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Conserved domains on  [gi|767904541|ref|XP_011539843|]
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enoyl-[acyl-carrier-protein] reductase, mitochondrial isoform X3 [Homo sapiens]

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

EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0050661
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 ...
44-327 1.65e-144

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: 412.38  E-value: 1.65e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  44 RALVYGHHGDPAKVVEgitrelfqrfpwiflqlitavissastvLKNLELAAVRGSD-VRVKMLAAPINPSDINMIQGNY 122
Cdd:cd08290    2 KALVYTEHGEPKEVLQ----------------------------LESYEIPPPGPPNeVLVKMLAAPINPADINQIQGVY 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 123 GFLP----ELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCT 198
Cdd:cd08290   54 PIKPpttpEPPAVGGNEGVGEVVKVGSGVKSLKPGDWVIPLRPGLGTWRTHAVVPADDLIKVPNDVDPEQAATLSVNPCT 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 199 AYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLGAEHVITEEELRRPEMKNF 278
Cdd:cd08290  134 AYRLLEDFVKLQPGDWVIQNGANSAVGQAVIQLAKLLGIKTINVVRDRPDLEELKERLKALGADHVLTEEELRSLLATEL 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767904541 279 FKDMP--QPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSP 327
Cdd:cd08290  214 LKSAPggRPKLALNCVGGKSATELARLLSPGGTMVTYGGMSGQPVTVPTSL 264
 
Name Accession Description Interval E-value
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
44-327 1.65e-144

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: 412.38  E-value: 1.65e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  44 RALVYGHHGDPAKVVEgitrelfqrfpwiflqlitavissastvLKNLELAAVRGSD-VRVKMLAAPINPSDINMIQGNY 122
Cdd:cd08290    2 KALVYTEHGEPKEVLQ----------------------------LESYEIPPPGPPNeVLVKMLAAPINPADINQIQGVY 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 123 GFLP----ELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCT 198
Cdd:cd08290   54 PIKPpttpEPPAVGGNEGVGEVVKVGSGVKSLKPGDWVIPLRPGLGTWRTHAVVPADDLIKVPNDVDPEQAATLSVNPCT 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 199 AYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLGAEHVITEEELRRPEMKNF 278
Cdd:cd08290  134 AYRLLEDFVKLQPGDWVIQNGANSAVGQAVIQLAKLLGIKTINVVRDRPDLEELKERLKALGADHVLTEEELRSLLATEL 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767904541 279 FKDMP--QPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSP 327
Cdd:cd08290  214 LKSAPggRPKLALNCVGGKSATELARLLSPGGTMVTYGGMSGQPVTVPTSL 264
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
87-328 4.13e-59

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: 193.83  E-value: 4.13e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpANAGLGTW 166
Cdd:COG0604   16 ELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPLPPGLPFIPGSDAAGVVVAVGEGVTGFKVGDRVA-GLGRGGGY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 167 RTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRdR 246
Cdd:COG0604   95 AEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKPGETVLVHGAAGGVGSAAVQLAKALGARVIATAS-S 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 247 PDiqKLsDRLKSLGAEHVI--TEEELRRPEMKNFFKDmpQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVAS 324
Cdd:COG0604  174 PE--KA-ELLRALGADHVIdyREEDFAERVRALTGGR--GVDVVLDTVGGDTLARSLRALAPGGRLVSIGAASGAPPPLD 248

                 ....
gi 767904541 325 VSPA 328
Cdd:COG0604  249 LAPL 252
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
103-236 2.60e-24

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 100.54  E-value: 2.60e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541   103 VKMLAAPINPSDINMIQGNYGFLPELpavgGNEGVAQVVAVGSNVTGLKPGDWVIpanaGL--GTWRTEAVFSEEALIQV 180
Cdd:smart00829   1 IEVRAAGLNFRDVLIALGLYPGEAVL----GGECAGVVTRVGPGVTGLAVGDRVM----GLapGAFATRVVTDARLVVPI 72
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767904541   181 PSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQAVIQIAAALG 236
Cdd:smart00829  73 PDGWSFEEAATVPVVFLTAYYALVDLARLRPGESVlIHAAA-GGVGQAAIQLARHLG 128
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
88-316 1.45e-23

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 99.72  E-value: 1.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  88 LKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGlGTWR 167
Cdd:PTZ00354  18 IGESPKPAPKRNDVLIKVSAAGVNRADTLQRQGKYPPPPGSSEILGLEVAGYVEDVGSDVKRFKEGDRVMALLPG-GGYA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 168 TEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRP 247
Cdd:PTZ00354  97 EYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQSVLIHAGASGVGTAAAQLAEKYGAATIITTSSEE 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767904541 248 DIQKlsdrLKSLGAEHVIteeelRRPEMKNF---FKDMPQPR---LALNCVGGKSSTELLRQLARGGTMVTYGGM 316
Cdd:PTZ00354 177 KVDF----CKKLAAIILI-----RYPDEEGFapkVKKLTGEKgvnLVLDCVGGSYLSETAEVLAVDGKWIVYGFM 242
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
223-327 1.09e-11

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 61.47  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  223 GVGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSLGAEHVITEEELRRPE-MKNFFKDMpQPRLALNCVG-GKSSTEL 300
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSE---EKL-ELAKELGADHVINPKETDLVEeIKELTGGK-GVDVVFDCVGsPATLEQA 75
                          90       100
                  ....*....|....*....|....*..
gi 767904541  301 LRQLARGGTMVTYgGMAKQPVVASVSP 327
Cdd:pfam00107  76 LKLLRPGGRVVVV-GLPGGPLPLPLAP 101
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
174-317 6.56e-06

leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase.


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 47.30  E-value: 6.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  174 EEALIQVPSDIPLQSA-ATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIqkl 252
Cdd:TIGR02825 100 EKLLTEWPDTLPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKV--- 176
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767904541  253 sDRLKSLGAEHVIT-------EEELRR--PEMKNFFKDMpqprlalncVGGKSSTELLRQLARGGTMVTYGGMA 317
Cdd:TIGR02825 177 -AYLKKLGFDVAFNyktvkslEETLKKasPDGYDCYFDN---------VGGEFSNTVIGQMKKFGRIAICGAIS 240
 
Name Accession Description Interval E-value
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
44-327 1.65e-144

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: 412.38  E-value: 1.65e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  44 RALVYGHHGDPAKVVEgitrelfqrfpwiflqlitavissastvLKNLELAAVRGSD-VRVKMLAAPINPSDINMIQGNY 122
Cdd:cd08290    2 KALVYTEHGEPKEVLQ----------------------------LESYEIPPPGPPNeVLVKMLAAPINPADINQIQGVY 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 123 GFLP----ELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCT 198
Cdd:cd08290   54 PIKPpttpEPPAVGGNEGVGEVVKVGSGVKSLKPGDWVIPLRPGLGTWRTHAVVPADDLIKVPNDVDPEQAATLSVNPCT 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 199 AYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLGAEHVITEEELRRPEMKNF 278
Cdd:cd08290  134 AYRLLEDFVKLQPGDWVIQNGANSAVGQAVIQLAKLLGIKTINVVRDRPDLEELKERLKALGADHVLTEEELRSLLATEL 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767904541 279 FKDMP--QPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSP 327
Cdd:cd08290  214 LKSAPggRPKLALNCVGGKSATELARLLSPGGTMVTYGGMSGQPVTVPTSL 264
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
87-327 3.39e-77

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: 240.26  E-value: 3.39e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSD--VRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPAnAGLG 164
Cdd:cd05282   13 VLELVSLPIPPPGPgeVLVRMLAAPINPSDLITISGAYGSRPPLPAVPGNEGVGVVVEVGSGVSGLLVGQRVLPL-GGEG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 165 TWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVR 244
Cdd:cd05282   92 TWQEYVVAPADDLIPVPDSISDEQAAMLYINPLTAWLMLTEYLKLPPGDWVIQNAANSAVGRMLIQLAKLLGFKTINVVR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 245 DRpdiqKLSDRLKSLGAEHVITEEELR-RPEMKNFFKDMPqPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVA 323
Cdd:cd05282  172 RD----EQVEELKALGADEVIDSSPEDlAQRVKEATGGAG-ARLALDAVGGESATRLARSLRPGGTLVNYGLLSGEPVPF 246

                 ....
gi 767904541 324 SVSP 327
Cdd:cd05282  247 PRSV 250
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
87-328 4.13e-59

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: 193.83  E-value: 4.13e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpANAGLGTW 166
Cdd:COG0604   16 ELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPLPPGLPFIPGSDAAGVVVAVGEGVTGFKVGDRVA-GLGRGGGY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 167 RTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRdR 246
Cdd:COG0604   95 AEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKPGETVLVHGAAGGVGSAAVQLAKALGARVIATAS-S 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 247 PDiqKLsDRLKSLGAEHVI--TEEELRRPEMKNFFKDmpQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVAS 324
Cdd:COG0604  174 PE--KA-ELLRALGADHVIdyREEDFAERVRALTGGR--GVDVVLDTVGGDTLARSLRALAPGGRLVSIGAASGAPPPLD 248

                 ....
gi 767904541 325 VSPA 328
Cdd:COG0604  249 LAPL 252
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
44-320 1.12e-46

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: 161.35  E-value: 1.12e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  44 RALVYGHHGDPAKVVEGITRELFQRFPwiflqlitavissastvlknlelaavrgSDVRVKMLAAPINPSDINMIQGNYG 123
Cdd:cd08292    2 RAAVHTQFGDPADVLEIGEVPKPTPGA----------------------------GEVLVRTTLSPIHNHDLWTIRGTYG 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 124 FLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPAnAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYrML 203
Cdd:cd08292   54 YKPELPAIGGSEAVGVVDAVGEGVKGLQVGQRVAVA-PVHGTWAEYFVAPADGLVPLPDGISDEVAAQLIAMPLSAL-ML 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 204 MDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKlsdrLKSLGAEHVITEEElrrPEMKNFFKDMP 283
Cdd:cd08292  132 LDFLGVKPGQWLIQNAAGGAVGKLVAMLAAARGINVINLVRRDAGVAE----LRALGIGPVVSTEQ---PGWQDKVREAA 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767904541 284 QPRL---ALNCVGGKSSTELLRQLARGGTMVTYGGMAKQP 320
Cdd:cd08292  205 GGAPisvALDSVGGKLAGELLSLLGEGGTLVSFGSMSGEP 244
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
100-323 3.59e-41

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: 145.54  E-value: 3.59e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANA------------------ 161
Cdd:cd05188    1 EVLVRVEAAGLCGTDLHIRRGGYPPPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNlgcgtcelcrelcpgggi 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 162 ----GLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNAsnSGVGQAVIQIAAALG 236
Cdd:cd05188   81 lgegLDGGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVLKPGDTVlVLGA--GGVGLLAAQLAKAAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 237 LRTINVVRDRpdiQKLsDRLKSLGAEHVI--TEEELRRPEMKNFFKDmpqPRLALNCVGGKSS-TELLRQLARGGTMVTY 313
Cdd:cd05188  159 ARVIVTDRSD---EKL-ELAKELGADHVIdyKEEDLEEELRLTGGGG---ADVVIDAVGGPETlAQALRLLRPGGRIVVV 231
                        250
                 ....*....|
gi 767904541 314 GGMAKQPVVA 323
Cdd:cd05188  232 GGTSGGPPLD 241
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
101-314 4.63e-40

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: 144.18  E-value: 4.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 101 VRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpANAGLGTWRTEAVFSEEALIQV 180
Cdd:cd08241   30 VRIRVEAAGVNFPDLLMIQGKYQVKPPLPFVPGSEVAGVVEAVGEGVTGFKVGDRVV-ALTGQGGFAEEVVVPAAAVFPL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 181 PSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSLG 260
Cdd:cd08241  109 PDGLSFEEAAALPVTYGTAYHALVRRARLQPGETVLVLGAAGGVGLAAVQLAKALGARVIAAASSE---EKL-ALARALG 184
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767904541 261 AEHVITeeeLRRPEMKNFFKDMPQPR---LALNCVGGKSSTELLRQLARGGTMVTYG 314
Cdd:cd08241  185 ADHVID---YRDPDLRERVKALTGGRgvdVVYDPVGGDVFEASLRSLAWGGRLLVIG 238
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
100-320 1.28e-39

