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Conserved domains on  [gi|1167503283|ref|NP_001336640|]
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enoyl-[acyl-carrier-protein] reductase, mitochondrial isoform b [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 ...
1-297 3.82e-174

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: 484.80  E-value: 3.82e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLP----ELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGLGTWRTEAVFSEEALIQV 76
Cdd:cd08290    36 MLAAPINPADINQIQGVYPIKPpttpEPPAVGGNEGVGEVVKVGSGVKSLKPGDWVIPLRPGLGTWRTHAVVPADDLIKV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  77 PSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLG 156
Cdd:cd08290   116 PNDVDPEQAATLSVNPCTAYRLLEDFVKLQPGDWVIQNGANSAVGQAVIQLAKLLGIKTINVVRDRPDLEELKERLKALG 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 157 AEHVITEEELRRPEMKNFFKDMP--QPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGF 234
Cdd:cd08290   196 ADHVLTEEELRSLLATELLKSAPggRPKLALNCVGGKSATELARLLSPGGTMVTYGGMSGQPVTVPTSLLIFKDITLRGF 275
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167503283 235 WLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQV---PLQDYQSALEASMKPFISSKQILTM 297
Cdd:cd08290   276 WLTRWLKRANPEEKEDMLEELAELIREGKLKAPPVEKVtddPLEEFKDALANALKGGGGGKQVLVM 341
 
Name Accession Description Interval E-value
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
1-297 3.82e-174

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: 484.80  E-value: 3.82e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLP----ELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGLGTWRTEAVFSEEALIQV 76
Cdd:cd08290    36 MLAAPINPADINQIQGVYPIKPpttpEPPAVGGNEGVGEVVKVGSGVKSLKPGDWVIPLRPGLGTWRTHAVVPADDLIKV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  77 PSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLG 156
Cdd:cd08290   116 PNDVDPEQAATLSVNPCTAYRLLEDFVKLQPGDWVIQNGANSAVGQAVIQLAKLLGIKTINVVRDRPDLEELKERLKALG 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 157 AEHVITEEELRRPEMKNFFKDMP--QPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGF 234
Cdd:cd08290   196 ADHVLTEEELRSLLATELLKSAPggRPKLALNCVGGKSATELARLLSPGGTMVTYGGMSGQPVTVPTSLLIFKDITLRGF 275
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167503283 235 WLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQV---PLQDYQSALEASMKPFISSKQILTM 297
Cdd:cd08290   276 WLTRWLKRANPEEKEDMLEELAELIREGKLKAPPVEKVtddPLEEFKDALANALKGGGGGKQVLVM 341
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
1-283 3.63e-70

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: 220.02  E-value: 3.63e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpANAGLGTWRTEAVFSEEALIQVPSDI 80
Cdd:COG0604    34 VKAAGVNPADLLIRRGLYPLPPGLPFIPGSDAAGVVVAVGEGVTGFKVGDRVA-GLGRGGGYAEYVVVPADQLVPLPDGL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  81 PLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRdRPDiqKLsDRLKSLGAEHV 160
Cdd:COG0604   113 SFEEAAALPLAGLTAWQALFDRGRLKPGETVLVHGAAGGVGSAAVQLAKALGARVIATAS-SPE--KA-ELLRALGADHV 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 161 I--TEEELRRPEMKNFFKDmpQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQ 238
Cdd:COG0604   189 IdyREEDFAERVRALTGGR--GVDVVLDTVGGDTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLLLKGLTLTGFTLFA 266
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1167503283 239 WKKDHSPDQFKELIltlcDLIRRGQLTAPACSQVPLQDYQSALEA 283
Cdd:COG0604   267 RDPAERRAALAELA----RLLAAGKLRPVIDRVFPLEEAAEAHRL 307
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
3-282 8.07e-31

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 116.72  E-value: 8.07e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283    3 AAPINPSDINMIQGNYGFLPELpavgGNEGVAQVVAVGSNVTGLKPGDWVIpanaGL--GTWRTEAVFSEEALIQVPSDI 80
Cdd:smart00829   5 AAGLNFRDVLIALGLYPGEAVL----GGECAGVVTRVGPGVTGLAVGDRVM----GLapGAFATRVVTDARLVVPIPDGW 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   81 PLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQAVIQIAAALGLrTINVVRDRPDIQKLsdrLKSLG--A 157
Cdd:smart00829  77 SFEEAATVPVVFLTAYYALVDLARLRPGESVlIHAAA-GGVGQAAIQLARHLGA-EVFATAGSPEKRDF---LRALGipD 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  158 EHVIT------EEELRRpemknffkdMPQPR---LALNCVGGksstELLRQ----LARGGTMVtygGMAKQPVVA--SVS 222
Cdd:smart00829 152 DHIFSsrdlsfADEILR---------ATGGRgvdVVLNSLSG----EFLDAslrcLAPGGRFV---EIGKRDIRDnsQLA 215
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167503283  223 LLIF-KDLKLRGFWLSQWKKDhsPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALE 282
Cdd:smart00829 216 MAPFrPNVSYHAVDLDALEEG--PDRIRELLAEVLELFAEGVLRPLPVTVFPISDAEDAFR 274
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
3-297 2.42e-23

