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Conserved domains on  [gi|6319500|ref|NP_009582|]
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enoyl-[acyl-carrier-protein] reductase [Saccharomyces cerevisiae S288C]

Protein Classification

MDR family NADPH-dependent oxidoreductase( domain architecture ID 10169684)

MDR (medium chain dehydrogenase/reductase) family NADPH-dependent oxidoreductase such as 2-enoyl thioester reductase (ETR), which catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis

CATH:  3.40.50.720|3.90.180.10
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0050661
PubMed:  19011751|12199705|8749365
SCOP:  4000090

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 21-345 1.52e-132

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: 382.72  E-value: 1.52e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   21 KSLIYSTHEveDCTKVLSVKNYTPKQDLSQS-IVLKTLAFPINPSDINQLQGVYPSRPEKTydystDEPAAIAGNEGVFE 99
Cdd:cd08290   2 KALVYTEHG--EPKEVLQLESYEIPPPGPPNeVLVKMLAAPINPADINQIQGVYPIKPPTT-----PEPPAVGGNEGVGE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  100 VVSLPSGSSkgDLKLGDRVIPLQANQGTWSNYRVFSSSsDLIKV-NDLDLFSAATVSVNGCTGFQLVSDYIDWNsnGNEW 178
Cdd:cd08290  75 VVKVGSGVK--SLKPGDWVIPLRPGLGTWRTHAVVPAD-DLIKVpNDVDPEQAATLSVNPCTAYRLLEDFVKLQ--PGDW 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  179 IIQNAGTSSVSKIVTQVAKAKGIKTLSVIRDRDNFDEVAKVLEDkYGATKVISESQNNDKtFAKEVLSKILGEnaRVRLA 258
Cdd:cd08290 150 VIQNGANSAVGQAVIQLAKLLGIKTINVVRDRPDLEELKERLKA-LGADHVLTEEELRSL-LATELLKSAPGG--RPKLA 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  259 LNSVGGKSSASIARKLENNALMLTYGGMSKQPVTLPTSLHIFKGLTSKGYWVTEKNK-KNPQSKIDTISDFIKMYNYGHI 337
Cdd:cd08290 226 LNCVGGKSATELARLLSPGGTMVTYGGMSGQPVTVPTSLLIFKDITLRGFWLTRWLKrANPEEKEDMLEELAELIREGKL 305


                ....*...
gi 6319500  338 ISPRDEIE 345
Cdd:cd08290 306 KAPPVEKV 313
 
Name Accession Description Interval E-value
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 21-345 1.52e-132

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: 382.72  E-value: 1.52e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   21 KSLIYSTHEveDCTKVLSVKNYTPKQDLSQS-IVLKTLAFPINPSDINQLQGVYPSRPEKTydystDEPAAIAGNEGVFE 99
Cdd:cd08290   2 KALVYTEHG--EPKEVLQLESYEIPPPGPPNeVLVKMLAAPINPADINQIQGVYPIKPPTT-----PEPPAVGGNEGVGE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  100 VVSLPSGSSkgDLKLGDRVIPLQANQGTWSNYRVFSSSsDLIKV-NDLDLFSAATVSVNGCTGFQLVSDYIDWNsnGNEW 178
Cdd:cd08290  75 VVKVGSGVK--SLKPGDWVIPLRPGLGTWRTHAVVPAD-DLIKVpNDVDPEQAATLSVNPCTAYRLLEDFVKLQ--PGDW 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  179 IIQNAGTSSVSKIVTQVAKAKGIKTLSVIRDRDNFDEVAKVLEDkYGATKVISESQNNDKtFAKEVLSKILGEnaRVRLA 258
Cdd:cd08290 150 VIQNGANSAVGQAVIQLAKLLGIKTINVVRDRPDLEELKERLKA-LGADHVLTEEELRSL-LATELLKSAPGG--RPKLA 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  259 LNSVGGKSSASIARKLENNALMLTYGGMSKQPVTLPTSLHIFKGLTSKGYWVTEKNK-KNPQSKIDTISDFIKMYNYGHI 337
Cdd:cd08290 226 LNCVGGKSATELARLLSPGGTMVTYGGMSGQPVTVPTSLLIFKDITLRGFWLTRWLKrANPEEKEDMLEELAELIREGKL 305


