EVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKV-ITLFLPQCGECTSCLNSEGNFCI 114
Cdd:PLN02178  33 DVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVGKNVTKFKEGDRVgVGVIIGSCQSCESCNQDLENYCP 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 115 QFKQSKTQLMSDGTSrftckgksiyhfgNTSTFCEYTVIKEISVAKI------DAVAPLEKVCLISCGFSTGFGAAINTa 188
Cdd:PLN02178 113 KVVFTYNSRSSDGTR-------------NQGGYSDVIVVDHRFVLSIpdglpsDSGAPLLCAGITVYSPMKYYGMTKES- 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 189 kvtpGSTCAVFGLGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKA-QELGATECLNPQDLKKpiqevlfdMTDA--GIDF 265
Cdd:PLN02178 179 ----GKRLGVNGLGGLGHIAVKIGKAFG-LRVTVISRSSEKEREAiDRLGADSFLVTTDSQK--------MKEAvgTMDF 245
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156523966 266 CFEAIGNLDVLaAALASCNESYGVCVVVGVLPASVQLKISgQLFFSGRSLKGSVFGGWKSRQHIPKLVADY 336
Cdd:PLN02178 246 IIDTVSAEHAL-LPLFSLLKVSGKLVALGLPEKPLDLPIF-PLVLGRKMVGGSQIGGMKETQEMLEFCAKH 314
sorbose_phosphate_red cd08238
L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, ...
24-280 9.85e-09

L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, catalyzes the NADPH-dependent conversion of l-sorbose 1-phosphate to d-glucitol 6-phosphate in the metabolism of L-sorbose to (also converts d-fructose 1-phosphate to d-mannitol 6-phosphate). The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176200 [Multi-domain]  Cd Length: 410  Bit Score: 56.68  E-value: 9.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  24 IEEVEVAPPKAKEVRIKVVATGLCGTEMKV--LGSKHLDLL-----YPTILGHEGAGIVESIGEGVS-TVKPGDKVITlf 95
Cdd:cd08238   16 LEKFELPEIADDEILVRVISDSLCFSTWKLalQGSDHKKVPndlakEPVILGHEFAGTILKVGKKWQgKYKPGQRFVI-- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  96 lpqcgectsclnsegnfciqfkQSKTQLmSDGTSrftCKGKSIYHFGNTSTfceYTVIKEIsVAKIDAVAP--------- 166
Cdd:cd08238   94 ----------------------QPALIL-PDGPS---CPGYSYTYPGGLAT---YHIIPNE-VMEQDCLLIyegdgyaea 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 167 --LEKVCLISCGFSTGF----GAAINTAKVTPGSTCAVFGLGGvglsvVMGCKAA--------GAARIIGVDVNKEKFKK 232
Cdd:cd08238  144 slVEPLSCVIGAYTANYhlqpGEYRHRMGIKPGGNTAILGGAG-----PMGLMAIdyaihgpiGPSLLVVTDVNDERLAR 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 156523966 233 AQELGATEC---------LNPQDLKKPIQEVLFDMTDAGID--FCFEAIGNLDVLAAAL 280
Cdd:cd08238  219 AQRLFPPEAasrgiellyVNPATIDDLHATLMELTGGQGFDdvFVFVPVPELVEEADTL 277
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
28-369 2.47e-08