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 97.41  E-value: 2.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGlGTWRTEAVFSEEALIQVPSDIPL 82
Cdd:PTZ00354   37 AAGVNRADTLQRQGKYPPPPGSSEILGLEVAGYVEDVGSDVKRFKEGDRVMALLPG-GGYAEYAVAHKGHVMHIPQGYTF 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  83 QSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKlsdrLKSLGAEHVIt 162
Cdd:PTZ00354  116 EEAAAIPEAFLTAWQLLKKHGDVKKGQSVLIHAGASGVGTAAAQLAEKYGAATIITTSSEEKVDF----CKKLAAIILI- 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 163 eeelRRPEMKNF---FKDMPQPR---LALNCVGGKSSTELLRQLARGGTMVTYGGM--AKQPVVASVSLL------IFKD 228
Cdd:PTZ00354  191 ----RYPDEEGFapkVKKLTGEKgvnLVLDCVGGSYLSETAEVLAVDGKWIVYGFMggAKVEKFNLLPLLrkrasiIFST 266
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167503283 229 LKLRGfwlSQWKKDHSpDQFKELILTlcdLIRRGQLTAPACSQVPLQDYQSA---LEASMKpfiSSKQILTM 297
Cdd:PTZ00354  267 LRSRS---DEYKADLV-ASFEREVLP---YMEEGEIKPIVDRTYPLEEVAEAhtfLEQNKN---IGKVVLTV 328
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
119-252 4.65e-18

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 78.42  E-value: 4.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 119 GVGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSLGAEHVITEEELRRPE-MKNFFKDMpQPRLALNCVG-GKSSTEL 196
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSE---EKL-ELAKELGADHVINPKETDLVEeIKELTGGK-GVDVVFDCVGsPATLEQA 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1167503283 197 LRQLARGGTMVTYgGMAKQPVVASVSLLIFKDLKLRGFWLSqwkkdhSPDQFKELI 252
Cdd:pfam00107  76 LKLLRPGGRVVVV-GLPGGPLPLPLAPLLLKELTILGSFLG------SPEEFPEAL 124
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
70-252 7.82e-11

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: 61.94  E-value: 7.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  70 EEALIQVPSDIPLQSA-ATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIqkl 148
Cdd:TIGR02825 100 EKLLTEWPDTLPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKV--- 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 149 sDRLKSLGAEHVIT-------EEELRR--PEMKNFFKDMpqprlalncVGGKSSTELLRQL------ARGGTMVTYGGMA 213
Cdd:TIGR02825 177 -AYLKKLGFDVAFNyktvkslEETLKKasPDGYDCYFDN---------VGGEFSNTVIGQMkkfgriAICGAISTYNRTG 246
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1167503283 214 KQPVVASVSLLIFKDLKLRGFWLSQWKKDHSPDQFKELI 252
Cdd:TIGR02825 247 PLPPGPPPEIVIYQELRMEGFIVNRWQGEVRQKALKELL 285
 
Name Accession Description Interval E-value
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
1-297 3.82e-174

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: 484.80  E-value: 3.82e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLP----ELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGLGTWRTEAVFSEEALIQV 76
Cdd:cd08290    36 MLAAPINPADINQIQGVYPIKPpttpEPPAVGGNEGVGEVVKVGSGVKSLKPGDWVIPLRPGLGTWRTHAVVPADDLIKV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  77 PSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLG 156
Cdd:cd08290   116 PNDVDPEQAATLSVNPCTAYRLLEDFVKLQPGDWVIQNGANSAVGQAVIQLAKLLGIKTINVVRDRPDLEELKERLKALG 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 157 AEHVITEEELRRPEMKNFFKDMP--QPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGF 234
Cdd:cd08290   196 ADHVLTEEELRSLLATELLKSAPggRPKLALNCVGGKSATELARLLSPGGTMVTYGGMSGQPVTVPTSLLIFKDITLRGF 275
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167503283 235 WLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQV---PLQDYQSALEASMKPFISSKQILTM 297
Cdd:cd08290   276 WLTRWLKRANPEEKEDMLEELAELIREGKLKAPPVEKVtddPLEEFKDALANALKGGGGGKQVLVM 341
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
1-296 1.85e-97