                ....*...
gi 6319500  338 ISPRDEIE 345
Cdd:cd08290 306 KAPPVEKV 313
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 52-310 4.96e-26

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: 106.39  E-value: 4.96e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   52 IVLKTLAFPINPSDINQLQGVYPSRPEktydystdEPAaIAGNEGVFEVVSLPSGSSkgDLKLGDRVIPLqANQGTWSNY 131
Cdd:COG0604  30 VLVRVKAAGVNPADLLIRRGLYPLPPG--------LPF-IPGSDAAGVVVAVGEGVT--GFKVGDRVAGL-GRGGGYAEY 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  132 RVFSSSSdLIKVND-LDLFSAATVSVNGCTGFQLVSDyidwnsNGN----EWIIQNAGTSSVSKIVTQVAKAKGIKTLSV 206
Cdd:COG0604  98 VVVPADQ-LVPLPDgLSFEEAAALPLAGLTAWQALFD------RGRlkpgETVLVHGAAGGVGSAAVQLAKALGARVIAT 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  207 IRDRDNFDEVAKvledkYGATKVISESQNNdktFAKEVLSkiLGENARVRLALNSVGGKSSASIARKLENNALMLTYGGM 286
Cdd:COG0604 171 ASSPEKAELLRA-----LGADHVIDYREED---FAERVRA--LTGGRGVDVVLDTVGGDTLARSLRALAPGGRLVSIGAA 240

                       250       260
                ....*....|....*....|....
gi 6319500  287 SKQPVTLPTSLHIFKGLTSKGYWV 310
Cdd:COG0604 241 SGAPPPLDLAPLLLKGLTLTGFTL 264
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 44-287 1.99e-04

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 43.10  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500    44 PKQDLSQSIVL-KTLAFPINPSDINQLQGVYPSRPEKTydystdepaAIAGNE--GVFEVVslpsGSSKGDLKLGDRVIP 120
Cdd:PTZ00354  22 PKPAPKRNDVLiKVSAAGVNRADTLQRQGKYPPPPGSS---------EILGLEvaGYVEDV----GSDVKRFKEGDRVMA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   121 LQANqGTWSNYRVFSSSSdLIKVND-LDLFSAATVSVNGCTGFQLVSDYIDWNSNGNEWIiqNAGTSSVSKIVTQVAK-- 197
Cdd:PTZ00354  89 LLPG-GGYAEYAVAHKGH-VMHIPQgYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQSVLI--HAGASGVGTAAAQLAEky 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   198 --AKGIKTLSvirdrdnfDEVAKVLEdKYGATKVIsesqnNDKT---FAKEVLsKILGENArVRLALNSVGGKSSASIAR 272
Cdd:PTZ00354 165 gaATIITTSS--------EEKVDFCK-KLAAIILI-----RYPDeegFAPKVK-KLTGEKG-VNLVLDCVGGSYLSETAE 228

                        250
                 ....*....|....*
gi 6319500   273 KLENNALMLTYGGMS 287
Cdd:PTZ00354 229 VLAVDGKWIVYGFMG 243
 
Name Accession Description Interval E-value
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 21-345 1.52e-132