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: 54.74  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  28 EVAPPKAKEVRIKVVATGLC-GTEMKVLGskhldlLYPTIL------GHEGAGIVESIGEGVSTVKPGDKVITlflpqcg 100
Cdd:cd08251    1 EVAPPGPGEVRIQVRAFSLNfGDLLCVRG------LYPTMPpypftpGFEASGVVRAVGPHVTRLAVGDEVIA------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 101 ectsclnsegnfciqfkqSKTQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLekvcliscGFSTG 180
Cdd:cd08251   68 ------------------GTGESMGGHATLVTVPEDQVVRKPASLSFEEACALPVVFLTVIDAFARA--------GLAKG 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 181 FGAAINTAKvtpgstcavfglGGVGLSVVMGCKAAGAArIIGVDVNKEKFKKAQELGATECLNPqdLKKPIQEVLFDMTD 260
Cdd:cd08251  122 EHILIQTAT------------GGTGLMAVQLARLKGAE-IYATASSDDKLEYLKQLGVPHVINY--VEEDFEEEIMRLTG 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 261 A-GIDFCF-----EAIGN-LDVLAaalascnesygvcvvvgvlPASVQLKISGQLFFSGRSLKGSVFGGWKSRQHI---- 329
Cdd:cd08251  187 GrGVDVVIntlsgEAIQKgLNCLA-------------------PGGRYVEIAMTALKSAPSVDLSVLSNNQSFHSVdlrk 247
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 156523966 330 -----PKLVADYMAEKLN------LDPLITHTLNLDKINEAVELMKTGKCI 369
Cdd:cd08251  248 lllldPEFIADYQAEMVSlveegeLRPTVSRIFPFDDIGEAYRYLSDRENI 298
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
11-91 4.61e-08

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: 54.07  E-value: 4.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGA---PFSIEEVEVAPPKAK--EVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTV 85
Cdd:cd08252    2 KAIGFTQPLPitdPDSLIDIELPKPVPGgrDLLVRVEAVSVNPVDTKVRAGGAPVPGQPKILGWDASGVVEAVGSEVTLF 81

                 ....*.
gi 156523966  86 KPGDKV 91
Cdd:cd08252   82 KVGDEV 87
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
11-239 7.33e-08

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


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 53.45  E-value: 7.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAPFSIEEVEVAP---PKAKEVRIKVVATGLCGTEMKV-LGSKHLD-------------------LLYPTIL 67
Cdd:cd08274    2 RAVLLTGHGGLDKLVYRDDVPvptPAPGEVLIRVGACGVNNTDINTrEGWYSTEvdgatdstgageagwwggtLSFPRIQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  68 GHEGAGIVESIGEGVSTVKPGDKVITLFlpqcgeCTSCLNSEGNFCIQFKQSKTqlmsDGTsrftckgksiyhfgntstF 147
Cdd:cd08274   82 GADIVGRVVAVGEGVDTARIGERVLVDP------SIRDPPEDDPADIDYIGSER----DGG------------------F 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 148 CEYTVIKEISVAKIDAVAPLEKVCLISCGFSTGFGAaINTAKVTPGSTCAVFGL-GGVGLSVVMGCKAAGaARIIGVdVN 226
Cdd:cd08274  134 AEYTVVPAENAYPVNSPLSDVELATFPCSYSTAENM-LERAGVGAGETVLVTGAsGGVGSALVQLAKRRG-AIVIAV-AG 210
                        250
                 ....*....|...
gi 156523966 227 KEKFKKAQELGAT 239
Cdd:cd08274  211 AAKEEAVRALGAD 223
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
18-367 8.41e-08

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


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 53.57  E-value: 8.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  18 PGAPFSIEEVEVAPPKAKEVRIKVVATGL--------CGTEMKVLGS---KHLDLLYpTILGHEGAGIVESIGEGVSTVK 86
Cdd:cd08246   26 PAQAIQLEDVPVPELGPGEVLVAVMAAGVnynnvwaaLGEPVSTFAArqrRGRDEPY-HIGGSDASGIVWAVGEGVKNWK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  87 PGDKVITLflpqcgectsclnsegnfCIQF-KQSKTQLMSDGTsrfTCKGKSIYHF-GNTSTFCEYTVIKEISV-AKIDA 163
Cdd:cd08246  105 VGDEVVVH------------------CSVWdGNDPERAGGDPM---FDPSQRIWGYeTNYGSFAQFALVQATQLmPKPKH 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 164 VAPLEKVCLISCGfSTG----FGAAINTakVTPGSTCAVFG-LGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGA 238
Cdd:cd08246  164 LSWEEAAAYMLVG-ATAyrmlFGWNPNT--VKPGDNVLIWGaSGGLGSMAIQLARAAG-ANPVAVVSSEEKAEYCRALGA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 239 TECLN------------------PQDLK--KPIQEVLFDMTDAG--IDFCFEAIGNlDVLAAALASCNESyGVCVVVGVL 296
Cdd:cd08246  240 EGVINrrdfdhwgvlpdvnseayTAWTKeaRRFGKAIWDILGGRedPDIVFEHPGR-ATFPTSVFVCDRG-GMVVICAGT 317
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156523966 297 P---ASVQLKisgQLFFSGRSLKGSVFGGWKSRQHIPKLVADYMaeklnLDPLITHTLNLDKINEAVELMKTGK 367
Cdd:cd08246  318 TgynHTYDNR---YLWMRQKRIQGSHFANDREAAEANRLVMKGR-----IDPCLSKVFSLDETPDAHQLMHRNQ 383
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
33-368 5.40e-07