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: 289.56  E-value: 1.85e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPAnAGLGTWRTEAVFSEEALIQVPSDI 80
Cdd:cd05282    33 MLAAPINPSDLITISGAYGSRPPLPAVPGNEGVGVVVEVGSGVSGLLVGQRVLPL-GGEGTWQEYVVAPADDLIPVPDSI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  81 PLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiqKLSDRLKSLGAEHV 160
Cdd:cd05282   112 SDEQAAMLYINPLTAWLMLTEYLKLPPGDWVIQNAANSAVGRMLIQLAKLLGFKTINVVRRD----EQVEELKALGADEV 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 161 ITEEELR-RPEMKNFFKDMPqPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQW 239
Cdd:cd05282   188 IDSSPEDlAQRVKEATGGAG-ARLALDAVGGESATRLARSLRPGGTLVNYGLLSGEPVPFPRSVFIFKDITVRGFWLRQW 266
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1167503283 240 KKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEASMKPFISSKQILT 296
Cdd:cd05282   267 LHSATKEAKQETFAEVIKLVEAGVLTTPVGAKFPLEDFEEAVAAAEQPGRGGKVLLT 323
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
1-283 3.63e-70

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: 220.02  E-value: 3.63e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpANAGLGTWRTEAVFSEEALIQVPSDI 80
Cdd:COG0604    34 VKAAGVNPADLLIRRGLYPLPPGLPFIPGSDAAGVVVAVGEGVTGFKVGDRVA-GLGRGGGYAEYVVVPADQLVPLPDGL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  81 PLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRdRPDiqKLsDRLKSLGAEHV 160
Cdd:COG0604   113 SFEEAAALPLAGLTAWQALFDRGRLKPGETVLVHGAAGGVGSAAVQLAKALGARVIATAS-SPE--KA-ELLRALGADHV 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 161 I--TEEELRRPEMKNFFKDmpQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQ 238
Cdd:COG0604   189 IdyREEDFAERVRALTGGR--GVDVVLDTVGGDTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLLLKGLTLTGFTLFA 266
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1167503283 239 WKKDHSPDQFKELIltlcDLIRRGQLTAPACSQVPLQDYQSALEA 283
Cdd:COG0604   267 RDPAERRAALAELA----RLLAAGKLRPVIDRVFPLEEAAEAHRL 307
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
1-287 5.37e-60

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: 193.70  E-value: 5.37e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPAnAGLGTWRTEAVFSEEALIQVPSDI 80
Cdd:cd08292    35 TTLSPIHNHDLWTIRGTYGYKPELPAIGGSEAVGVVDAVGEGVKGLQVGQRVAVA-PVHGTWAEYFVAPADGLVPLPDGI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  81 PLQSAATLGVNPCTAYrMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLsdrlKSLGAEHV 160
Cdd:cd08292   114 SDEVAAQLIAMPLSAL-MLLDFLGVKPGQWLIQNAAGGAVGKLVAMLAAARGINVINLVRRDAGVAEL----RALGIGPV 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 161 ITEEElrrPEMKNFFKDMPQPRL---ALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLS 237
Cdd:cd08292   189 VSTEQ---PGWQDKVREAAGGAPisvALDSVGGKLAGELLSLLGEGGTLVSFGSMSGEPMQISSGDLIFKQATVRGFWGG 265
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1167503283 238 QWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEASMKP 287
Cdd:cd08292   266 RWSQEMSVEYRKRMIAELLTLALKGQLLLPVEAVFDLGDAAKAAAASMRP 315
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
3-283 4.68e-51

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: 170.76  E-value: 4.68e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpANAGLGTWRTEAVFSEEALIQVPSDIPL 82
Cdd:cd08241    36 AAGVNFPDLLMIQGKYQVKPPLPFVPGSEVAGVVEAVGEGVTGFKVGDRVV-ALTGQGGFAEEVVVPAAAVFPLPDGLSF 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  83 QSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSLGAEHVIT 162
Cdd:cd08241   115 EEAAALPVTYGTAYHALVRRARLQPGETVLVLGAAGGVGLAAVQLAKALGARVIAAASSE---EKL-ALARALGADHVID 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 163 eeeLRRPEMKNFFKDMPQPR---LALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQW 239
Cdd:cd08241   191 ---YRDPDLRERVKALTGGRgvdVVYDPVGGDVFEASLRSLAWGGRLLVIGFASGEIPQIPANLLLLKNISVVGVYWGAY 267
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1167503283 240 KKdHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEA 283
Cdd:cd08241   268 AR-REPELLRANLAELFDLLAEGKIRPHVSAVFPLEQAAEALRA 310
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-252 2.17e-46