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: 143.12  E-value: 1.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI---PANAGL-GTWRTEAVFSEE 175
Cdd:cd08268   29 EVLIRVEAIGLNRADAMFRRGAYIEPPPLPARLGYEAAGVVEAVGAGVTGFAVGDRVSvipAADLGQyGTYAEYALVPAA 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 176 ALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiQKlSDR 255
Cdd:cd08268  109 AVVKLPDGLSFVEAAALWMQYLTAYGALVELAGLRPGDSVLITAASSSVGLAAIQIANAAGATVIATTRTS---EK-RDA 184
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767904541 256 LKSLGAEHVI--TEEELRRPEMKnfFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQP 320
Cdd:cd08268  185 LLALGAAHVIvtDEEDLVAEVLR--ITGGKGVDVVFDPVGGPQFAKLADALAPGGTLVVYGALSGEP 249
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
85-315 9.64e-38

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: 137.74  E-value: 9.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  85 STVLKNLELAAVRG-----SDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTG-LKPGDWVIP 158
Cdd:cd08291   12 PLEVKELSLPEPEVpepgpGEVLIKVEAAPINPSDLGFLKGQYGSTKALPVPPGFEGSGTVVAAGGGPLAqSLIGKRVAF 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 159 ANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLmDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLR 238
Cdd:cd08291   92 LAGSYGTYAEYAVADAQQCLPLPDGVSFEQGASSFVNPLTALGML-ETAREEGAKAVVHTAAASALGRMLVRLCKADGIK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 239 TINVVRdRPDIQKLsdrLKSLGAEHVITEEElrrpemKNFFKDMP------QPRLALNCVGGKSSTELLRQLARGGTMVT 312
Cdd:cd08291  171 VINIVR-RKEQVDL---LKKIGAEYVLNSSD------PDFLEDLKeliaklNATIFFDAVGGGLTGQILLAMPYGSTLYV 240

                 ...
gi 767904541 313 YGG 315
Cdd:cd08291  241 YGY 243
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
100-323 1.31e-34

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: 129.22  E-value: 1.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGFLP--ELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI--PANAGLGTWRTEAVFSEE 175
Cdd:cd05289   29 EVLVKVHAAGVNPVDLKIREGLLKAAFplTLPLIPGHDVAGVVVAVGPGVTGFKVGDEVFgmTPFTRGGAYAEYVVVPAD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 176 ALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQAVIQIAAALGLRTINVVRDRpdiqkLSD 254
Cdd:cd05289  109 ELALKPANLSFEEAAALPLAGLTAWQALFELGGLKAGQTVlIHGAA-GGVGSFAVQLAKARGARVIATASAA-----NAD 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767904541 255 RLKSLGAEHVI--TEEELRRPEMKNFFKdmpqprLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVA 323
Cdd:cd05289  183 FLRSLGADEVIdyTKGDFERAAAPGGVD------AVLDTVGGETLARSLALVKPGGRLVSIAGPPPAEQAA 247
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
100-315 9.94e-31

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: 119.28  E-value: 9.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpANAGLGTWRTE---------- 169
Cdd:cd08266   29 EVLVRVKAAALNHLDLWVRRGMPGIKLPLPHILGSDGAGVVEAVGPGVTNVKPGQRVV-IYPGISCGRCEyclagrenlc 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 170 -----------------AVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIA 232
Cdd:cd08266  108 aqygilgehvdggyaeyVAVPARNLLPIPDNLSFEEAAAAPLTFLTAWHMLVTRARLRPGETVLVHGAGSGVGSAAIQIA 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 233 AALGLRTINVVRDRpdiQKLsDRLKSLGAEHVI--TEEELRRPEMKNFFKdmPQPRLALNCVGGKSSTELLRQLARGGTM 310
Cdd:cd08266  188 KLFGATVIATAGSE---DKL-ERAKELGADYVIdyRKEDFVREVRELTGK--RGVDVVVEHVGAATWEKSLKSLARGGRL 261

                 ....*
gi 767904541 311 VTYGG 315
Cdd:cd08266  262 VTCGA 266
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
84-322 7.20e-29

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: 114.22  E-value: 7.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  84 ASTVLKNLELAA--VRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANA 161
Cdd:cd08253   11 APDVLRLGDLPVptPGPGEVLVRVHASGVNPVDTYIRAGAYPGLPPLPYVPGSDGAGVVEAVGEGVDGLKVGDRVWLTNL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 162 GL----GTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGL 237
Cdd:cd08253   91 GWgrrqGTAAEYVVVPADQLVPLPDGVSFEQGAALGIPALTAYRALFHRAGAKAGETVLVHGGSGAVGHAAVQLARWAGA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 238 RTINVVRDRPDIQklsdRLKSLGAEHVI--TEEELrRPEMKNfFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGG 315
Cdd:cd08253  171 RVIATASSAEGAE----LVRQAGADAVFnyRAEDL-ADRILA-ATAGQGVDVIIEVLANVNLAKDLDVLAPGGRIVVYGS 244

                 ....*..
gi 767904541 316 MAKQPVV 322
Cdd:cd08253  245 GGLRGTI 251
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
87-321 1.68e-28

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 113.28  E-value: 1.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGfLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI--------- 157
Cdd:COG1064   14 ELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWP-VPKLPLVPGHEIVGRVVAVGPGVTGFKVGDRVGvgwvdscgt 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 158 --------------PANAGLGTW---RTEAVFSEEALIQVPSDIPLQSAATLGvnpC---TAYRMLMDFEqLQPGDSV-I 216
Cdd:COG1064   93 ceycrsgrenlcenGRFTGYTTDggyAEYVVVPARFLVKLPDGLDPAEAAPLL---CagiTAYRALRRAG-VGPGDRVaV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 217 QNAsnSGVGQAVIQIAAALGLRTInVVrDRPDiQKLsDRLKSLGAEHVITEEElrRPEMKNfFKDMPQPRLALNCVGGKS 296
Cdd:COG1064  169 IGA--GGLGHLAVQIAKALGAEVI-AV-DRSP-EKL-ELARELGADHVVNSSD--EDPVEA-VRELTGADVVIDTVGAPA 239
                        250       260
                 ....*....|....*....|....*.
gi 767904541 297 STEL-LRQLARGGTMVTyGGMAKQPV 321
Cdd:COG1064  240 TVNAaLALLRRGGRLVL-VGLPGGPI 264
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
99-315 1.43e-26

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: 107.73  E-value: 1.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  99 SDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVipanAGL---GTWRTEAVFSEE 175
Cdd:cd08273   28 GEVVVKVEASGVSFADVQMRRGLYPDQPPLPFTPGYDLVGRVDALGSGVTGFEVGDRV----AALtrvGGNAEYINLDAK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 176 ALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQAVIQIAAALGLRTINVVRDRpdiqkLSD 254
Cdd:cd08273  104 YLVPVPEGVDAAEAVCLVLNYVTAYQMLHRAAKVLTGQRVlIHGAS-GGVGQALLELALLAGAEVYGTASER-----NHA 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767904541 255 RLKSLGAEHViteeeLRRPemKNFFKDMPQPRLA---LNCVGGKSSTELLRQLARGGTMVTYGG 315
Cdd:cd08273  178 ALRELGATPI-----DYRT--KDWLPAMLTPGGVdvvFDGVGGESYEESYAALAPGGTLVCYGG 234
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
88-314 2.48e-26

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: 107.14  E-value: 2.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  88 LKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGflPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAgLGTWR 167
Cdd:cd05286   16 YEDVPVPEPGPGEVLVRNTAIGVNFIDTYFRSGLYP--LPLPFVLGVEGAGVVEAVGPGVTGFKVGDRVAYAGP-PGAYA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 168 TEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVrDRP 247
Cdd:cd05286   93 EYRVVPASRLVKLPDGISDETAAALLLQGLTAHYLLRETYPVKPGDTVLVHAAAGGVGLLLTQWAKALGATVIGTV-SSE 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767904541 248 DIQKLSdrlKSLGAEHVI--TEEELrRPEMKnffkdmpqpRL--------ALNCVGGKSSTELLRQLARGGTMVTYG 314
Cdd:cd05286  172 EKAELA---RAAGADHVInyRDEDF-VERVR---------EItggrgvdvVYDGVGKDTFEGSLDSLRPRGTLVSFG 235
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
90-265 8.25e-26

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: 105.70  E-value: 8.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  90 NLELAAV-----RGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP------ 158
Cdd:cd08276   14 NLKLVEEpvpepGPGEVLVRVHAVSLNYRDLLILNGRYPPPVKDPLIPLSDGAGEVVAVGEGVTRFKVGDRVVPtffpnw 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 159 ---------ANAGL-----GTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQnaSNSG 223
Cdd:cd08276   94 ldgpptaedEASALggpidGVLAEYVVLPEEGLVRAPDHLSFEEAATLPCAGLTAWNALFGLGPLKPGDTVlVQ--GTGG 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767904541 224 VGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSLGAEHVI 265
Cdd:cd08276  172 VSLFALQFAKAAGARVIATSSSD---EKL-ERAKALGADHVI 209
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
101-315 1.45e-25

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: 105.36  E-value: 1.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 101 VRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpanaGL---GTWRTEAVFSEEAL 177
Cdd:cd08275   29 VRVRVEACGLNFADLMARQGLYDSAPKPPFVPGFECAGTVEAVGEGVKDFKVGDRVM----GLtrfGGYAEVVNVPADQV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 178 IQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQAVIQIAAAlgLRTINVVRDrPDIQKLsDRL 256
Cdd:cd08275  105 FPLPDGMSFEEAAAFPVNYLTAYYALFELGNLRPGQSVlVHSAA-GGVGLAAGQLCKT--VPNVTVVGT-ASASKH-EAL 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767904541 257 KSLGAEHVITEEELR-RPEMKNFfkdMPQP-RLALNCVGGKSSTELLRQLARGGTMVTYGG 315
Cdd:cd08275  180 KENGVTHVIDYRTQDyVEEVKKI---SPEGvDIVLDALGGEDTRKSYDLLKPMGRLVVYGA 237
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
87-317 1.80e-25

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: 104.83  E-value: 1.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEgVA-QVVAVGSNVTGLKPGDWVipanAGL-- 163
Cdd:cd05276   16 ELGEVPKPAPGPGEVLIRVAAAGVNRADLLQRQGLYPPPPGASDILGLE-VAgVVVAVGPGVTGWKVGDRV----CALla 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 164 -GTWRTEAVFSEEALIQVPSDIPLQSAATLgvnP---CTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRT 239
Cdd:cd05276   91 gGGYAEYVVVPAGQLLPVPEGLSLVEAAAL---PevfFTAWQNLFQLGGLKAGETVLIHGGASGVGTAAIQLAKALGARV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 240 INVVRDRpdiQKLsDRLKSLGAEHVITeeelRRPEmkNF---FKDMPQPR---LALNCVGGKSSTELLRQLARGGTMVTY 313
Cdd:cd05276  168 IATAGSE---EKL-EACRALGADVAIN----YRTE--DFaeeVKEATGGRgvdVILDMVGGDYLARNLRALAPDGRLVLI 237

                 ....
gi 767904541 314 GGMA 317
Cdd:cd05276  238 GLLG 241
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
103-236 2.60e-24

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 100.54  E-value: 2.60e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541   103 VKMLAAPINPSDINMIQGNYGFLPELpavgGNEGVAQVVAVGSNVTGLKPGDWVIpanaGL--GTWRTEAVFSEEALIQV 180
Cdd:smart00829   1 IEVRAAGLNFRDVLIALGLYPGEAVL----GGECAGVVTRVGPGVTGLAVGDRVM----GLapGAFATRVVTDARLVVPI 72
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767904541   181 PSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQAVIQIAAALG 236
Cdd:smart00829  73 PDGWSFEEAATVPVVFLTAYYALVDLARLRPGESVlIHAAA-GGVGQAAIQLARHLG 128
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
100-311 4.18e-24

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: 100.34  E-value: 4.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGFLPELPavgGNEGVAQVVAVGSNVTGLKPGDWVipanAGL--GTWRTEAVFSEEAL 177
Cdd:cd05195    2 EVEVEVKAAGLNFRDVLVALGLLPGDETPL---GLECSGIVTRVGSGVTGLKVGDRV----MGLapGAFATHVRVDARLV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 178 IQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQAVIQIAAALGLRTINVVRDRPDIqklsDRL 256
Cdd:cd05195   75 VKIPDSLSFEEAATLPVAYLTAYYALVDLARLQKGESVlIHAAA-GGVGQAAIQLAQHLGAEVFATVGSEEKR----EFL 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 257 KSLG--AEHVITEeelRRPEMKNFFKDMPQPR---LALNCVGGKSSTELLRQLARGGTMV 311
Cdd:cd05195  150 RELGgpVDHIFSS---RDLSFADGILRATGGRgvdVVLNSLSGELLRASWRCLAPFGRFV 206
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
78-312 5.84e-24