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: 51.11  E-value: 5.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  33 KAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTI-LGHEGAGIVESIGEGV-STVKPGDKVitlflpqCGectsclnseg 110
Cdd:cd08247   27 KDNEIVVKVHAAALNPVDLKLYNSYTFHFKVKEKgLGRDYSGVIVKVGSNVaSEWKVGDEV-------CG---------- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 111 nfciqfkqsktqlmsdgtsrftckgksIYH--FGNTSTFCEYTVI----KEISVAKIDAVAPLEKvcliSCGFSTGFGAA 184
Cdd:cd08247   90 ---------------------------IYPhpYGGQGTLSQYLLVdpkkDKKSITRKPENISLEE----AAAWPLVLGTA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 185 INT-----AKVTPGSTCAVFGlGG--VGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDLK--KPIQEVL 255
Cdd:cd08247  139 YQIledlgQKLGPDSKVLVLG-GStsVGRFAIQLAKNHYNIGTVVGTCSSRSAELNKKLGADHFIDYDAHSgvKLLKPVL 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 256 FDMTDAG-IDFCFEAIGNLDVLAAA---LASCNE-SYGVCVV--VGVLPASVQLKISGQLFFSGRSLKGSVfGGWKSRQH 328
Cdd:cd08247  218 ENVKGQGkFDLILDCVGGYDLFPHInsiLKPKSKnGHYVTIVgdYKANYKKDTFNSWDNPSANARKLFGSL-GLWSYNYQ 296
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 156523966 329 ---------IPKLVADYMAEKlNLDPLITHTLNLDKINEAVELMKTGKC 368
Cdd:cd08247  297 fflldpnadWIEKCAELIADG-KVKPPIDSVYPFEDYKEAFERLKSNRA 344
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
13-281 1.47e-06

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: 49.55  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  13 AILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVL-GSKHldllYPTILGHEGAGIVESIGEGVSTvkpGDKV 91
Cdd:cd08242    3 ALVLDGGLDLRVEDLPKPEPPPGEALVRVLLAGICNTDLEIYkGYYP----FPGVPGHEFVGIVEEGPEAELV---GKRV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  92 ITLFLPQCGECTSCLNSEGNFCIQfkqsKTQLmsdGTSRFtckgksiyhfgnTSTFCEYTVIKEISVAKI-DAVAPLEKV 170
Cdd:cd08242   76 VGEINIACGRCEYCRRGLYTHCPN----RTVL---GIVDR------------DGAFAEYLTLPLENLHVVpDLVPDEQAV 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 171 cliscgFSTGFGAAINT---AKVTPGSTCAVFGLGGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGATECLNPQDL 247
Cdd:cd08242  137 ------FAEPLAAALEIleqVPITPGDKVAVLGDGKLGLLIAQVLALTG-PDVVLVGRHSEKLALARRLGVETVLPDEAE 209
                        250       260       270
                 ....*....|....*....|....*....|....
gi 156523966 248 KKpiqevlfdmtDAGIDFCFEAIGNLDVLAAALA 281
Cdd:cd08242  210 SE----------GGGFDVVVEATGSPSGLELALR 233
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
18-374 1.90e-06