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: 157.10  E-value: 2.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANA----------------------G 58
Cdd:cd05188     6 VEAAGLCGTDLHIRRGGYPPPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNlgcgtcelcrelcpgggilgegL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  59 LGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNAsnSGVGQAVIQIAAALGLRTIn 137
Cdd:cd05188    86 DGGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVLKPGDTVlVLGA--GGVGLLAAQLAKAAGARVI- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 138 vVRDRPDiQKLsDRLKSLGAEHVI--TEEELRRPEMKNFFKDmpqPRLALNCVGGKSS-TELLRQLARGGTMVTYGGMAK 214
Cdd:cd05188   163 -VTDRSD-EKL-ELAKELGADHVIdyKEEDLEEELRLTGGGG---ADVVIDAVGGPETlAQALRLLRPGGRIVVVGGTSG 236
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1167503283 215 QPVVASVSLLIFKDLKLRGFWLSqwkkdhSPDQFKELI 252
Cdd:cd05188   237 GPPLDDLRRLLFKELTIIGSTGG------TREDFEEAL 268
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
1-296 1.46e-43

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: 151.22  E-value: 1.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTG-LKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSD 79
Cdd:cd08291    37 VEAAPINPSDLGFLKGQYGSTKALPVPPGFEGSGTVVAAGGGPLAqSLIGKRVAFLAGSYGTYAEYAVADAQQCLPLPDG 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  80 IPLQSAATLGVNPCTAYRMLmDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRdRPDIQKLsdrLKSLGAEH 159
Cdd:cd08291   117 VSFEQGASSFVNPLTALGML-ETAREEGAKAVVHTAAASALGRMLVRLCKADGIKVINIVR-RKEQVDL---LKKIGAEY 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 160 VITEEElrrpemKNFFKDMP------QPRLALNCVGGKSSTELLRQLARGGTMVTYGGM-AKQPVVASVSLLIFKDLKLR 232
Cdd:cd08291   192 VLNSSD------PDFLEDLKeliaklNATIFFDAVGGGLTGQILLAMPYGSTLYVYGYLsGKLDEPIDPVDLIFKNKSIE 265
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167503283 233 GFWLSQWKKDHSPD---QFKELILTlcdlirrgQLTAPACSQVPLQDYQSALEASMKPFISSKQILT 296
Cdd:cd08291   266 GFWLTTWLQKLGPEvvkKLKKLVKT--------ELKTTFASRYPLALTLEAIAFYSKNMSTGKKLLI 324
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
6-280 1.56e-43

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: 151.21  E-value: 1.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   6 INPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI---PANAGL-GTWRTEAVFSEEALIQVPSDIP 81
Cdd:cd08268    39 LNRADAMFRRGAYIEPPPLPARLGYEAAGVVEAVGAGVTGFAVGDRVSvipAADLGQyGTYAEYALVPAAAVVKLPDGLS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  82 LQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiQKlSDRLKSLGAEHVI 161
Cdd:cd08268   119 FVEAAALWMQYLTAYGALVELAGLRPGDSVLITAASSSVGLAAIQIANAAGATVIATTRTS---EK-RDALLALGAAHVI 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 162 --TEEELRRPEMKnfFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQW 239
Cdd:cd08268   195 vtDEEDLVAEVLR--ITGGKGVDVVFDPVGGPQFAKLADALAPGGTLVVYGALSGEPTPFPLKAALKKSLTFRGYSLDEI 272
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1167503283 240 KKDhsPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSA 280
Cdd:cd08268   273 TLD--PEARRRAIAFILDGLASGALKPVVDRVFPFDDIVEA 311
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
3-284 3.64e-38

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: 136.54  E-value: 3.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGNYGFLP--ELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI--PANAGLGTWRTEAVFSEEALIQVPS 78
Cdd:cd05289    36 AAGVNPVDLKIREGLLKAAFplTLPLIPGHDVAGVVVAVGPGVTGFKVGDEVFgmTPFTRGGAYAEYVVVPADELALKPA 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  79 DIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQAVIQIAAALGLRTINVVRDRpdiqkLSDRLKSLGA 157
Cdd:cd05289   116 NLSFEEAAALPLAGLTAWQALFELGGLKAGQTVlIHGAA-GGVGSFAVQLAKARGARVIATASAA-----NADFLRSLGA 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 158 EHVI--TEEELRRPEMKNFFKdmpqprLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASvslliFKDLKLRGFW 235
Cdd:cd05289   190 DEVIdyTKGDFERAAAPGGVD------AVLDTVGGETLARSLALVKPGGRLVSIAGPPPAEQAAK-----RRGVRAGFVF 258
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1167503283 236 LSQwkkdhSPDQFKEliltLCDLIRRGQLTAPACSQVPLQDYQSALEAS 284
Cdd:cd05289   259 VEP-----DGEQLAE----LAELVEAGKLRPVVDRVFPLEDAAEAHERL 298
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
2-283 5.22e-34