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: 100.74  E-value: 5.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  78 TAVISSAS----TVLKNLELAAVRGSDVRVKMLAAPINPSDINMIQgnYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPG 153
Cdd:cd08249    2 KAAVLTGPggglLVVVDVPVPKPGPDEVLVKVKAVALNPVDWKHQD--YGFIPSYPAILGCDFAGTVVEVGSGVTRFKVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 154 DWVI-------PANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTA-----YRMLMDF-----EQLQPGDSVI 216
Cdd:cd08249   80 DRVAgfvhggnPNDPRNGAFQEYVVADADLTAKIPDNISFEEAATLPVGLVTAalalfQKLGLPLpppkpSPASKGKPVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 217 QNASNSGVGQAVIQIAAALGLRTINVVrdrpdiqklS----DRLKSLGAEHVI------TEEELRRPEMKNFfkdmpqpR 286
Cdd:cd08249  160 IWGGSSSVGTLAIQLAKLAGYKVITTA---------SpknfDLVKSLGADAVFdyhdpdVVEDIRAATGGKL-------R 223
                        250       260
                 ....*....|....*....|....*....
gi 767904541 287 LALNCVGGKSSTELLRQL---ARGGTMVT 312
Cdd:cd08249  224 YALDCISTPESAQLCAEAlgrSGGGKLVS 252
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
100-325 1.06e-23

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: 99.60  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGN-YGFLPE-LPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANA--GLGTWRTEAVFSEE 175
Cdd:cd08267   28 EVLVKVHAASVNPVDWKLRRGPpKLLLGRpFPPIPGMDFAGEVVAVGSGVTRFKVGDEVFGRLPpkGGGALAEYVVAPES 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 176 ALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiqKLsDR 255
Cdd:cd08267  108 GLAKKPEGVSFEEAAALPVAGLTALQALRDAGKVKPGQRVLINGASGGVGTFAVQIAKALGAHVTGVCSTR----NA-EL 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767904541 256 LKSLGAEHVI--TEEelrrpemkNFFKDMPQPR---LALNCVGGKSST--ELLRQLARGGTMVTYGGMAKQPVVASV 325
Cdd:cd08267  183 VRSLGADEVIdyTTE--------DFVALTAGGEkydVIFDAVGNSPFSlyRASLALKPGGRYVSVGGGPSGLLLVLL 251
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
87-312 1.32e-23

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: 99.56  E-value: 1.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGL--- 163
Cdd:cd08272   16 ELREVPRPQPGPGQVLVRVHASGVNPLDTKIRRGGAAARPPLPAILGCDVAGVVEAVGEGVTRFRVGDEVYGCAGGLggl 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 164 -GTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINV 242
Cdd:cd08272   96 qGSLAEYAVVDARLLALKPANLSMREAAALPLVGITAWEGLVDRAAVQAGQTVLIHGGAGGVGHVAVQLAKAAGARVYAT 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767904541 243 VRDRpdiqKLsDRLKSLGAEHVI------TEEELRRPEMKNFfkdmpqpRLALNCVGGKSSTELLRQLARGGTMVT 312
Cdd:cd08272  176 ASSE----KA-AFARSLGADPIIyyretvVEYVAEHTGGRGF-------DVVFDTVGGETLDASFEAVALYGRVVS 239
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
88-316 1.45e-23

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 99.72  E-value: 1.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  88 LKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGlGTWR 167
Cdd:PTZ00354  18 IGESPKPAPKRNDVLIKVSAAGVNRADTLQRQGKYPPPPGSSEILGLEVAGYVEDVGSDVKRFKEGDRVMALLPG-GGYA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 168 TEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRP 247
Cdd:PTZ00354  97 EYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQSVLIHAGASGVGTAAAQLAEKYGAATIITTSSEE 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767904541 248 DIQKlsdrLKSLGAEHVIteeelRRPEMKNF---FKDMPQPR---LALNCVGGKSSTELLRQLARGGTMVTYGGM 316
Cdd:PTZ00354 177 KVDF----CKKLAAIILI-----RYPDEEGFapkVKKLTGEKgvnLVLDCVGGSYLSETAEVLAVDGKWIVYGFM 242
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
100-311 9.66e-23

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: 96.96  E-value: 9.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGfLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVipanAGLGTWRTEAVFSE----- 174
Cdd:cd08271   29 EVLVKVHAAGLNPVDWKVIAWGPP-AWSYPHVPGVDGAGVVVAVGAKVTGWKVGDRV----AYHASLARGGSFAEytvvd 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 175 -EALIQVPSDIPLQSAATLgvnPC---TAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPdiq 250
Cdd:cd08271  104 aRAVLPLPDSLSFEEAAAL---PCaglTAYQALFKKLRIEAGRTILITGGAGGVGSFAVQLAKRAGLRVITTCSKRN--- 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767904541 251 klSDRLKSLGAEHVITEeelRRPEMKNFFKDMPQPR---LALNCVGGKSSTELLRQLARGGTMV 311
Cdd:cd08271  178 --FEYVKSLGADHVIDY---NDEDVCERIKEITGGRgvdAVLDTVGGETAAALAPTLAFNGHLV 236
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
87-322 2.25e-22

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: 96.84  E-value: 2.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFlpELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI--------- 157
Cdd:cd08279   14 EIEEVELDDPGPGEVLVRIAAAGLCHSDLHVVTGDLPA--PLPAVLGHEGAGVVEEVGPGVTGVKPGDHVVlswipacgt 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 158 -------------------------------------PANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLG------- 193
Cdd:cd08279   92 crycsrgqpnlcdlgagilggqlpdgtrrftadgepvGAMCGLGTFAEYTVVPEASVVKIDDDIPLDRAALLGcgvttgv 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 194 ---VNpcTAyrmlmdfeQLQPGDS--VIqnaSNSGVGQAVIQIAAALGLRTINVVrDrPDIQKLsDRLKSLGAEHVITEE 268
Cdd:cd08279  172 gavVN--TA--------RVRPGDTvaVI---GCGGVGLNAIQGARIAGASRIIAV-D-PVPEKL-ELARRFGATHTVNAS 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767904541 269 ElrrPEMKNFFKDMPQPRL---ALNCVGGKSSTEL-LRQLARGGTMVTYGGMAKQPVV 322
Cdd:cd08279  236 E---DDAVEAVRDLTDGRGadyAFEAVGRAATIRQaLAMTRKGGTAVVVGMGPPGETV 290
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
91-328 7.64e-22

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 95.15  E-value: 7.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  91 LELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLpeLPAVGGNEGVAQVVAVGSNVTGLKPGDWVI------------- 157
Cdd:COG1062    9 VELDEPRPGEVLVRIVAAGLCHSDLHVRDGDLPVP--LPAVLGHEGAGVVEEVGPGVTGVAPGDHVVlsfipscghcryc 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 158 ------------PANA-----------------------GLGTWRTEAVFSEEALIQVPSDIPLQSAATLGvnpC---TA 199
Cdd:COG1062   87 asgrpalceagaALNGkgtlpdgtsrlssadgepvghffGQSSFAEYAVVPERSVVKVDKDVPLELAALLG---CgvqTG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 200 YRMLMDFEQLQPGDSVIqnasnsGVGQAVIQIAAALGLRTINVVrdrpDIqkLSDRL---KSLGAEHVI--TEEELRRpE 274
Cdd:COG1062  164 AGAVLNTAKVRPGDTVAvfg-lgGVGLSAVQGARIAGASRIIAV----DP--VPEKLelaRELGATHTVnpADEDAVE-A 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767904541 275 MKNFFKDMPQprLALNCVGgksSTELLRQ----LARGGTMVTYgGMAKQPVVASVSPA 328
Cdd:COG1062  236 VRELTGGGVD--YAFETTG---NPAVIRQaleaLRKGGTVVVV-GLAPPGAEISLDPF 287
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
100-316 6.13e-21

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: 92.03  E-value: 6.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGnYGFLPeLPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPAN------------------- 160
Cdd:cd08264   28 EVLIRVKMAGVNPVDYNVINA-VKVKP-MPHIPGAEFAGVVEEVGDHVKGVKKGDRVVVYNrvfdgtcdmclsgnemlcr 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 161 ----AGLGT---WRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEqLQPGDSVIQNASNSGVGQAVIQIAA 233
Cdd:cd08264  106 nggiIGVVSnggYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYHALKTAG-LGPGETVVVFGASGNTGIFAVQLAK 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 234 ALGLRTINVVRdrpdiqklSDRLKSLGAEHVITEEELRrPEMKNFFKdmpQPRLALNCVGGKSSTELLRQLARGGTMVTY 313
Cdd:cd08264  185 MMGAEVIAVSR--------KDWLKEFGADEVVDYDEVE-EKVKEITK---MADVVINSLGSSFWDLSLSVLGRGGRLVTF 252

                 ...
gi 767904541 314 GGM 316
Cdd:cd08264  253 GTL 255
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
98-314 6.98e-20

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: 89.13  E-value: 6.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  98 GSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGD-----WVIPA------------- 159
Cdd:cd08297   26 PGEVLVKLEASGVCHTDLHAALGDWPVKPKLPLIGGHEGAGVVVAVGPGVSGLKVGDrvgvkWLYDAcgkceycrtgdet 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 160 ------NAGL---GTWRTEAVFSEEALIQVPSDIPLQSAATL---GVnpcTAYRMLMDfEQLQPGDSVIQNASNSGVGQA 227
Cdd:cd08297  106 lcpnqkNSGYtvdGTFAEYAIADARYVTPIPDGLSFEQAAPLlcaGV---TVYKALKK-AGLKPGDWVVISGAGGGLGHL 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 228 VIQIAAALGLRTINV-VRDRPdiQKLSdrlKSLGAEHVIteeelrrpemkNFFKDMPQPRL-----------ALNCVGGK 295
Cdd:cd08297  182 GVQYAKAMGLRVIAIdVGDEK--LELA---KELGADAFV-----------DFKKSDDVEAVkeltggggahaVVVTAVSA 245
                        250       260
                 ....*....|....*....|
gi 767904541 296 SSTEL-LRQLARGGTMVTYG 314
Cdd:cd08297  246 AAYEQaLDYLRPGGTLVCVG 265
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
83-327 3.39e-19

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


Pssm-ID: 176183 [Multi-domain]  Cd Length: 325  Bit Score: 87.21  E-value: 3.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  83 SASTVLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAvgSNVTGLKPGDWVIPANAG 162
Cdd:cd05280   12 GVSLFLRTLPLDDLPEGDVLIRVHYSSLNYKDALAATGNGGVTRNYPHTPGIDAAGTVVS--SDDPRFREGDEVLVTGYD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 163 LG--TWRTeavFSEeaLIQVPSD----IP----LQSAATLGVNPCTAYRMLMDFEQ--LQPGDSVIQ-NASNSGVGQAVI 229
Cdd:cd05280   90 LGmnTDGG---FAE--YVRVPADwvvpLPeglsLREAMILGTAGFTAALSVHRLEDngQTPEDGPVLvTGATGGVGSIAV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 230 QIAAALGLRTINVVRDrpdiQKLSDRLKSLGAEHVITEEEL----RRPEMKNFFKdmpqprLALNCVGGKSSTELLRQLA 305
Cdd:cd05280  165 AILAKLGYTVVALTGK----EEQADYLKSLGASEVLDREDLldesKKPLLKARWA------GAIDTVGGDVLANLLKQTK 234
                        250       260
                 ....*....|....*....|..
gi 767904541 306 RGGTMVTYGGMAKQPVVASVSP 327
Cdd:cd05280  235 YGGVVASCGNAAGPELTTTVLP 256
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
87-328 1.30e-18

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: 85.45  E-value: 1.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGnygFLP--ELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP------ 158
Cdd:cd08259   14 QIEEVPDPEPGPGEVLIKVKAAGVCYRDLLFWKG---FFPrgKYPLILGHEIVGTVEEVGEGVERFKPGDRVILyyyipc 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 159 --------------ANAGLGTWRTEAVFSEEA------LIQVPSDIPLQSAATLGVNPCTAYRMLmDFEQLQPGDSVIQN 218
Cdd:cd08259   91 gkceyclsgeenlcRNRAEYGEEVDGGFAEYVkvpersLVKLPDNVSDESAALAACVVGTAVHAL-KRAGVKKGDTVLVT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 219 ASNSGVGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSLGAEHVIT----EEElrrpemknfFKDMPQPRLALNCVGG 294
Cdd:cd08259  170 GAGGGVGIHAIQLAKALGARVIAVTRSP---EKL-KILKELGADYVIDgskfSED---------VKKLGGADVVIELVGS 236
                        250       260       270
                 ....*....|....*....|....*....|....
gi 767904541 295 KSSTELLRQLARGGTMVTYGGMAkqPVVASVSPA 328
Cdd:cd08259  237 PTIEESLRSLNKGGRLVLIGNVT--PDPAPLRPG 268
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
100-314 1.79e-17