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


Pssm-ID: 176645 [Multi-domain]  Cd Length: 323  Bit Score: 49.20  E-value: 1.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  18 PGAPFSIEEVEVAPPKAK--EVRIKVVATGLcgtemkvlgsKHLDLLY-----------PTILGHEGAGIVESIGEGVST 84
Cdd:cd05282    8 EPLPLVLELVSLPIPPPGpgEVLVRMLAAPI----------NPSDLITisgaygsrpplPAVPGNEGVGVVVEVGSGVSG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  85 VKPGDKVITLFlpqcgectsclnSEGnfciqfkqsktqlmsdgtsrftckgksiyhfgntsTFCEYTVIKEISVAKIDAV 164
Cdd:cd05282   78 LLVGQRVLPLG------------GEG-----------------------------------TWQEYVVAPADDLIPVPDS 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 165 APLEKVCLIScgfstgfgaaIN--TA--------KVTPGSTCAVFGLG-GVGLSVVMGCKAAGAARIIGV--DVNKEKFK 231
Cdd:cd05282  111 ISDEQAAMLY----------INplTAwlmlteylKLPPGDWVIQNAANsAVGRMLIQLAKLLGFKTINVVrrDEQVEELK 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 232 kaqELGATE--CLNPQDLKKPIQEVL-FDMTDAGIDfcfeAIGNldVLAAALASCNESYGVCVVVGVLPASVQLKISGQL 308
Cdd:cd05282  181 ---ALGADEviDSSPEDLAQRVKEATgGAGARLALD----AVGG--ESATRLARSLRPGGTLVNYGLLSGEPVPFPRSVF 251
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156523966 309 FFSGRSLKGSVFGGWKSRQHIPKLVA--DYMAEKLN---LDPLITHTLNLDKINEAVEL----MKTGKcircILL 374
Cdd:cd05282  252 IFKDITVRGFWLRQWLHSATKEAKQEtfAEVIKLVEagvLTTPVGAKFPLEDFEEAVAAaeqpGRGGK----VLL 322
PRK10754 PRK10754
NADPH:quinone reductase;
19-92 3.73e-06

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 48.19  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  19 GAPFSIEEVEVAP--PKAKEVRIkvvatglcgtEMKVLGSKHLDL-----LYPTI-----LGHEGAGIVESIGEGVSTVK 86
Cdd:PRK10754  11 GGPEVLQAVEFTPadPAENEVQV----------ENKAIGINYIDTyirsgLYPPPslpsgLGTEAAGVVSKVGSGVKHIK 80

                 ....*.
gi 156523966  87 PGDKVI 92
Cdd:PRK10754  81 VGDRVV 86
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
64-367 4.92e-06

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: 47.98  E-value: 4.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  64 PTILGHEGAGIVESIGEGVSTVKPGDKVITLfLPQCGectsclnsegnfciqfkqsktqlmsdgtsrftckgksiyhfgn 143
Cdd:cd08290   64 PAVGGNEGVGEVVKVGSGVKSLKPGDWVIPL-RPGLG------------------------------------------- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 144 tsTFCEYTVIKEISVAKIDAVAPLEKVCLISCGFST------GFGAA------INTAkvtpgstcavfGLGGVGLSVVMG 211
Cdd:cd08290  100 --TWRTHAVVPADDLIKVPNDVDPEQAATLSVNPCTayrlleDFVKLqpgdwvIQNG-----------ANSAVGQAVIQL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 212 CKAAGaARIIGVDVNKEKFKKA----QELGATECLNPQDLKKP-IQEVLFDMTDAGIDFCFEAIGnlDVLAAALASCNES 286
Cdd:cd08290  167 AKLLG-IKTINVVRDRPDLEELkerlKALGADHVLTEEELRSLlATELLKSAPGGRPKLALNCVG--GKSATELARLLSP 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 287 YGVCVVVGVLpASVQLKIS-GQLFFSGRSLKGSVFGGWKSRQHIPKLVadymaeklnldplithtlnlDKINEAVELMKT 365
Cdd:cd08290  244 GGTMVTYGGM-SGQPVTVPtSLLIFKDITLRGFWLTRWLKRANPEEKE--------------------DMLEELAELIRE 302

                 ..
gi 156523966 366 GK 367
Cdd:cd08290  303 GK 304
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
39-95 7.60e-06