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 126.38  E-value: 5.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   2 LAAPINPSDINMIQGNYGfLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI-----------------------PANAG 58
Cdd:COG1064    33 EACGVCHSDLHVAEGEWP-VPKLPLVPGHEIVGRVVAVGPGVTGFKVGDRVGvgwvdscgtceycrsgrenlcenGRFTG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  59 LGTW---RTEAVFSEEALIQVPSDIPLQSAATLGvnpC---TAYRMLMDFEqLQPGDSV-IQNAsnSGVGQAVIQIAAAL 131
Cdd:COG1064   112 YTTDggyAEYVVVPARFLVKLPDGLDPAEAAPLL---CagiTAYRALRRAG-VGPGDRVaVIGA--GGLGHLAVQIAKAL 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 132 GLRTInVVrDRPDiQKLsDRLKSLGAEHVITEEElrRPEMKNfFKDMPQPRLALNCVGGKSSTEL-LRQLARGGTMVTyG 210
Cdd:COG1064   186 GAEVI-AV-DRSP-EKL-ELARELGADHVVNSSD--EDPVEA-VRELTGADVVIDTVGAPATVNAaLALLRRGGRLVL-V 257
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167503283 211 GMAKQPVVASVSLLIFKDLKLRGfwlSQWkkdHSPDQFKELIltlcDLIRRGQLTaPACSQVPLQDYQSALEA 283
Cdd:COG1064   258 GLPGGPIPLPPFDLILKERSIRG---SLI---GTRADLQEML----DLAAEGKIK-PEVETIPLEEANEALER 319
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
3-297 1.37e-33

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: 125.00  E-value: 1.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGL----GTWRTEAVFSEEALIQVPS 78
Cdd:cd08253    36 ASGVNPVDTYIRAGAYPGLPPLPYVPGSDGAGVVEAVGEGVDGLKVGDRVWLTNLGWgrrqGTAAEYVVVPADQLVPLPD 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  79 DIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQklsdRLKSLGAE 158
Cdd:cd08253   116 GVSFEQGAALGIPALTAYRALFHRAGAKAGETVLVHGGSGAVGHAAVQLARWAGARVIATASSAEGAE----LVRQAGAD 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 159 HVI--TEEELrRPEMKNfFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLiFKDLKLRGFWL 236
Cdd:cd08253   192 AVFnyRAEDL-ADRILA-ATAGQGVDVIIEVLANVNLAKDLDVLAPGGRIVVYGSGGLRGTIPINPLM-AKEASIRGVLL 268
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167503283 237 SQwkkdHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEASMKPFISSKQILTM 297
Cdd:cd08253   269 YT----ATPEERAAAAEAIAAGLADGALRPVIAREYPLEEAAAAHEAVESGGAIGKVVLDP 325
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
3-282 4.83e-33

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: 123.91  E-value: 4.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpANAGLGTWRTE----------------- 65
Cdd:cd08266    36 AAALNHLDLWVRRGMPGIKLPLPHILGSDGAGVVEAVGPGVTNVKPGQRVV-IYPGISCGRCEyclagrenlcaqygilg 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  66 ----------AVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRT 135
Cdd:cd08266   115 ehvdggyaeyVAVPARNLLPIPDNLSFEEAAAAPLTFLTAWHMLVTRARLRPGETVLVHGAGSGVGSAAIQIAKLFGATV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 136 INVVRDRpdiQKLsDRLKSLGAEHVI--TEEELRRPEMKNFFKdmpqpRLA---LNCVGGKSSTELLRQLARGGTMVTYG 210
Cdd:cd08266   195 IATAGSE---DKL-ERAKELGADYVIdyRKEDFVREVRELTGK-----RGVdvvVEHVGAATWEKSLKSLARGGRLVTCG 265
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167503283 211 GMAKQPVVASVSLLIFKDLKLRGFWLSqwkkdhSPDQFKELIltlcDLIRRGQLTAPACSQVPLQDYQSALE 282
Cdd:cd08266   266 ATTGYEAPIDLRHVFWRQLSILGSTMG------TKAELDEAL----RLVFRGKLKPVIDSVFPLEEAAEAHR 327
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-283 1.25e-31

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: 120.06  E-value: 1.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVipanAGL---GTWRTEAVFSEEALIQVP 77
Cdd:cd08273    34 VEASGVSFADVQMRRGLYPDQPPLPFTPGYDLVGRVDALGSGVTGFEVGDRV----AALtrvGGNAEYINLDAKYLVPVP 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  78 SDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQAVIQIAAALGLRTINVVRDRpdiqkLSDRLKSLG 156
Cdd:cd08273   110 EGVDAAEAVCLVLNYVTAYQMLHRAAKVLTGQRVlIHGAS-GGVGQALLELALLAGAEVYGTASER-----NHAALRELG 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 157 AEHViteeeLRRPemKNFFKDMPQPRLA---LNCVGGKSSTELLRQLARGGTMVTYG-------GMAKQPVVASVSLLIF 226
Cdd:cd08273   184 ATPI-----DYRT--KDWLPAMLTPGGVdvvFDGVGGESYEESYAALAPGGTLVCYGgnssllqGRRSLAALGSLLARLA 256
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167503283 227 K------DLKLRGFWLSQWKKDHsPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEA 283
Cdd:cd08273   257 KlkllptGRRATFYYVWRDRAED-PKLFRQDLTELLDLLAKGKIRPKIAKRLPLSEVAEAHRL 318
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
3-282 8.07e-31