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: 82.37  E-value: 1.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGFlPELPAVGGNEGVAQVVAVGSNVTGLKPGD-----WVIPA--------------- 159
Cdd:cd08245   26 EVLIKIEACGVCHTDLHAAEGDWGG-SKYPLVPGHEIVGEVVEVGAGVEGRKVGDrvgvgWLVGScgrceycrrglenlc 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 160 ----NAGL---GTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEqLQPGDSV-IQNAsnSGVGQAVIQI 231
Cdd:cd08245  105 qkavNTGYttqGGYAEYMVADAEYTVLLPDGLPLAQAAPLLCAGITVYSALRDAG-PRPGERVaVLGI--GGLGHLAVQY 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 232 AAALGLRTINVVRDrPDIQKLSdrlKSLGAEHVI-TEEELRRPEMKNFFkdmpqpRLALNCV-GGKSSTELLRQLARGGT 309
Cdd:cd08245  182 ARAMGFETVAITRS-PDKRELA---RKLGADEVVdSGAELDEQAAAGGA------DVILVTVvSGAAAEAALGGLRRGGR 251

                 ....*
gi 767904541 310 MVTYG 314
Cdd:cd08245  252 IVLVG 256
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
100-318 6.75e-17

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: 80.57  E-value: 6.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGFLPElPAVGGNEGVAQVVAVGSNVTGLKPGDWVI---------------------P 158
Cdd:COG1063   26 EVLVRVTAVGICGSDLHIYRGGYPFVRP-PLVLGHEFVGEVVEVGEGVTGLKVGDRVVvepnipcgecrycrrgrynlcE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 159 ANAGLGTWRTEAVFSE------EALIQVPSDIPLQSAATlgVNP-CTAYRMLMDFeQLQPGDSV-IQNAsnsG-VGQAVI 229
Cdd:COG1063  105 NLQFLGIAGRDGGFAEyvrvpaANLVKVPDGLSDEAAAL--VEPlAVALHAVERA-GVKPGDTVlVIGA---GpIGLLAA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 230 QIAAALGLRTINVVRDRPDiqKLsDRLKSLGAEHVITeeeLRRPEMKNFFKDMPQPR---LALNCVGGKSS-TELLRQLA 305
Cdd:COG1063  179 LAARLAGAARVIVVDRNPE--RL-ELARELGADAVVN---PREEDLVEAVRELTGGRgadVVIEAVGAPAAlEQALDLVR 252
                        250
                 ....*....|...
gi 767904541 306 RGGTMVTYGGMAK 318
Cdd:COG1063  253 PGGTVVLVGVPGG 265
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
100-317 1.01e-16

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: 79.99  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVipANAGLGTWRTEAVFSEEALIQ 179
Cdd:cd08250   32 EVLVKNRFVGINASDINFTAGRYDPGVKPPFDCGFEGVGEVVAVGEGVTDFKVGDAV--ATMSFGAFAEYQVVPARHAVP 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 180 VPSDIPlqSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVrDRPDIQKLsdrLKSL 259
Cdd:cd08250  110 VPELKP--EVLPLLVSGLTASIALEEVGEMKSGETVLVTAAAGGTGQFAVQLAKLAGCHVIGTC-SSDEKAEF---LKSL 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767904541 260 GAEHVI--TEEELRRPEMKNFfkdmpqPR---LALNCVGGKSSTELLRQLARGGTMVTYGGMA 317
Cdd:cd08250  184 GCDRPInyKTEDLGEVLKKEY------PKgvdVVYESVGGEMFDTCVDNLALKGRLIVIGFIS 240
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
86-353 1.41e-16

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: 79.96  E-value: 1.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  86 TVLKNLELAAVRGS-DVRVKMLAAPINPSDINMIQGnYG--FL-------------PELPAVGGNEGVAQVVAVGSNVTG 149
Cdd:cd08248   16 LLLENARIPVIRKPnQVLIKVHAASVNPIDVLMRSG-YGrtLLnkkrkpqsckysgIEFPLTLGRDCSGVVVDIGSGVKS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 150 LKPGD--WVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQP----GDSVIQNASNSG 223
Cdd:cd08248   95 FEIGDevWGAVPPWSQGTHAEYVVVPENEVSKKPKNLSHEEAASLPYAGLTAWSALVNVGGLNPknaaGKRVLILGGSGG 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 224 VGQAVIQIAAALGlrtINVV-----RDRPDIqklsdrlKSLGAEHVIT------EEELRRPEMKNFFkdmpqprlaLNCV 292
Cdd:cd08248  175 VGTFAIQLLKAWG---AHVTttcstDAIPLV-------KSLGADDVIDynnedfEEELTERGKFDVI---------LDTV 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767904541 293 GGKSSTELLRQLARGGTMVTyggmAKQPVVASVS--PACPSCVCRACSFLRI---SNFE------AFGCPSG 353
Cdd:cd08248  236 GGDTEKWALKLLKKGGTYVT----LVSPLLKNTDklGLVGGMLKSAVDLLKKnvkSLLKgshyrwGFFSPSG 303
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
88-314 5.89e-16

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: 78.25  E-value: 5.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  88 LKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLpeLPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANA------ 161
Cdd:cd05279   15 IEEIEVAPPKAGEVRIKVVATGVCHTDLHVIDGKLPTP--LPVILGHEGAGIVESIGPGVTTLKPGDKVIPLFGpqcgkc 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 162 -----------------------------------------GLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAY 200
Cdd:cd05279   93 kqclnprpnlcsksrgtngrglmsdgtsrftckgkpihhflGTSTFAEYTVVSEISLAKIDPDAPLEKVCLIGCGFSTGY 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 201 RMLMDFEQLQPGDSVIQNASnSGVGQAVIQIAAALGLRTINVVrdrpDIQKlsDRL---KSLGAEHVITEEELRRP---- 273
Cdd:cd05279  173 GAAVNTAKVTPGSTCAVFGL-GGVGLSVIMGCKAAGASRIIAV----DINK--DKFekaKQLGATECINPRDQDKPivev 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 767904541 274 --EMKNFFKDmpqprLALNCVGgksSTELLRQL-----ARGGTMVTYG 314
Cdd:cd05279  246 ltEMTDGGVD-----YAFEVIG---SADTLKQAldatrLGGGTSVVVG 285
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
101-320 1.41e-14

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: 73.56  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 101 VRVKMLAAPINPSDINMIQGNYG--FLPELPAVGGNEGVAQVVAVGSNV-TGLKPGDWVIPANAGLGTWRTEAVFSEEAL 177
Cdd:cd08244   30 VRIAVAAAGVHFVDTQLRSGWGPgpFPPELPYVPGGEVAGVVDAVGPGVdPAWLGRRVVAHTGRAGGGYAELAVADVDSL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 178 IQVPSDIPLQSAATLGVNPCTAYRMLmDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVR-DRpdiqKLsDRL 256
Cdd:cd08244  110 HPVPDGLDLEAAVAVVHDGRTALGLL-DLATLTPGDVVLVTAAAGGLGSLLVQLAKAAGATVVGAAGgPA----KT-ALV 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767904541 257 KSLGAEHVITEEELRRPEMKNFFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQP 320
Cdd:cd08244  184 RALGADVAVDYTRPDWPDQVREALGGGGVTVVLDGVGGAIGRAALALLAPGGRFLTYGWASGEW 247
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
88-327 1.97e-14

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: 73.03  E-value: 1.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  88 LKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLpELPAVGGNEGVAQVVAVGSNvtGLKPGDWVIPANAGLGtwR 167
Cdd:cd08243   17 LREIPIPEPKPGWVLIRVKAFGLNRSEIFTRQGHSPSV-KFPRVLGIEAVGEVEEAPGG--TFTPGQRVATAMGGMG--R 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 168 T-------EAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTI 240
Cdd:cd08243   92 TfdgsyaeYTLVPNEQVYAIDSDLSWAELAALPETYYTAWGSLFRSLGLQPGDTLLIRGGTSSVGLAALKLAKALGATVT 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 241 NVVRDrpdiQKLSDRLKSLGAEHVITE-----EELRRpEMKNFFKdmpqprlALNCVGGKSSTELLRQLARGGTMVTYGG 315
Cdd:cd08243  172 ATTRS----PERAALLKELGADEVVIDdgaiaEQLRA-APGGFDK-------VLELVGTATLKDSLRHLRPGGIVCMTGL 239
                        250
                 ....*....|..
gi 767904541 316 MAKQPVVASVSP 327
Cdd:cd08243  240 LGGQWTLEDFNP 251
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
87-314 3.30e-14

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: 72.79  E-value: 3.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPelPAVGGNEGVAQVVAVGSNVT---GLKPGD-----WVIP 158
Cdd:cd08263   14 TIEEIPVPRPKEGEILIRVAACGVCHSDLHVLKGELPFPP--PFVLGHEISGEVVEVGPNVEnpyGLSVGDrvvgsFIMP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 159 --------------------ANAGLGT-----------------------WRTEAVFSEEALIQVPSDIPLQSAATLGVN 195
Cdd:cd08263   92 cgkcrycargkenlcedffaYNRLKGTlydgttrlfrldggpvymysmggLAEYAVVPATALAPLPESLDYTESAVLGCA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 196 PCTAYRMLMDFEQLQPGDSVIQNASnSGVGQAVIQIAAALGLRTINVVrdrpDIQKlsDRLKS---LGAEHVITEEELRR 272
Cdd:cd08263  172 GFTAYGALKHAADVRPGETVAVIGV-GGVGSSAIQLAKAFGASPIIAV----DVRD--EKLAKakeLGATHTVNAAKEDA 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 767904541 273 PEMknfFKDMPQPRLALNCVGGKSSTELLRQ----LARGGTMVTYG 314
Cdd:cd08263  245 VAA---IREITGGRGVDVVVEALGKPETFKLaldvVRDGGRAVVVG 287
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
100-272 4.61e-14

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: 72.07  E-value: 4.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpANAG--LGTWRTEAVFSEEAL 177
Cdd:cd08251    9 EVRIQVRAFSLNFGDLLCVRGLYPTMPPYPFTPGFEASGVVRAVGPHVTRLAVGDEVI-AGTGesMGGHATLVTVPEDQV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 178 IQVPSDIPLQSAATLgvnPCTAYRMLMDFEQ--LQPGDSV-IQNASnSGVGQAVIQIAAALGLrTINVVRDRPDiqKLsD 254
Cdd:cd08251   88 VRKPASLSFEEACAL---PVVFLTVIDAFARagLAKGEHIlIQTAT-GGTGLMAVQLARLKGA-EIYATASSDD--KL-E 159
                        170       180
                 ....*....|....*....|....
gi 767904541 255 RLKSLGAEHVIT------EEELRR 272
Cdd:cd08251  160 YLKQLGVPHVINyveedfEEEIMR 183
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
99-321 5.42e-14

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 71.99  E-value: 5.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  99 SDVRVKMLAAPINPSDINMIQGnygFLP--ELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPA-NAGLGTW--------- 166
Cdd:PRK13771  26 DEVVIKVNYAGLCYRDLLQLQG---FYPrmKYPVILGHEVVGTVEEVGENVKGFKPGDRVASLlYAPDGTCeycrsgeea 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 167 --RTEAVFSEE--------------ALIQVPSDIPLQSAAtlgVNPC---TAYRMLMDFEqLQPGDSVIQNASNSGVGQA 227
Cdd:PRK13771 103 ycKNRLGYGEEldgffaeyakvkvtSLVKVPPNVSDEGAV---IVPCvtgMVYRGLRRAG-VKKGETVLVTGAGGGVGIH 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 228 VIQIAAALGLRTINVVRDrpdiqklSDRLKSLG--AEHVITEEELRRpEMKNFfkdmPQPRLALNCVGGKSSTELLRQLA 305
Cdd:PRK13771 179 AIQVAKALGAKVIAVTSS-------ESKAKIVSkyADYVIVGSKFSE-EVKKI----GGADIVIETVGTPTLEESLRSLN 246
                        250
                 ....*....|....*.
gi 767904541 306 RGGTMVTYGGMAKQPV 321
Cdd:PRK13771 247 MGGKIIQIGNVDPSPT 262
PRK10754 PRK10754
NADPH:quinone reductase;
100-321 5.80e-14