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: 382.72  E-value: 1.52e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   21 KSLIYSTHEveDCTKVLSVKNYTPKQDLSQS-IVLKTLAFPINPSDINQLQGVYPSRPEKTydystDEPAAIAGNEGVFE 99
Cdd:cd08290   2 KALVYTEHG--EPKEVLQLESYEIPPPGPPNeVLVKMLAAPINPADINQIQGVYPIKPPTT-----PEPPAVGGNEGVGE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  100 VVSLPSGSSkgDLKLGDRVIPLQANQGTWSNYRVFSSSsDLIKV-NDLDLFSAATVSVNGCTGFQLVSDYIDWNsnGNEW 178
Cdd:cd08290  75 VVKVGSGVK--SLKPGDWVIPLRPGLGTWRTHAVVPAD-DLIKVpNDVDPEQAATLSVNPCTAYRLLEDFVKLQ--PGDW 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  179 IIQNAGTSSVSKIVTQVAKAKGIKTLSVIRDRDNFDEVAKVLEDkYGATKVISESQNNDKtFAKEVLSKILGEnaRVRLA 258
Cdd:cd08290 150 VIQNGANSAVGQAVIQLAKLLGIKTINVVRDRPDLEELKERLKA-LGADHVLTEEELRSL-LATELLKSAPGG--RPKLA 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  259 LNSVGGKSSASIARKLENNALMLTYGGMSKQPVTLPTSLHIFKGLTSKGYWVTEKNK-KNPQSKIDTISDFIKMYNYGHI 337
Cdd:cd08290 226 LNCVGGKSATELARLLSPGGTMVTYGGMSGQPVTVPTSLLIFKDITLRGFWLTRWLKrANPEEKEDMLEELAELIREGKL 305


                ....*...
gi 6319500  338 ISPRDEIE 345
Cdd:cd08290 306 KAPPVEKV 313
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 52-332 8.51e-62

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: 201.35  E-value: 8.51e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   52 IVLKTLAFPINPSDINQLQGVYPSRPEKtydystdepAAIAGNEGVFEVVSLPSGSSKgdLKLGDRVIPLQAnQGTWSNY 131
Cdd:cd05282  29 VLVRMLAAPINPSDLITISGAYGSRPPL---------PAVPGNEGVGVVVEVGSGVSG--LLVGQRVLPLGG-EGTWQEY 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  132 RVfSSSSDLIKV-NDLDLFSAATVSVNGCTGFQLVSDYIdwNSNGNEWIIQNAGTSSVSKIVTQVAKAKGIKTLSVIRDR 210
Cdd:cd05282  97 VV-APADDLIPVpDSISDEQAAMLYINPLTAWLMLTEYL--KLPPGDWVIQNAANSAVGRMLIQLAKLLGFKTINVVRRD 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  211 DNFDEVAKvledkYGATKVISESQNNdktFAKEVLSKILGenARVRLALNSVGGKSSASIARKLENNALMLTYGGMSKQP 290
Cdd:cd05282 174 EQVEELKA-----LGADEVIDSSPED---LAQRVKEATGG--AGARLALDAVGGESATRLARSLRPGGTLVNYGLLSGEP 243

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 6319500  291 VTLPTSLHIFKGLTSKGYWVTEKNKKNPQSKI-DTISDFIKMY 332
Cdd:cd05282 244 VPFPRSVFIFKDITVRGFWLRQWLHSATKEAKqETFAEVIKLV 286
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
 21-316 5.69e-33

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: 125.52  E-value: 5.69e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   21 KSLIYSTHEveDCTKVLSVKNYTPKQDLSQSIVLKTLAFPINPSDINQLQGVYPSRPEKtydystdepAAIAGNEGVFEV 100
Cdd:cd08292   2 RAAVHTQFG--DPADVLEIGEVPKPTPGAGEVLVRTTLSPIHNHDLWTIRGTYGYKPEL---------PAIGGSEAVGVV 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  101 VSLPSGSSkgDLKLGDRVIpLQANQGTWSNYRVFSSSSdLIKVND-LDLFSAATVSVNGCTGFQLVSDYidwNSNGNEWI 179
Cdd:cd08292  71 DAVGEGVK--GLQVGQRVA-VAPVHGTWAEYFVAPADG-LVPLPDgISDEVAAQLIAMPLSALMLLDFL---GVKPGQWL 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  180 IQNAGTSSVSKIVTQVAKAKGIKTLSVIRDRDNFDEVAKVledkyGATKVISESQNNDKTFAKEVLSkilGENARVrlAL 259
Cdd:cd08292 144 IQNAAGGAVGKLVAMLAAARGINVINLVRRDAGVAELRAL-----GIGPVVSTEQPGWQDKVREAAG---GAPISV--AL 213