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 116.72  E-value: 8.07e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283    3 AAPINPSDINMIQGNYGFLPELpavgGNEGVAQVVAVGSNVTGLKPGDWVIpanaGL--GTWRTEAVFSEEALIQVPSDI 80
Cdd:smart00829   5 AAGLNFRDVLIALGLYPGEAVL----GGECAGVVTRVGPGVTGLAVGDRVM----GLapGAFATRVVTDARLVVPIPDGW 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   81 PLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQAVIQIAAALGLrTINVVRDRPDIQKLsdrLKSLG--A 157
Cdd:smart00829  77 SFEEAATVPVVFLTAYYALVDLARLRPGESVlIHAAA-GGVGQAAIQLARHLGA-EVFATAGSPEKRDF---LRALGipD 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  158 EHVIT------EEELRRpemknffkdMPQPR---LALNCVGGksstELLRQ----LARGGTMVtygGMAKQPVVA--SVS 222
Cdd:smart00829 152 DHIFSsrdlsfADEILR---------ATGGRgvdVVLNSLSG----EFLDAslrcLAPGGRFV---EIGKRDIRDnsQLA 215
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167503283  223 LLIF-KDLKLRGFWLSQWKKDhsPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALE 282
Cdd:smart00829 216 MAPFrPNVSYHAVDLDALEEG--PDRIRELLAEVLELFAEGVLRPLPVTVFPISDAEDAFR 274
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
1-283 9.77e-27

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: 106.11  E-value: 9.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLPELPavgGNEGVAQVVAVGSNVTGLKPGDWVipanAGL--GTWRTEAVFSEEALIQVPS 78
Cdd:cd05195     7 VKAAGLNFRDVLVALGLLPGDETPL---GLECSGIVTRVGSGVTGLKVGDRV----MGLapGAFATHVRVDARLVVKIPD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  79 DIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQAVIQIAAALGLRTINVVRDRPDIqklsDRLKSLG- 156
Cdd:cd05195    80 SLSFEEAATLPVAYLTAYYALVDLARLQKGESVlIHAAA-GGVGQAAIQLAQHLGAEVFATVGSEEKR----EFLRELGg 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 157 -AEHVITEeelRRPEMKNFFKDMPQPR---LALNCVGGKSSTELLRQLARGGTMVtygGMAKQPVVA--SVSLLIF-KDL 229
Cdd:cd05195   155 pVDHIFSS---RDLSFADGILRATGGRgvdVVLNSLSGELLRASWRCLAPFGRFV---EIGKRDILSnsKLGMRPFlRNV 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1167503283 230 KLRGFWLSQWKKdHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEA 283
Cdd:cd05195   229 SFSSVDLDQLAR-ERPELLRELLREVLELLEAGVLKPLPPTVVPSASEIDAFRL 281
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
3-286 3.58e-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: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 104.99  E-value: 3.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGN-YGFLPE-LPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANA--GLGTWRTEAVFSEEALIQVPS 78
Cdd:cd08267    35 AASVNPVDWKLRRGPpKLLLGRpFPPIPGMDFAGEVVAVGSGVTRFKVGDEVFGRLPpkGGGALAEYVVAPESGLAKKPE 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  79 DIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiqKLsDRLKSLGAE 158
Cdd:cd08267   115 GVSFEEAAALPVAGLTALQALRDAGKVKPGQRVLINGASGGVGTFAVQIAKALGAHVTGVCSTR----NA-ELVRSLGAD 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 159 HVI--TEEelrrpemkNFFKDMPQPR---LALNCVGGKSST--ELLRQLARGGTMVTYGGMAKQPVVASVSLLIFkdlkl 231
Cdd:cd08267   190 EVIdyTTE--------DFVALTAGGEkydVIFDAVGNSPFSlyRASLALKPGGRYVSVGGGPSGLLLVLLLLPLT----- 256
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1167503283 232 rGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEASMK 286
Cdd:cd08267   257 -LGGGGRRLKFFLAKPNAEDLEQLAELVEEGKLKPVIDSVYPLEDAPEAYRRLKS 310
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
3-283 1.00e-25