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 72.07  E-value: 5.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGfLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGLGTWRTEAVFSEEALIQ 179
Cdd:PRK10754  30 EVQVENKAIGINYIDTYIRSGLYP-PPSLPSGLGTEAAGVVSKVGSGVKHIKVGDRVVYAQSALGAYSSVHNVPADKAAI 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 180 VPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQklsdRLKSL 259
Cdd:PRK10754 109 LPDAISFEQAAASFLKGLTVYYLLRKTYEIKPDEQFLFHAAAGGVGLIACQWAKALGAKLIGTVGSAQKAQ----RAKKA 184
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767904541 260 GAEHVITEEELRRPEMKNFFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGmAKQPV 321
Cdd:PRK10754 185 GAWQVINYREENIVERVKEITGGKKVRVVYDSVGKDTWEASLDCLQRRGLMVSFGN-ASGPV 245
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
77-314 8.55e-14

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: 71.76  E-value: 8.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  77 ITAVISSAST---VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGflPELPAVGGNEGVAQVVAVGSNVTGLKPG 153
Cdd:cd08278    3 TTAAVVREPGgpfVLEDVELDDPRPDEVLVRIVATGICHTDLVVRDGGLP--TPLPAVLGHEGAGVVEAVGSAVTGLKPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 154 DWVI----------------PA---------NAGL---GTWR--------------------TEAVFSEEALIQVPSDIP 185
Cdd:cd08278   81 DHVVlsfascgecanclsghPAycenffplnFSGRrpdGSTPlslddgtpvhghffgqssfaTYAVVHERNVVKVDKDVP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 186 LQSAATLGvnpC-------TAYRMLmdfeQLQPGDSV-IQNAsnSGVGQAVIQIAAALGLRTINVVrdrpDIQklSDRL- 256
Cdd:cd08278  161 LELLAPLG---CgiqtgagAVLNVL----KPRPGSSIaVFGA--GAVGLAAVMAAKIAGCTTIIAV----DIV--DSRLe 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767904541 257 --KSLGAEHVI------TEEELRR--PEMKNFfkdmpqprlALNCVGgksSTELLRQ----LARGGTMVTYG 314
Cdd:cd08278  226 laKELGATHVInpkeedLVAAIREitGGGVDY---------ALDTTG---VPAVIEQavdaLAPRGTLALVG 285
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
131-240 1.30e-13

NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 441733 [Multi-domain]  Cd Length: 333  Bit Score: 70.86  E-value: 1.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 131 VGGneGVAQVVAvgSNVTGLKPGDWVIpanaGLGTWRTEAVFSEEALIQV-PSDIPLQSA-ATLGVNPCTAYRMLMDFEQ 208
Cdd:COG2130   72 RGG--AVGEVVE--SRHPDFAVGDLVL----GMLGWQDYAVSDGAGLRKVdPSLAPLSAYlGVLGMPGLTAYFGLLDIGK 143
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767904541 209 LQPGDSVIQNASNSGVGQAVIQIAAALGLRTI 240
Cdd:COG2130  144 PKAGETVVVSAAAGAVGSVVGQIAKLKGCRVV 175
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
81-311 1.81e-13

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: 70.60  E-value: 1.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  81 ISSASTVLK--NLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFlPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVip 158
Cdd:cd05283    5 ARDASGKLEpfTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGP-TKYPLVPGHEIVGIVVAVGSKVTKFKVGDRV-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 159 anaGLGTWR---------------------------------------TEAVFSEEALIQVPSDIPLQSAATL---GVnp 196
Cdd:cd05283   82 ---GVGCQVdscgtceqcksgeeqycpkgvvtyngkypdgtitqggyaDHIVVDERFVFKIPEGLDSAAAAPLlcaGI-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 197 cTAYRMLMDFeQLQPGDSViqnasnsGV------GQAVIQIAAALGLRTinVVRDRPDIQKlsDRLKSLGAEHVI-TEEE 269
Cdd:cd05283  157 -TVYSPLKRN-GVGPGKRV-------GVvgigglGHLAVKFAKALGAEV--TAFSRSPSKK--EDALKLGADEFIaTKDP 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 767904541 270 lrrPEMKNFFKDMpqpRLALNCVGGKSS-TELLRQLARGGTMV 311
Cdd:cd05283  224 ---EAMKKAAGSL---DLIIDTVSASHDlDPYLSLLKPGGTLV 260
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
125-265 7.53e-13

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: 68.78  E-value: 7.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 125 LPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI-PANAGLGTWR-------------------TEAVFSEEA-------- 176
Cdd:cd08260   51 DVTLPHVPGHEFAGVVVEVGEDVSRWRVGDRVTvPFVLGCGTCPycragdsnvcehqvqpgftHPGSFAEYVavpradvn 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 177 LIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASnSGVGQAVIQIAAALGLRTINVvrdrpDI--QKLsD 254
Cdd:cd08260  131 LVRLPDDVDFVTAAGLGCRFATAFRALVHQARVKPGEWVAVHGC-GGVGLSAVMIASALGARVIAV-----DIddDKL-E 203
                        170
                 ....*....|.
gi 767904541 255 RLKSLGAEHVI 265
Cdd:cd08260  204 LARELGAVATV 214
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
128-272 8.93e-13

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: 67.68  E-value: 8.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 128 LPAVGGNEGVAQVVAVGSNVTGLKPGDWVipanAGLGTWRTEAVFSEEALIQVPSDIPLQSAAtLGVNPCTAYRMLMDFE 207
Cdd:cd08255   20 LPLPPGYSSVGRVVEVGSGVTGFKPGDRV----FCFGPHAERVVVPANLLVPLPDGLPPERAA-LTALAATALNGVRDAE 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767904541 208 qLQPGDSVI---QNAsnsgVGQAVIQIAAALGLRTInVVRDR-PDIQKLSDRLKSLGAEHVITEEELRR 272
Cdd:cd08255   95 -PRLGERVAvvgLGL----VGLLAAQLAKAAGAREV-VGVDPdAARRELAEALGPADPVAADTADEIGG 157
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
97-276 9.27e-13

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: 68.32  E-value: 9.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  97 RGSDVRVKMLAAPINPSDINMIQGNYGFLPElPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPA--------NAGLgtwrt 168
Cdd:cd08252   29 GGRDLLVRVEAVSVNPVDTKVRAGGAPVPGQ-PKILGWDASGVVEAVGSEVTLFKVGDEVYYAgditrpgsNAEY----- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 169 EAVfsEEALI-QVPSDIPLQSAATLGVNPCTAYRMLmdFEQLQpGDSVIQNASNS--------GVGQAVIQIAAALGLRT 239
Cdd:cd08252  103 QLV--DERIVgHKPKSLSFAEAAALPLTSLTAWEAL--FDRLG-ISEDAENEGKTlliiggagGVGSIAIQLAKQLTGLT 177
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767904541 240 INVVRDRPDIQklsDRLKSLGAEHVITEEELRRPEMK 276
Cdd:cd08252  178 VIATASRPESI---AWVKELGADHVINHHQDLAEQLE 211
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
136-240 1.01e-12

Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the 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: 176190 [Multi-domain]  Cd Length: 329  Bit Score: 68.28  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 136 GVAQVVAvgSNVTGLKPGDWVIpanaGLGTWRTEAVFSEEALIQV---PSDIPLQSAA-TLGVNPCTAYRMLMDFEQLQP 211
Cdd:cd05288   72 GVGEVVE--SRSPDFKVGDLVS----GFLGWQEYAVVDGASGLRKldpSLGLPLSAYLgVLGMTGLTAYFGLTEIGKPKP 145
                         90       100
                 ....*....|....*....|....*....
gi 767904541 212 GDSVIQNASNSGVGQAVIQIAAALGLRTI 240
Cdd:cd05288  146 GETVVVSAAAGAVGSVVGQIAKLLGARVV 174
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
96-327 1.45e-12

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: 67.97  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  96 VRGSDVRVKMLAAPINPSDINMIQGNYG--FLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI---------------- 157
Cdd:cd05284   23 PGPGQVLVRVGGAGVCHSDLHVIDGVWGgiLPYKLPFTLGHENAGWVEEVGSGVDGLKEGDPVVvhppwgcgtcrycrrg 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 158 -------PANAGLGTWRTEA---VFSEEALIQVPSDIPLQSAATLGVNPCTAYRML---MDFeqLQPGDSVIQNASnSGV 224
Cdd:cd05284  103 eenycenARFPGIGTDGGFAeylLVPSRRLVKLPRGLDPVEAAPLADAGLTAYHAVkkaLPY--LDPGSTVVVIGV-GGL 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 225 GQAVIQIAAALGLRTINVVRDRPDIQKLSDRlksLGAEHVI-----TEEELRRpemknfFKDMPQPRLALNCVGGKSSTE 299
Cdd:cd05284  180 GHIAVQILRALTPATVIAVDRSEEALKLAER---LGADHVLnasddVVEEVRE------LTGGRGADAVIDFVGSDETLA 250
                        250       260       270
                 ....*....|....*....|....*....|.
gi 767904541 300 L-LRQLARGG--TMVTYGGMAKQPVVASVSP 327
Cdd:cd05284  251 LaAKLLAKGGryVIVGYGGHGRLPTSDLVPT 281
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
87-273 2.66e-12

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: 67.36  E-value: 2.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGnyGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANA----- 161
Cdd:cd08277   16 VIEEIEVAPPKANEVRIKMLATSVCHTDILAIEG--FKATLFPVILGHEGAGIVESVGEGVTNLKPGDKVIPLFIgqcge 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 162 -----------------------------------------GLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAY 200
Cdd:cd08277   94 csncrsgktnlcqkyranesglmpdgtsrftckgkkiyhflGTSTFSQYTVVDENYVAKIDPAAPLEHVCLLGCGFSTGY 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767904541 201 RMLMDFEQLQPGDSVIQNASnSGVGQAVIQIAAALGLRTINVVrdrpDIQKLSD-RLKSLGAEHVITEEELRRP 273
Cdd:cd08277  174 GAAWNTAKVEPGSTVAVFGL-GAVGLSAIMGAKIAGASRIIGV----DINEDKFeKAKEFGATDFINPKDSDKP 242
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
87-314 2.97e-12

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: 67.02  E-value: 2.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYgflPE-LPAVGGNEGVAQVVAVGSNVTGLKPGDWVI-------- 157
Cdd:cd08281   22 VIEEVELDPPGPGEVLVKIAAAGLCHSDLSVINGDR---PRpLPMALGHEAAGVVVEVGEGVTDLEVGDHVVlvfvpscg 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 158 -----------------PANA----------------------GLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCT 198
Cdd:cd08281   99 hcrpcaegrpalcepgaAANGagtllsggrrlrlrggeinhhlGVSAFAEYAVVSRRSVVKIDKDVPLEIAALFGCAVLT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 199 AYRMLMDFEQLQPGDSVIQnASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSdrlKSLGAEHVITEEElrrPEMKNF 278
Cdd:cd08281  179 GVGAVVNTAGVRPGQSVAV-VGLGGVGLSALLGAVAAGASQVVAVDLNEDKLALA---RELGATATVNAGD---PNAVEQ 251
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 767904541 279 FKDMPQ--PRLALNCVGGKSSTEL-LRQLARGGTMVTYG 314
Cdd:cd08281  252 VRELTGggVDYAFEMAGSVPALETaYEITRRGGTTVTAG 290
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
142-322 3.44e-12

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


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 66.24  E-value: 3.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 142 AVGSNVTGLKPGdwvipanaglGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQpGDSVIQNASN 221
Cdd:cd08270   74 AVGARVVGLGAM----------GAWAELVAVPTGWLAVLPDGVSFAQAATLPVAGVTALRALRRGGPLL-GRRVLVTGAS 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 222 SGVGQAVIQIAAALGLRTINVVRDRPDiqklSDRLKSLGAEH-VITEEELRRPEMKnffkdmpqprLALNCVGGKSSTEL 300
Cdd:cd08270  143 GGVGRFAVQLAALAGAHVVAVVGSPAR----AEGLRELGAAEvVVGGSELSGAPVD----------LVVDSVGGPQLARA 208
                        170       180
                 ....*....|....*....|..
gi 767904541 301 LRQLARGGTMVTYGGMAKQPVV 322
Cdd:cd08270  209 LELLAPGGTVVSVGSSSGEPAV 230
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
100-321 8.41e-12