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6319500  260 NSVGGKSSASIARKLENNALMLTYGGMSKQPVTLPTSLHIFKGLTSKGYWVTEKNKK 316
Cdd:cd08292 214 DSVGGKLAGELLSLLGEGGTLVSFGSMSGEPMQISSGDLIFKQATVRGFWGGRWSQE 270
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 52-310 4.96e-26

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: 106.39  E-value: 4.96e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   52 IVLKTLAFPINPSDINQLQGVYPSRPEktydystdEPAaIAGNEGVFEVVSLPSGSSkgDLKLGDRVIPLqANQGTWSNY 131
Cdd:COG0604  30 VLVRVKAAGVNPADLLIRRGLYPLPPG--------LPF-IPGSDAAGVVVAVGEGVT--GFKVGDRVAGL-GRGGGYAEY 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  132 RVFSSSSdLIKVND-LDLFSAATVSVNGCTGFQLVSDyidwnsNGN----EWIIQNAGTSSVSKIVTQVAKAKGIKTLSV 206
Cdd:COG0604  98 VVVPADQ-LVPLPDgLSFEEAAALPLAGLTAWQALFD------RGRlkpgETVLVHGAAGGVGSAAVQLAKALGARVIAT 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  207 IRDRDNFDEVAKvledkYGATKVISESQNNdktFAKEVLSkiLGENARVRLALNSVGGKSSASIARKLENNALMLTYGGM 286
Cdd:COG0604 171 ASSPEKAELLRA-----LGADHVIDYREED---FAERVRA--LTGGRGVDVVLDTVGGDTLARSLRALAPGGRLVSIGAA 240

                       250       260
                ....*....|....*....|....
gi 6319500  287 SKQPVTLPTSLHIFKGLTSKGYWV 310
Cdd:COG0604 241 SGAPPPLDLAPLLLKGLTLTGFTL 264
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
 52-312 8.07e-24

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: 100.37  E-value: 8.07e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   52 IVLKTLAFPINPSDINQLQGVYPSRPEKtydystdepAAIAGNEGVFEVVSLpSGSSKGDLKLGDRVIPLQANQGTWSNY 131
Cdd:cd08291  33 VLIKVEAAPINPSDLGFLKGQYGSTKAL---------PVPPGFEGSGTVVAA-GGGPLAQSLIGKRVAFLAGSYGTYAEY 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  132 RVFSSSSDLIKVNDLDLFSAATVSVNGCTGFQLVSDYIdwnSNGNEWIIQNAGTSSVSKIVTQVAKAKGIKTLSVIRdRD 211
Cdd:cd08291 103 AVADAQQCLPLPDGVSFEQGASSFVNPLTALGMLETAR---EEGAKAVVHTAAASALGRMLVRLCKADGIKVINIVR-RK 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  212 NFDEVAKvledKYGATKVISESqnnDKTFAKEVLSKILGENARVrlALNSVGGKSSASIARKLENNALMLTYGGMSKQPV 291
Cdd:cd08291 179 EQVDLLK----KIGAEYVLNSS---DPDFLEDLKELIAKLNATI--FFDAVGGGLTGQILLAMPYGSTLYVYGYLSGKLD 249

                       250       260
                ....*....|....*....|...
gi 6319500  292 TlPTSLH--IFKGLTSKGYWVTE 312
Cdd:cd08291 250 E-PIDPVdlIFKNKSIEGFWLTT 271
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 52-310 5.04e-16