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: 103.67  E-value: 1.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGNYGflPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAgLGTWRTEAVFSEEALIQVPSDIPL 82
Cdd:cd05286    35 AIGVNFIDTYFRSGLYP--LPLPFVLGVEGAGVVEAVGPGVTGFKVGDRVAYAGP-PGAYAEYRVVPASRLVKLPDGISD 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  83 QSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVrDRPDIQKLSdrlKSLGAEHVI- 161
Cdd:cd05286   112 ETAAALLLQGLTAHYLLRETYPVKPGDTVLVHAAAGGVGLLLTQWAKALGATVIGTV-SSEEKAELA---RAAGADHVIn 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 162 -TEEELrRPEMKnffkdmpqpRL--------ALNCVGGKSSTELLRQLARGGTMVTYgGMAKQPVVA-SVSLLIFKDLKL 231
Cdd:cd05286   188 yRDEDF-VERVR---------EItggrgvdvVYDGVGKDTFEGSLDSLRPRGTLVSF-GNASGPVPPfDLLRLSKGSLFL 256
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1167503283 232 -RGfwlSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDY---QSALEA 283
Cdd:cd05286   257 tRP---SLFHYIATREELLARAAELFDAVASGKLKVEIGKRYPLADAaqaHRDLES 309
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
3-282 1.95e-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: 102.90  E-value: 1.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGNYGFLPELPAVGGNEgVA-QVVAVGSNVTGLKPGDWVipanAGL---GTWRTEAVFSEEALIQVPS 78
Cdd:cd05276    36 AAGVNRADLLQRQGLYPPPPGASDILGLE-VAgVVVAVGPGVTGWKVGDRV----CALlagGGYAEYVVVPAGQLLPVPE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  79 DIPLQSAATLgvnP---CTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSL 155
Cdd:cd05276   111 GLSLVEAAAL---PevfFTAWQNLFQLGGLKAGETVLIHGGASGVGTAAIQLAKALGARVIATAGSE---EKL-EACRAL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 156 GAEHVITeeelRRPEmkNF---FKDMPQPR---LALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDL 229
Cdd:cd05276   184 GADVAIN----YRTE--DFaeeVKEATGGRgvdVILDMVGGDYLARNLRALAPDGRLVLIGLLGGAKAELDLAPLLRKRL 257
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1167503283 230 KLRGFWL-SQwkkdhsPDQFK-----ELILTLCDLIRRGQLTAPACSQVPLQDYQSALE 282
Cdd:cd05276   258 TLTGSTLrSR------SLEEKaalaaAFREHVWPLFASGRIRPVIDKVFPLEEAAEAHR 310
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
3-233 3.91e-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: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 102.61  E-value: 3.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP---------------ANAGL-----GTW 62
Cdd:cd08276    36 AVSLNYRDLLILNGRYPPPVKDPLIPLSDGAGEVVAVGEGVTRFKVGDRVVPtffpnwldgpptaedEASALggpidGVL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  63 RTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQnaSNSGVGQAVIQIAAALGLRTINVVRD 141
Cdd:cd08276   116 AEYVVLPEEGLVRAPDHLSFEEAATLPCAGLTAWNALFGLGPLKPGDTVlVQ--GTGGVSLFALQFAKAAGARVIATSSS 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 142 RpdiQKLsDRLKSLGAEHVIT-------EEELRRpemknffkdMPQPR---LALNCVGGKSSTELLRQLARGGTMVTYGG 211
Cdd:cd08276   194 D---EKL-ERAKALGADHVINyrttpdwGEEVLK---------LTGGRgvdHVVEVGGPGTLAQSIKAVAPGGVISLIGF 260
                         250       260
                  ....*....|....*....|..
gi 1167503283 212 MAKQPVVASVSLLIFKDLKLRG 233
Cdd:cd08276   261 LSGFEAPVLLLPLLTKGATLRG 282
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
3-211 1.27e-24

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: 101.12  E-value: 1.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpanaGL---GTWRTEAVFSEEALIQVPSD 79
Cdd:cd08275    35 ACGLNFADLMARQGLYDSAPKPPFVPGFECAGTVEAVGEGVKDFKVGDRVM----GLtrfGGYAEVVNVPADQVFPLPDG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  80 IPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQAVIQIAAAlgLRTINVVRDrPDIQKLsDRLKSLGAE 158
Cdd:cd08275   111 MSFEEAAAFPVNYLTAYYALFELGNLRPGQSVlVHSAA-GGVGLAAGQLCKT--VPNVTVVGT-ASASKH-EALKENGVT 185
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1167503283 159 HVITEEELR-RPEMKNFfkdMPQP-RLALNCVGGKSSTELLRQLARGGTMVTYGG 211
Cdd:cd08275   186 HVIDYRTQDyVEEVKKI---SPEGvDIVLDALGGEDTRKSYDLLKPMGRLVVYGA 237
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
3-265 1.88e-24