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: 65.35  E-value: 8.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI---------------------- 157
Cdd:cd08254   28 EVLVKVKAAGVCHSDLHILDGGVPTLTKLPLTLGHEIAGTVVEVGAGVTNFKVGDRVAvpavipcgacalcrrgrgnlcl 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 158 ----PANAGLGTWRTEAVFSEEALIQVPSDIPLQ--SAATLGVNpcTAYRMLMDFEQLQPGDSV-IQNAsnSGVGQAVIQ 230
Cdd:cd08254  108 nqgmPGLGIDGGFAEYIVVPARALVPVPDGVPFAqaAVATDAVL--TPYHAVVRAGEVKPGETVlVIGL--GGLGLNAVQ 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 231 IAAALGLRTINVVRDRpdiQKLsDRLKSLGA-EHVITEEELRRPEMKNffkdmPQPR---LALNCVGGKSSTEL-LRQLA 305
Cdd:cd08254  184 IAKAMGAAVIAVDIKE---EKL-ELAKELGAdEVLNSLDDSPKDKKAA-----GLGGgfdVIFDFVGTQPTFEDaQKAVK 254
                        250
                 ....*....|....*..
gi 767904541 306 RGGTMVTYG-GMAKQPV 321
Cdd:cd08254  255 PGGRIVVVGlGRDKLTV 271
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
223-327 1.09e-11

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 61.47  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  223 GVGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSLGAEHVITEEELRRPE-MKNFFKDMpQPRLALNCVG-GKSSTEL 300
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSE---EKL-ELAKELGADHVINPKETDLVEeIKELTGGK-GVDVVFDCVGsPATLEQA 75
                          90       100
                  ....*....|....*....|....*..
gi 767904541  301 LRQLARGGTMVTYgGMAKQPVVASVSP 327
Cdd:pfam00107  76 LKLLRPGGRVVVV-GLPGGPLPLPLAP 101
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
87-269 1.61e-11

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


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 64.30  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMI-QGNYGFL-PELPAVGGNEGVAQVVAVGSNVTGLKPGDWVipANAGLG 164
Cdd:cd08269    8 EVEEHPRPTPGPGQVLVRVEGCGVCGSDLPAFnQGRPWFVyPAEPGGPGHEGWGRVVALGPGVRGLAVGDRV--AGLSGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 165 TWRTEAVFSEEALIQVPSD-----IPLQSAATlGVNpctayrmLMDFEQLQPGDSVIQNASNSgVGQAVIQIAAALGLRT 239
Cdd:cd08269   86 AFAEYDLADADHAVPLPSLldgqaFPGEPLGC-ALN-------VFRRGWIRAGKTVAVIGAGF-IGLLFLQLAAAAGARR 156
                        170       180       190
                 ....*....|....*....|....*....|
gi 767904541 240 INVVRDRPDIQKLSdrlKSLGAEHVITEEE 269
Cdd:cd08269  157 VIAIDRRPARLALA---RELGATEVVTDDS 183
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
100-157 2.40e-11

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: 59.93  E-value: 2.40e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767904541  100 DVRVKMLAAPINPSDINMIQGNYgFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI 157
Cdd:pfam08240   2 EVLVKVKAAGICGSDLHIYKGGN-PPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVV 58
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
131-265 2.84e-11

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


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 64.36  E-value: 2.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 131 VGGNEGVAQVVAVGSNVTGLKPGDWVI----------PANAGLGT--------WRTE---AVFSEEALIQV------PSD 183
Cdd:cd08246   84 IGGSDASGIVWAVGEGVKNWKVGDEVVvhcsvwdgndPERAGGDPmfdpsqriWGYEtnyGSFAQFALVQAtqlmpkPKH 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 184 IPLQSAATLGVNPCTAYRMLMDFE--QLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiQKlSDRLKSLGA 261
Cdd:cd08246  164 LSWEEAAAYMLVGATAYRMLFGWNpnTVKPGDNVLIWGASGGLGSMAIQLARAAGANPVAVVSSE---EK-AEYCRALGA 239

                 ....
gi 767904541 262 EHVI 265
Cdd:cd08246  240 EGVI 243
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
101-323 3.26e-11

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


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 63.86  E-value: 3.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 101 VRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEG-------------------VAQVVAVGSNVTGLKPGDWVIpana 161
Cdd:cd08274   31 VLIRVGACGVNNTDINTREGWYSTEVDGATDSTGAGeagwwggtlsfpriqgadiVGRVVAVGEGVDTARIGERVL---- 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 162 gLGTWRTEAVFSEEALIQ---------------VPSD-----IPLQSAATLGVNPC---TAYRMLmDFEQLQPGDSVIQN 218
Cdd:cd08274  107 -VDPSIRDPPEDDPADIDyigserdggfaeytvVPAEnaypvNSPLSDVELATFPCsysTAENML-ERAGVGAGETVLVT 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 219 ASNSGVGQAVIQIAAALGLRTINVVRDRPDiqklsDRLKSLGAEHVITEEELRRPEMKNFFKdmPQPRLALNCVGGKSST 298
Cdd:cd08274  185 GASGGVGSALVQLAKRRGAIVIAVAGAAKE-----EAVRALGADTVILRDAPLLADAKALGG--EPVDVVADVVGGPLFP 257
                        250       260
                 ....*....|....*....|....*
gi 767904541 299 ELLRQLARGGTMVTYGGMAKqPVVA 323
Cdd:cd08274  258 DLLRLLRPGGRYVTAGAIAG-PVVE 281
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
88-314 4.19e-11

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: 63.10  E-value: 4.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  88 LKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFlPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI---------- 157
Cdd:cd08258   16 LREVPEPEPGPGEVLIKVAAAGICGSDLHIYKGDYDP-VETPVVLGHEFSGTIVEVGPDVEGWKVGDRVVsettfstcgr 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 158 ------------PANAGLGTWR----TEAVFS-EEALIQVPSDIPLQSAATLgvNP-CTAYRMLMDFEQLQPGDSVIqnA 219
Cdd:cd08258   95 cpycrrgdynlcPHRKGIGTQAdggfAEYVLVpEESLHELPENLSLEAAALT--EPlAVAVHAVAERSGIRPGDTVV--V 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 220 SNSG-VGQAVIQIAAALGLRTINVvrdrpDIQKLSDRL---KSLGAEHVITEEELRRpEMKNFFKDMPQPRLALNCVGG- 294
Cdd:cd08258  171 FGPGpIGLLAAQVAKLQGATVVVV-----GTEKDEVRLdvaKELGADAVNGGEEDLA-ELVNEITDGDGADVVIECSGAv 244
                        250       260
                 ....*....|....*....|...
gi 767904541 295 ---KSSTELLRqlaRGGTMVTYG 314
Cdd:cd08258  245 palEQALELLR---KGGRIVQVG 264
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
89-327 4.36e-11

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


Pssm-ID: 176249 [Multi-domain]  Cd Length: 326  Bit Score: 63.12  E-value: 4.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  89 KNLELAAVRGSDVRVKMLAAPINPSD------INMIQGNYGFLPELPAVGgnegvaqvVAVGSNVTGLKPGDWVIPANAG 162
Cdd:cd08289   18 KNLTLDDLPEGDVLIRVAYSSVNYKDglasipGGKIVKRYPFIPGIDLAG--------TVVESNDPRFKPGDEVIVTSYD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 163 LGTWRtEAVFSEEA------LIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQ--LQP-GDSVIQNASNSGVGQAVIQIAA 233
Cdd:cd08289   90 LGVSH-HGGYSEYArvpaewVVPLPKGLTLKEAMILGTAGFTAALSIHRLEEngLTPeQGPVLVTGATGGVGSLAVSILA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 234 ALGLRTINVVRDRPDiqklSDRLKSLGAEHVITEEELRRPEMKNFFKDMPQPrlALNCVGGKSSTELLRQLARGGTMVTY 313
Cdd:cd08289  169 KLGYEVVASTGKADA----ADYLKKLGAKEVIPREELQEESIKPLEKQRWAG--AVDPVGGKTLAYLLSTLQYGGSVAVS 242
                        250
                 ....*....|....
gi 767904541 314 GGMAKQPVVASVSP 327
Cdd:cd08289  243 GLTGGGEVETTVFP 256
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
100-262 3.78e-10

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: 60.35  E-value: 3.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGFLPelPAVGGNEGVAQVVAVGSNVTGLKPGDWVI-PANAGLG---------TWR-- 167
Cdd:cd08284   27 DAIVKVTAAAICGSDLHIYRGHIPSTP--GFVLGHEFVGEVVEVGPEVRTLKVGDRVVsPFTIACGecfycrrgqSGRca 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 168 -----------------TEAV---FSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFeQLQPGDSVIQNASNSgVGQA 227
Cdd:cd08284  105 kgglfgyagspnldgaqAEYVrvpFADGTLLKLPDGLSDEAALLLGDILPTGYFGAKRA-QVRPGDTVAVIGCGP-VGLC 182
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767904541 228 VIQIAAALGLRTINVVrDRpdiqkLSDRL---KSLGAE 262
Cdd:cd08284  183 AVLSAQVLGAARVFAV-DP-----VPERLeraAALGAE 214
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
100-322 4.16e-10

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: 60.28  E-value: 4.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGFLpELPAVGGNEGVAQVVAVGSNVTGLKPGDWV--IP------------------- 158
Cdd:cd08261   26 EVLVRVKRVGICGSDLHIYHGRNPFA-SYPRILGHELSGEVVEVGEGVAGLKVGDRVvvDPyiscgecyacrkgrpncce 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 159 ANAGLGTWRTEAvFSE-----EALIQVPSDIPLQSAA-----TLGVNpcTAYRMlmdfeQLQPGDSV-IQNAsnSGVGQA 227
Cdd:cd08261  105 NLQVLGVHRDGG-FAEyivvpADALLVPEGLSLDQAAlveplAIGAH--AVRRA-----GVTAGDTVlVVGA--GPIGLG 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 228 VIQIAAALGLRTInvVRDRPDiqklsDRL---KSLGAEHVI------TEEELRrpEMKNffKDMPQprLALNCVGGKSS- 297
Cdd:cd08261  175 VIQVAKARGARVI--VVDIDD-----ERLefaRELGADDTInvgdedVAARLR--ELTD--GEGAD--VVIDATGNPASm 241
                        250       260
                 ....*....|....*....|....*
gi 767904541 298 TELLRQLARGGTMVtYGGMAKQPVV 322
Cdd:cd08261  242 EEAVELVAHGGRVV-LVGLSKGPVT 265
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
91-158 5.49e-10

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


Pssm-ID: 176259 [Multi-domain]  Cd Length: 373  Bit Score: 60.02  E-value: 5.49e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767904541  91 LELAAVRGSDVRVKMLAAPINPSDINMIQGNygFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP 158
Cdd:cd08299   25 IEVAPPKAHEVRIKIVATGICRSDDHVVSGK--LVTPFPVILGHEAAGIVESVGEGVTTVKPGDKVIP 90
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
99-312 6.28e-10

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: 59.97  E-value: 6.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  99 SDVRVKMLAAPINPSDInMIQGNYGFLPELPAVG-GNE--GVaqVVAVGSNV-TGLKPGDWV----IPANAGLGTWRTEA 170
Cdd:cd08247   29 NEIVVKVHAAALNPVDL-KLYNSYTFHFKVKEKGlGRDysGV--IVKVGSNVaSEWKVGDEVcgiyPHPYGGQGTLSQYL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 171 VF----SEEALIQVPSDIPLQSAA----TLGvnpcTAYRMLMDFEQ-LQPGDSVIQNASNSGVGQAVIQIaAALGLRTIN 241
Cdd:cd08247  106 LVdpkkDKKSITRKPENISLEEAAawplVLG----TAYQILEDLGQkLGPDSKVLVLGGSTSVGRFAIQL-AKNHYNIGT 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 242 VV---RDRPdiqklSDRLKSLGAEHVI-----TEEELRRPEMKNfFKDMPQPRLALNCVGG----KSSTELLRQLARGGT 309
Cdd:cd08247  181 VVgtcSSRS-----AELNKKLGADHFIdydahSGVKLLKPVLEN-VKGQGKFDLILDCVGGydlfPHINSILKPKSKNGH 254