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 47.00  E-value: 7.60e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966    39 IKVVATGLCGTE-MKVLGskhldlLYP--TILGHEGAGIVESIGEGVSTVKPGDKVITLF 95
Cdd:smart00829   1 IEVRAAGLNFRDvLIALG------LYPgeAVLGGECAGVVTRVGPGVTGLAVGDRVMGLA 54
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
11-91 3.78e-05

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


Pssm-ID: 176252 [Multi-domain]  Cd Length: 324  Bit Score: 45.02  E-value: 3.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  11 KAAILWKPGAP---FSIEEVEVAPPKAKEVRIKVVATGL-CGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVK 86
Cdd:cd08292    2 RAAVHTQFGDPadvLEIGEVPKPTPGAGEVLVRTTLSPIhNHDLWTIRGTYGYKPELPAIGGSEAVGVVDAVGEGVKGLQ 81

                 ....*
gi 156523966  87 PGDKV 91
Cdd:cd08292   82 VGQRV 86
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
11-82 2.27e-04

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


Pssm-ID: 176251 [Multi-domain]  Cd Length: 324  Bit Score: 42.59  E-value: 2.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156523966  11 KAAILWKPGAP-----FSIEEVEVAPPKAKEVRIKVVATGLCGTE-MKVLGSKHLDLLYPTILGHEGAGIVESIGEGV 82
Cdd:cd08291    2 KALLLEEYGKPlevkeLSLPEPEVPEPGPGEVLIKVEAAPINPSDlGFLKGQYGSTKALPVPPGFEGSGTVVAAGGGP 79
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
25-238 7.11e-04

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


Pssm-ID: 176206 [Multi-domain]  Cd Length: 324  Bit Score: 41.20  E-value: 7.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966  25 EEVEVAPPKAKEVRIKVVATG--LCGTEMK--VLGSKHLDLLyPTILGHEGAGIVESIGEGVSTVKPGDKVITlflpqcg 100
Cdd:cd08244   18 EDVPDPVPGPGQVRIAVAAAGvhFVDTQLRsgWGPGPFPPEL-PYVPGGEVAGVVDAVGPGVDPAWLGRRVVA------- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523966 101 ectsclnsegnfciqfkqsktqlmsdgtsrftckgksiyHFGNTST-FCEYTVIKEISVAKI-DAVAPLEKVCLISCGfS 178
Cdd:cd08244   90 ---------------------------------------HTGRAGGgYAELAVADVDSLHPVpDGLDLEAAVAVVHDG-R 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156523966 179 TGFGaAINTAKVTPGSTCAVFGL-GGVGLSVVMGCKAAGaARIIGVDVNKEKFKKAQELGA 238
Cdd:cd08244  130 TALG-LLDLATLTPGDVVLVTAAaGGLGSLLVQLAKAAG-ATVVGAAGGPAKTALVRALGA 188
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
197-238 1.10e-03

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 40.49  E-value: 1.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 156523966 197 AVFGLGGVGLSVVMGCKAAGAA-RIIGVDVNKEKFKKAQELGA 238
Cdd:COG0287    5 AIIGLGLIGGSLALALKRAGLAhEVVGVDRSPETLERALELGV 47
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
33-91 1.94e-03

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: 39.90  E-value: 1.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156523966  33 KAKEVRIKVVATGL--------CG-------TEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKV 91
Cdd:cd08248   28 KPNQVLIKVHAASVnpidvlmrSGygrtllnKKRKPQSCKYSGIEFPLTLGRDCSGVVVDIGSGVKSFEIGDEV 101
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
175-238 5.74e-03

Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439939 [Multi-domain]  Cd Length: 270  Bit Score: 38.20  E-value: 5.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156523966 175 CGFST---GFGAAINTAKVTP-GSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEkfkKAQELGA 238
Cdd:COG0169   99 IGDNTdgiGFVRALREAGVDLaGKRVLVLGAGGAARAVAAALAEAGAAEITIVNRTPE---RAEALAA 163
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
194-229 8.65e-03

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 37.98  E-value: 8.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523966  194 STCAVFGLGGVGLsVVMGCKAAGAARIIGVDVNKEK 229
Cdd:TIGR03026   1 MKIAVIGLGYVGL-PLAALLADLGHDVTGVDIDQEK 35
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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