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: 77.36  E-value: 5.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   52 IVLKTLAFPINPSDINQLQGVYPSRPektydystdEPAAIAGNEGVFEVVSLpsGSSKGDLKLGDRVIPLQA-------- 123
Cdd:cd05188   2 VLVRVEAAGLCGTDLHIRRGGYPPPP---------KLPLILGHEGAGVVVEV--GPGVTGVKVGDRVVVLPNlgcgtcel 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  124 --------------NQGTWSNYrVFSSSSDLIKVND-LDLFSAATVSVNGCTGFQLVsdyidwNSNG----NEWI-IQNA 183
Cdd:cd05188  71 crelcpgggilgegLDGGFAEY-VVVPADNLVPLPDgLSLEEAALLPEPLATAYHAL------RRAGvlkpGDTVlVLGA 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  184 GTssVSKIVTQVAKAKGIKTLSVIRDRDNFdEVAKvledKYGATKVISESQNNDKTFAKEVlskilgENARVRLALNSVG 263
Cdd:cd05188 144 GG--VGLLAAQLAKAAGARVIVTDRSDEKL-ELAK----ELGADHVIDYKEEDLEEELRLT------GGGGADVVIDAVG 210

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 6319500  264 GKSSASIA-RKLENNALMLTYGGMSKQPVTLPTSLHIFKGLTSKGYWV 310
Cdd:cd05188 211 GPETLAQAlRLLRPGGRIVVVGGTSGGPPLDDLRRLLFKELTIIGSTG 258
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 52-312 2.86e-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: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 69.94  E-value: 2.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   52 IVLKTLAFPINPSDINQLQGVYPSRPEktydystdePAAIAGNEGVFEVVSLpsGSSKGDLKLGDRV-IPLQANQGTWSN 130
Cdd:cd08268  30 VLIRVEAIGLNRADAMFRRGAYIEPPP---------LPARLGYEAAGVVEAV--GAGVTGFAVGDRVsVIPAADLGQYGT 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  131 Y--RVFSSSSDLIKVND-LDLFSAATVSVNGCTGFQLVSDyidwnsNGN----EWIIQNAGTSSVSKIVTQVAKAKGIKT 203
Cdd:cd08268  99 YaeYALVPAAAVVKLPDgLSFVEAAALWMQYLTAYGALVE------LAGlrpgDSVLITAASSSVGLAAIQIANAAGATV 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  204 LSVIRDRDNFDEvakvLEDkYGATKVISeSQNNDktFAKEVLSKILGENARVrlALNSVGGKSSASIARKLENNALMLTY 283
Cdd:cd08268 173 IATTRTSEKRDA----LLA-LGAAHVIV-TDEED--LVAEVLRITGGKGVDV--VFDPVGGPQFAKLADALAPGGTLVVY 242

                       250       260
                ....*....|....*....|....*....
gi 6319500  284 GGMSKQPVTLPTSLHIFKGLTSKGYWVTE 312
Cdd:cd08268 243 GALSGEPTPFPLKAALKKSLTFRGYSLDE 271
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 52-271 2.26e-09

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: 58.36  E-value: 2.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   52 IVLKTLAFPINPSD-INQLQGVYPSRPektydystdepaAIAGNEGVFEVVSLPSGSSKgdLKLGDRVI-------PLQA 123
Cdd:cd08249  29 VLVKVKAVALNPVDwKHQDYGFIPSYP------------AILGCDFAGTVVEVGSGVTR--FKVGDRVAgfvhggnPNDP 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  124 NQGTWSNYRVFSSSSdLIKV-NDLDLFSAATVSVNGCTGFQL--VSDYIDWN------SNGNEWIIQNAGTSSVSKIVTQ 194
Cdd:cd08249  95 RNGAFQEYVVADADL-TAKIpDNISFEEAATLPVGLVTAALAlfQKLGLPLPppkpspASKGKPVLIWGGSSSVGTLAIQ 173