                 ...
gi 767904541 310 MVT 312
Cdd:cd08247  255 YVT 257
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
100-265 6.26e-09

formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase (FDH), which is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. This family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Another member is identified as a dihydroxyacetone reductase. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176246 [Multi-domain]  Cd Length: 345  Bit Score: 56.88  E-value: 6.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNygfLPELPA--VGGNEGVAQVVAVGSNVTGLKPGDWVIPA-----------NAGL--- 163
Cdd:cd08286   27 DAIVKMLKTTICGTDLHILKGD---VPTVTPgrILGHEGVGVVEEVGSAVTNFKVGDRVLIScisscgtcgycRKGLysh 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 164 ---GTWR-------TEAVF-----SEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIqnASNSG-VGQA 227
Cdd:cd08286  104 cesGGWIlgnlidgTQAEYvriphADNSLYKLPEGVDEEAAVMLSDILPTGYECGVLNGKVKPGDTVA--IVGAGpVGLA 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767904541 228 VIQIAAALGLRTINVVrDRPDiqklsDRL---KSLGAEHVI 265
Cdd:cd08286  182 ALLTAQLYSPSKIIMV-DLDD-----NRLevaKKLGATHTV 216
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
87-361 1.78e-08

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: 55.23  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGflPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI--------- 157
Cdd:cd08234   13 EVEEVPVPEPGPDEVLIKVAACGICGTDLHIYEGEFG--AAPPLVPGHEFAGVVVAVGSKVTGFKVGDRVAvdpniycge 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 158 ------------PANAGLGTWRT----E-AVFSEEALIQVPSDIPLQSAATL--------GVNPCtayrmlmdfeQLQPG 212
Cdd:cd08234   91 cfycrrgrpnlcENLTAVGVTRNggfaEyVVVPAKQVYKIPDNLSFEEAALAeplscavhGLDLL----------GIKPG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 213 DSV-IQNAsnsGV-GQAVIQIAAALGLRTINVVrDRPDIqKLsDRLKSLGAEHVITEEELRRPEMKNffkdmPQPR---L 287
Cdd:cd08234  161 DSVlVFGA---GPiGLLLAQLLKLNGASRVTVA-EPNEE-KL-ELAKKLGATETVDPSREDPEAQKE-----DNPYgfdV 229
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767904541 288 ALNCVGGKSSTEL-LRQLARGGTMVTYgGMAKQPVVASVSPacpscvcracsflrisnFEAFgcpsGRRITVQTS 361
Cdd:cd08234  230 VIEATGVPKTLEQaIEYARRGGTVLVF-GVYAPDARVSISP-----------------FEIF----QKELTIIGS 282
MDR_yhdh cd08288
Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR ...
88-317 4.83e-08

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


Pssm-ID: 176248 [Multi-domain]  Cd Length: 324  Bit Score: 54.08  E-value: 4.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  88 LKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNvtGLKPGDWVIPANAGLGTWR 167
Cdd:cd08288   17 LRELDESDLPEGDVTVEVHYSTLNYKDGLAITGKGGIVRTFPLVPGIDLAGTVVESSSP--RFKPGDRVVLTGWGVGERH 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 168 -----TEAVFSEEALIQVPSDIPLQSAATLGVNPCTAyrML--MDFEQ--LQPGDS-VIQNASNSGVGQAVIQIAAALGL 237
Cdd:cd08288   95 wggyaQRARVKADWLVPLPEGLSARQAMAIGTAGFTA--MLcvMALEDhgVTPGDGpVLVTGAAGGVGSVAVALLARLGY 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 238 RTInVVRDRPDiqkLSDRLKSLGAEHVITEEELRRPEmknffKDMPQPRLA--LNCVGGKSSTELLRQLARGGTmVTYGG 315
Cdd:cd08288  173 EVV-ASTGRPE---EADYLRSLGASEIIDRAELSEPG-----RPLQKERWAgaVDTVGGHTLANVLAQTRYGGA-VAACG 242

                 ..
gi 767904541 316 MA 317
Cdd:cd08288  243 LA 244
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
90-322 6.38e-08

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: 53.77  E-value: 6.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  90 NLELAAVRGSDVRVKMLAAPINPSDINMIQGNY----GFL-------PELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI- 157
Cdd:cd08240   17 EIDTPKPPGTEVLVKVTACGVCHSDLHIWDGGYdlggGKTmslddrgVKLPLVLGHEIVGEVVAVGPDAADVKVGDKVLv 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 158 ----------------------PANAGL---GTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAY---RMLMDFEQL 209
Cdd:cd08240   97 ypwigcgecpvclagdenlcakGRALGIfqdGGYAEYVIVPHSRYLVDPGGLDPALAATLACSGLTAYsavKKLMPLVAD 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 210 QPgdSVIQNAsnSGVGQAVIQIAAALGLRTInVVRDrPDIQKLsDRLKSLGAEHVITEEELRrpEMKNFFKDMP-QPRLA 288
Cdd:cd08240  177 EP--VVIIGA--GGLGLMALALLKALGPANI-IVVD-IDEAKL-EAAKAAGADVVVNGSDPD--AAKRIIKAAGgGVDAV 247
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 767904541 289 LNCVGGKSSTEL-LRQLARGGTMVT---YGGMAKQPVV 322
Cdd:cd08240  248 IDFVNNSATASLaFDILAKGGKLVLvglFGGEATLPLP 285
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
87-323 7.75e-08

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: 53.42  E-value: 7.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPeLPAVGGNEGVAQVVAVGSNVT------GLKPGDWVI--- 157
Cdd:cd08231   14 EIREVPLPDLEPGAVLVRVRLAGVCGSDVHTVAGRRPRVP-LPIILGHEGVGRVVALGGGVTtdvagePLKVGDRVTwsv 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 158 --------------PA----------NAGLGTWRTEAVFSEEALIQ-------VPSDIPLQSAATLGVNPCTAYRMLMDF 206
Cdd:cd08231   93 gapcgrcyrclvgdPTkcenrkkyghEASCDDPHLSGGYAEHIYLPpgtaivrVPDNVPDEVAAPANCALATVLAALDRA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 207 EQLQPGDSV-IQNAsnSGVGQAVIQIAAALGLRTInVVRDRPDiqklsDRLK---SLGAEHVITEEELRRPEMKNFFKDM 282
Cdd:cd08231  173 GPVGAGDTVvVQGA--GPLGLYAVAAAKLAGARRV-IVIDGSP-----ERLElarEFGADATIDIDELPDPQRRAIVRDI 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 767904541 283 PQPR---LALNCVGGKSS-TELLRQLARGGTMVTYGGMAKQPVVA 323
Cdd:cd08231  245 TGGRgadVVIEASGHPAAvPEGLELLRRGGTYVLVGSVAPAGTVP 289
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
100-324 2.04e-07

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: 52.23  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGFLPelPAVGGNEGVAQVVAVGSNVTGLKPGDWV-----IPANA------G------ 162
Cdd:cd08236   26 EVLVKVKACGICGSDIPRYLGTGAYHP--PLVLGHEFSGTVEEVGSGVDDLAVGDRVavnplLPCGKceyckkGeyslcs 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 163 ----LGTWRTEAvFSE------EALIQVPSDIPLQSAATlgVNPCT----AYRMLMdfeqLQPGDSVIqnASNSG-VGQA 227
Cdd:cd08236  104 nydyIGSRRDGA-FAEyvsvpaRNLIKIPDHVDYEEAAM--IEPAAvalhAVRLAG----ITLGDTVV--VIGAGtIGLL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 228 VIQIAAALGLRTINVVrDrPDIQKLsDRLKSLGAEHVIteeelrRPEMKNFFKDMPQ-----PRLALNCVGGKSSTELLR 302
Cdd:cd08236  175 AIQWLKILGAKRVIAV-D-IDDEKL-AVARELGADDTI------NPKEEDVEKVRELtegrgADLVIEAAGSPATIEQAL 245
                        250       260
                 ....*....|....*....|..
gi 767904541 303 QLARGGTMVTYGGMAKQPVVAS 324
Cdd:cd08236  246 ALARPGGKVVLVGIPYGDVTLS 267
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
100-170 4.53e-07

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: 51.09  E-value: 4.53e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGFLPElPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpANAGLGTWRTEA 170
Cdd:cd08285   26 DAIVRPTAVAPCTSDVHTVWGGAPGERH-GMILGHEAVGVVEEVGSEVKDFKPGDRVI-VPAITPDWRSVA 94
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
100-165 5.32e-07

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: 51.05  E-value: 5.32e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGflPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV-IPANAGLGT 165
Cdd:cd08282   27 DAIVRITTTAICGSDLHMYRGRTG--AEPGLVLGHEAMGEVEEVGSAVESLKVGDRVvVPFNVACGR 91
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
87-158 3.60e-06

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


Pssm-ID: 176260 [Multi-domain]  Cd Length: 368  Bit Score: 48.38  E-value: 3.60e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYgflPE--LPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP 158
Cdd:cd08300   16 SIEEVEVAPPKAGEVRIKILATGVCHTDAYTLSGAD---PEglFPVILGHEGAGIVESVGEGVTSVKPGDHVIP 86
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
195-269 4.37e-06

CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.


Pssm-ID: 107204 [Multi-domain]  Cd Length: 291  Bit Score: 47.89  E-value: 4.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 195 NPC------TAYRMLMDFEQ---LQPGDSVIQNAS-NSGVGQAVIqiAAALGLRTINVVRDRPDIQKLsDRLKSLGAEHV 264
Cdd:cd01561   27 NPGgsvkdrIALYMIEDAEKrglLKPGTTIIEPTSgNTGIGLAMV--AAAKGYRFIIVMPETMSEEKR-KLLRALGAEVI 103

                 ....*
gi 767904541 265 ITEEE 269
Cdd:cd01561  104 LTPEA 108
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
100-262 4.80e-06

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 47.95  E-value: 4.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGFlPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV----------------------- 156
Cdd:PLN02586  39 DVTVKILYCGVCHSDLHTIKNEWGF-TRYPIVPGHEIVGIVTKLGKNVKKFKEGDRVgvgvivgsckscescdqdlenyc 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 157 ----IPANA-------GLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSvIQNASNSGVG 225
Cdd:PLN02586 118 pkmiFTYNSighdgtkNYGGYSDMIVVDQHFVLRFPDNLPLDAGAPLLCAGITVYSPMKYYGMTEPGKH-LGVAGLGGLG 196
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767904541 226 QAVIQIAAALGLRtINVVRDRPdiQKLSDRLKSLGAE 262
Cdd:PLN02586 197 HVAVKIGKAFGLK-VTVISSSS--NKEDEAINRLGAD 230
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
174-317 6.56e-06

leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase.


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 47.30  E-value: 6.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  174 EEALIQVPSDIPLQSA-ATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIqkl 252
Cdd:TIGR02825 100 EKLLTEWPDTLPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKV--- 176
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767904541  253 sDRLKSLGAEHVIT-------EEELRR--PEMKNFFKDMpqprlalncVGGKSSTELLRQLARGGTMVTYGGMA 317
Cdd:TIGR02825 177 -AYLKKLGFDVAFNyktvkslEETLKKasPDGYDCYFDN---------VGGEFSNTVIGQMKKFGRIAICGAIS 240
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
135-308 6.82e-06

13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 hydroxydehydrogenase activity; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto- 13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the 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: 176254 [Multi-domain]  Cd Length: 329  Bit Score: 47.26  E-value: 6.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 135 EGVAQVVAvgSNVTGLKPGDWVIpANAGlgtWRTEAVFSEEA---LIQVPSDIPLQ---SAA--TLGVNPCTAYRMLMDF 206
Cdd:cd08294   65 TQVAKVIE--SKNSKFPVGTIVV-ASFG---WRTHTVSDGKDqpdLYKLPADLPDDlppSLAlgVLGMPGLTAYFGLLEI 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 207 EQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRdrpdiqklSD----RLKSLGAEHVIT------EEELRR--PE 274
Cdd:cd08294  139 CKPKAGETVVVNGAAGAVGSLVGQIAKIKGCKVIGCAG--------SDdkvaWLKELGFDAVFNyktvslEEALKEaaPD 210
                        170       180       190
                 ....*....|....*....|....*....|....
gi 767904541 275 MKNFFKDmpqprlalNcVGGKSSTELLRQLARGG 308
Cdd:cd08294  211 GIDCYFD--------N-VGGEFSSTVLSHMNDFG 235
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
100-316 8.67e-06

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: 47.27  E-value: 8.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNyGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV-IPANA----------------- 161
Cdd:cd05278   27 DAIVRVTATSICGSDLHIYRGG-VPGAKHGMILGHEFVGEVVEVGSDVKRLKPGDRVsVPCITfcgrcrfcrrgyhahce 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 162 -GLGTW----RTEAVFSE--------EALIQVPSDIPLQSAATLGVNPCTAY---RMlmdfEQLQPGDSVIqnASNSG-V 224
Cdd:cd05278  106 nGLWGWklgnRIDGGQAEyvrvpyadMNLAKIPDGLPDEDALMLSDILPTGFhgaEL----AGIKPGSTVA--VIGAGpV 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 225 GQAVIQIAAALGLRTINVVRDRPDIQKLsdrLKSLGAEHVITeeeLRRPEMKNFFKDMPQPRLA---LNCVGGKSSTELL 301
Cdd:cd05278  180 GLCAVAGARLLGAARIIAVDSNPERLDL---AKEAGATDIIN---PKNGDIVEQILELTGGRGVdcvIEAVGFEETFEQA 253
                        250
                 ....*....|....*
gi 767904541 302 RQLARGGTMVTYGGM 316
Cdd:cd05278  254 VKVVRPGGTIANVGV 268
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
79-156 9.38e-06

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: 46.82  E-value: 9.38e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767904541  79 AVISSASTV-LKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYgFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV 156
Cdd:cd08235    4 AVLHGPNDVrLEEVPVPEPGPGEVLVKVRACGICGTDVKKIRGGH-TDLKPPRILGHEIAGEIVEVGDGVTGFKVGDRV 81
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
101-266 1.17e-05

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: 46.54  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 101 VRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPAN-AGLGTWRT----------- 168
Cdd:cd08239   27 VLLRVKASGLCGSDLHYYYHGHRAPAYQGVIPGHEPAGVVVAVGPGVTHFRVGDRVMVYHyVGCGACRNcrrgwmqlcts 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 169 ------------EAVF---SEEALIQVPSDIPLQSAATLGVNPCTAYRMLmDFEQLQPGDSVIqnASNSG-VGQAVIQIA 232
Cdd:cd08239  107 kraaygwnrdggHAEYmlvPEKTLIPLPDDLSFADGALLLCGIGTAYHAL-RRVGVSGRDTVL--VVGAGpVGLGALMLA 183
                        170       180       190
                 ....*....|....*....|....*....|....
gi 767904541 233 AALGLRTINVVRDRPDIQKLSdrlKSLGAEHVIT 266
Cdd:cd08239  184 RALGAEDVIGVDPSPERLELA---KALGADFVIN 214
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
85-327 1.93e-05

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


Pssm-ID: 274315 [Multi-domain]  Cd Length: 323  Bit Score: 46.01  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541   85 STVLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVA-------VGSNV--TGLK---- 151
Cdd:TIGR02823  13 SAQVETLDLSDLPEGDVLIKVAYSSLNYKDALAITGKGGVVRSYPMIPGIDAAGTVVSsedprfrEGDEVivTGYGlgvs 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  152 -----------PGDWVIPanaglgtwrteavfseealiqVPSDIPLQSAATLGVNPCTAYRMLMDFEQ--LQPGD-SVIQ 217
Cdd:TIGR02823  93 hdggysqyarvPADWLVP---------------------LPEGLSLREAMALGTAGFTAALSVMALERngLTPEDgPVLV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  218 NASNSGVGQAVIQIAAALGLRTInVVRDRPDiqkLSDRLKSLGAEHVITEEELR---RPEMKNFFKDmpqprlALNCVGG 294
Cdd:TIGR02823 152 TGATGGVGSLAVAILSKLGYEVV-ASTGKAE---EEDYLKELGASEVIDREDLSppgKPLEKERWAG------AVDTVGG 221
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767904541  295 KSSTELLRQLARGGTMVTYGGMAKQPVVASVSP 327
Cdd:TIGR02823 222 HTLANVLAQLKYGGAVAACGLAGGPDLPTTVLP 254
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
100-158 3.30e-05

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: 45.36  E-value: 3.30e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNyGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP 158
Cdd:cd08301   29 EVRIKILHTSLCHTDVYFWEAK-GQTPLFPRILGHEAAGIVESVGEGVTDLKPGDHVLP 86
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
87-156 3.54e-05

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: 45.25  E-value: 3.54e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGfLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV 156
Cdd:cd08298   18 RLTEVPVPEPGPGEVLIKVEACGVCRTDLHIVEGDLP-PPKLPLIPGHEIVGRVEAVGPGVTRFSVGDRV 86
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
136-232 7.98e-05

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 44.06  E-value: 7.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 136 GVAQVVAvgSNVTGLKPGDWVipanAGLGTWRTEAVF--SEEAL--IQVPSDIPLQ-SAATLGVNPCTAYRMLMDFEQLQ 210
Cdd:PLN03154  84 GVSKVVD--SDDPNFKPGDLI----SGITGWEEYSLIrsSDNQLrkIQLQDDIPLSyHLGLLGMAGFTAYAGFYEVCSPK 157
                         90       100
                 ....*....|....*....|..
gi 767904541 211 PGDSVIQNASNSGVGQAVIQIA 232
Cdd:PLN03154 158 KGDSVFVSAASGAVGQLVGQLA 179
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
99-256 1.62e-04

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 43.09  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  99 SDVRVKMLAAPINPSDINMIQGNYGFlPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV------------IPANAGLGTW 166
Cdd:PLN02178  32 NDVTVKILFCGVCHSDLHTIKNHWGF-SRYPIIPGHEIVGIATKVGKNVTKFKEGDRVgvgviigscqscESCNQDLENY 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 167 RTEAVFSEEA----------------------LIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGV 224
Cdd:PLN02178 111 CPKVVFTYNSrssdgtrnqggysdvivvdhrfVLSIPDGLPSDSGAPLLCAGITVYSPMKYYGMTKESGKRLGVNGLGGL 190
                        170       180       190
                 ....*....|....*....|....*....|..
gi 767904541 225 GQAVIQIAAALGLRTINVVRDRPDIQKLSDRL 256
Cdd:PLN02178 191 GHIAVKIGKAFGLRVTVISRSSEKEREAIDRL 222
PLN02740 PLN02740
Alcohol dehydrogenase-like
87-158 1.91e-04

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 42.86  E-value: 1.91e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP 158
Cdd:PLN02740  24 VMEEIRVDPPQKMEVRIKILYTSICHTDLSAWKGENEAQRAYPRILGHEAAGIVESVGEGVEDLKAGDHVIP 95
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
88-160 3.77e-04

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: 42.21  E-value: 3.77e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767904541  88 LKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPE----LpaVGGNEGVAQVVAVGSNvTGLKPGDWVIPAN 160
Cdd:cd08230   15 VVDIPEPEPTPGEVLVRTLEVGVCGTDREIVAGEYGTAPPgedfL--VLGHEALGVVEEVGDG-SGLSPGDLVVPTV 88
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
90-240 3.85e-04

Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This group includes proteins identified as the Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase. The Arabidopsis enzyme, a member of the medium chain dehydrogenase/reductase family, catalyzes the reduction of 7-8-double bond of phenylpropanal substrates as a plant defense mechanism. Prostaglandins and related eicosanoids (lipid mediators involved in host defense and inflamation) are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. Leukotriene B4 (LTB4) can be metabolized by LTB4 20-hydroxylase in inflamatory cells, and in other cells by bifunctional LTB4 12-HD/PGR. These 15-PGDH and related enzymes are members of the 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 an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176255 [Multi-domain]  Cd Length: 338  Bit Score: 41.92  E-value: 3.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  90 NLELAAVRGS--DVRVKMLAAPINP------SDINMIQGNYGFLPELPAVGGneGVAQVVAvgSNVTGLKPGDWVipanA 161
Cdd:cd08295   27 KLTLKVPPGGsgDVLVKNLYLSCDPymrgrmKGHDDSLYLPPFKPGEVITGY--GVAKVVD--SGNPDFKVGDLV----W 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 162 GLGTWRTEAVFS-EEALIQV-PSDIPLQS-AATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLR 238
Cdd:cd08295   99 GFTGWEEYSLIPrGQDLRKIdHTDVPLSYyLGLLGMPGLTAYAGFYEVCKPKKGETVFVSAASGAVGQLVGQLAKLKGCY 178

                 ..
gi 767904541 239 TI 240
Cdd:cd08295  179 VV 180
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
87-321 4.97e-04

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: 41.71  E-value: 4.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  87 VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQ--GNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV-----IPA 159
Cdd:cd05285   11 RLEERPIPEPGPGEVLVRVRAVGICGSDVHYYKhgRIGDFVVKEPMVLGHESAGTVVAVGSGVTHLKVGDRVaiepgVPC 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 160 N------AGL----------------GTWRTEAVFSEEALIQVPSDIPLQSAA---TLGVNPCTAYRMlmdfeQLQPGDS 214
Cdd:cd05285   91 RtcefckSGRynlcpdmrfaatppvdGTLCRYVNHPADFCHKLPDNVSLEEGAlvePLSVGVHACRRA-----GVRPGDT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 215 V-IQNAsnsG-VGQAVIQIAAALGLRTINVVrdrpDIQKlsDRL---KSLGAEHVI----TEEELRRPEMKNFFKDMpQP 285
Cdd:cd05285  166 VlVFGA---GpIGLLTAAVAKAFGATKVVVT----DIDP--SRLefaKELGATHTVnvrtEDTPESAEKIAELLGGK-GP 235
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 767904541 286 RLALNCVGGKSSTEL-LRQLARGGTMVTyGGMAKQPV 321
Cdd:cd05285  236 DVVIECTGAESCIQTaIYATRPGGTVVL-VGMGKPEV 271
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
100-273 5.45e-04

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: 41.75  E-value: 5.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 100 DVRVKMLAAPINPSDINMIQGnygFLPELPA--VGGNEGVAQVVAVGSNVTGLKPGDWV-IPANAGLGT----------- 165
Cdd:cd08283   27 DAIVRVTATAICGSDLHLYHG---YIPGMKKgdILGHEFMGVVEEVGPEVRNLKVGDRVvVPFTIACGEcfyckrglysq 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541 166 ---------------WRTEAVF---------------------SEEALIQVPSDIPLQSAATLGVNPCTAYrMLMDFEQL 209
Cdd:cd08283  104 cdntnpsaemaklygHAGAGIFgyshltggyaggqaeyvrvpfADVGPFKIPDDLSDEKALFLSDILPTGY-HAAELAEV 182
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767904541 210 QPGDSV-IQNAsnSGVGQAVIQIAAALGLRTINVVrDRPDiqklsDRL----KSLGAEhVITEEELRRP 273
Cdd:cd08283  183 KPGDTVaVWGC--GPVGLFAARSAKLLGAERVIAI-DRVP-----ERLemarSHLGAE-TINFEEVDDV 242
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
199-269 9.49e-04

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 40.76  E-value: 9.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767904541  199 AYRMLMDFEQLQPGDSVIQnASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLsDRLKSLGAEHVITEEE 269
Cdd:pfam00291  42 ALNLLLRLKEGEGGKTVVE-ASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKL-LLMRALGAEVVLVGGD 110
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
100-156 1.29e-03

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 40.55  E-value: 1.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767904541 100 DVRVKMLAAPINPSDINMIQGNYGfLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV 156
Cdd:PLN02514  36 DVVIKVIYCGICHTDLHQIKNDLG-MSNYPMVPGHEVVGEVVEVGSDVSKFTVGDIV 91
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
100-156 4.77e-03

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: 38.37  E-value: 4.77e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767904541 100 DVRVKMLAAPINPSDINMIQ-GNYG-FLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV 156
Cdd:cd08232   23 EVRVRVAAGGICGSDLHYYQhGGFGtVRLREPMVLGHEVSGVVEAVGPGVTGLAPGQRV 81
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
129-156 5.38e-03

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 38.27  E-value: 5.38e-03
                         10        20
                 ....*....|....*....|....*...
gi 767904541 129 PAVGGNEGVAQVVAVGSNVTGLKPGDWV 156
Cdd:PRK05396  58 PMVVGHEFVGEVVEVGSEVTGFKVGDRV 85
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
79-156 8.22e-03

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 37.71  E-value: 8.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904541  79 AVISSAST--VLKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELpaVGGNEGVAQVVAVGSNVTGLKPGDWV 156
Cdd:PRK09422   4 AVVNKDHTgdVVVEKTLRPLKHGEALVKMEYCGVCHTDLHVANGDFGDKTGR--ILGHEGIGIVKEVGPGVTSLKVGDRV 81
 
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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