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6319500  195 VAKAKGIKTLSVIrDRDNFDEVaKvledKYGATKVISesqNNDKTFAKEVLSKilgENARVRLALNSVGGKSSASIA 271
Cdd:cd08249 174 LAKLAGYKVITTA-SPKNFDLV-K----SLGADAVFD---YHDPDVVEDIRAA---TGGKLRYALDCISTPESAQLC 238
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 44-287 1.99e-04

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 43.10  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500    44 PKQDLSQSIVL-KTLAFPINPSDINQLQGVYPSRPEKTydystdepaAIAGNE--GVFEVVslpsGSSKGDLKLGDRVIP 120
Cdd:PTZ00354  22 PKPAPKRNDVLiKVSAAGVNRADTLQRQGKYPPPPGSS---------EILGLEvaGYVEDV----GSDVKRFKEGDRVMA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   121 LQANqGTWSNYRVFSSSSdLIKVND-LDLFSAATVSVNGCTGFQLVSDYIDWNSNGNEWIiqNAGTSSVSKIVTQVAK-- 197
Cdd:PTZ00354  89 LLPG-GGYAEYAVAHKGH-VMHIPQgYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQSVLI--HAGASGVGTAAAQLAEky 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   198 --AKGIKTLSvirdrdnfDEVAKVLEdKYGATKVIsesqnNDKT---FAKEVLsKILGENArVRLALNSVGGKSSASIAR 272
Cdd:PTZ00354 165 gaATIITTSS--------EEKVDFCK-KLAAIILI-----RYPDeegFAPKVK-KLTGEKG-VNLVLDCVGGSYLSETAE 228

                        250
                 ....*....|....*
gi 6319500   273 KLENNALMLTYGGMS 287
Cdd:PTZ00354 229 VLAVDGKWIVYGFMG 243
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 43-265 3.37e-03

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: 38.96  E-value: 3.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   43 TPKQDLSQsIVLKTLAFPINPSDINQLQGVYPSRPEktydySTD----EpaaIAGnegvfEVVSLpsGSSKGDLKLGDRV 118
Cdd:cd05276  22 KPAPGPGE-VLIRVAAAGVNRADLLQRQGLYPPPPG-----ASDilglE---VAG-----VVVAV--GPGVTGWKVGDRV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500  119 IPLqANQGTWSNYrVFSSSSDLIKV-NDLDLFSAATVSVNGCTGFQLVSDyidwnsNGN----EWIIQNAGTSSVSKIVT 193
Cdd:cd05276  86 CAL-LAGGGYAEY-VVVPAGQLLPVpEGLSLVEAAALPEVFFTAWQNLFQ------LGGlkagETVLIHGGASGVGTAAI 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319500  194 QVAKAKGIKTLSVIRDrdnfDEVAKVLEdKYGATKVIsesqnNDKT--FAKEVLSKILGEnaRVRLALNSVGGK 265
Cdd:cd05276 158 QLAKALGARVIATAGS----EEKLEACR-ALGADVAI-----NYRTedFAEEVKEATGGR--GVDVILDMVGGD 219
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 52-165 6.03e-03

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


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 38.40  E-value: 6.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319500   52 IVLKTLAFPINPSDINQLQGVYPsrpektydystDEPAA--IAGNEGVFEVVSLPSGSSKgdLKLGDRVIPLqANQGTWS 129
Cdd:cd08273  30 VVVKVEASGVSFADVQMRRGLYP-----------DQPPLpfTPGYDLVGRVDALGSGVTG--FEVGDRVAAL-TRVGGNA 95

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 6319500  130 NYRVFSSSsDLIKVND-LDLFSAATVSVNGCTGFQLV 165
Cdd:cd08273  96 EYINLDAK-YLVPVPEgVDAAEAVCLVLNYVTAYQML 131
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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