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: 100.33  E-value: 1.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGL----GTWRTEAVFSEEALIQVPS 78
Cdd:cd08272    36 ASGVNPLDTKIRRGGAAARPPLPAILGCDVAGVVEAVGEGVTRFRVGDEVYGCAGGLgglqGSLAEYAVVDARLLALKPA 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  79 DIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiqKLsDRLKSLGAE 158
Cdd:cd08272   116 NLSMREAAALPLVGITAWEGLVDRAAVQAGQTVLIHGGAGGVGHVAVQLAKAAGARVYATASSE----KA-AFARSLGAD 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 159 HVI------TEEELRRPEMKNFfkdmpqpRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQpvvaSVSLLIFKDLKLR 232
Cdd:cd08272   191 PIIyyretvVEYVAEHTGGRGF-------DVVFDTVGGETLDASFEAVALYGRVVSILGGATH----DLAPLSFRNATYS 259
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1167503283 233 G-FWLSQWKKDHSPDQFKELILTLCDLIRRGQLT 265
Cdd:cd08272   260 GvFTLLPLLTGEGRAHHGEILREAARLVERGQLR 293
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
9-233 4.22e-24

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: 99.92  E-value: 4.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   9 SDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGD-----WVIPA-------------------NAGL---GT 61
Cdd:cd08297    41 TDLHAALGDWPVKPKLPLIGGHEGAGVVVAVGPGVSGLKVGDrvgvkWLYDAcgkceycrtgdetlcpnqkNSGYtvdGT 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  62 WRTEAVFSEEALIQVPSDIPLQSAATL---GVnpcTAYRMLMDfEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINV 138
Cdd:cd08297   121 FAEYAIADARYVTPIPDGLSFEQAAPLlcaGV---TVYKALKK-AGLKPGDWVVISGAGGGLGHLGVQYAKAMGLRVIAI 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 139 -VRDRPdiQKLSdrlKSLGAEHVIteeelrrpemkNFFKDMPQPRL-----------ALNCVGGKSSTEL-LRQLARGGT 205
Cdd:cd08297   197 dVGDEK--LELA---KELGADAFV-----------DFKKSDDVEAVkeltggggahaVVVTAVSAAAYEQaLDYLRPGGT 260
                         250       260
                  ....*....|....*....|....*...
gi 1167503283 206 MVTYGGMAKQPVVASVSLLIFKDLKLRG 233
Cdd:cd08297   261 LVCVGLPPGGFIPLDPFDLVLRGITIVG 288
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
3-208 5.27e-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: 99.58  E-value: 5.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQgnYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI-------PANAGLGTWRTEAVFSEEALIQ 75
Cdd:cd08249    35 AVALNPVDWKHQD--YGFIPSYPAILGCDFAGTVVEVGSGVTRFKVGDRVAgfvhggnPNDPRNGAFQEYVVADADLTAK 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  76 VPSDIPLQSAATLGVNPCTA-----YRMLMDF-----EQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVrdrpdi 145
Cdd:cd08249   113 IPDNISFEEAATLPVGLVTAalalfQKLGLPLpppkpSPASKGKPVLIWGGSSSVGTLAIQLAKLAGYKVITTA------ 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167503283 146 qklS----DRLKSLGAEHVI------TEEELRRPEMKNFfkdmpqpRLALNCVGGKSSTELLRQL---ARGGTMVT 208
Cdd:cd08249   187 ---SpknfDLVKSLGADAVFdyhdpdVVEDIRAATGGKL-------RYALDCISTPESAQLCAEAlgrSGGGKLVS 252
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
9-287 1.19e-23

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: 98.67  E-value: 1.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   9 SDINMIQGNYGFLPElPAVGGNEGVAQVVAVGSNVTGLKPGDWVI---------------------PANAGLGTWRTEAV 67
Cdd:COG1063    39 SDLHIYRGGYPFVRP-PLVLGHEFVGEVVEVGEGVTGLKVGDRVVvepnipcgecrycrrgrynlcENLQFLGIAGRDGG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  68 FSE------EALIQVPSDIPLQSAATlgVNP-CTAYRMLMDFeQLQPGDSV-IQNAsnsG-VGQAVIQIAAALGLRTINV 138
Cdd:COG1063   118 FAEyvrvpaANLVKVPDGLSDEAAAL--VEPlAVALHAVERA-GVKPGDTVlVIGA---GpIGLLAALAARLAGAARVIV 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 139 VRDRPDiqKLsDRLKSLGAEHVITeeeLRRPEMKNFFKDMPQPR---LALNCVGGKSS-TELLRQLARGGTMVTYGGMAK 214
Cdd:COG1063   192 VDRNPE--RL-ELARELGADAVVN---PREEDLVEAVRELTGGRgadVVIEAVGAPAAlEQALDLVRPGGTVVLVGVPGG 265
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167503283 215 qPVVASVSLLIFKDLKLRGFWLsqwkkdHSPDQFKELIltlcDLIRRGQL-TAPACS-QVPLQDYQSALEASMKP 287
Cdd:COG1063   266 -PVPIDLNALVRKELTLRGSRN------YTREDFPEAL----ELLASGRIdLEPLIThRFPLDDAPEAFEAAADR 329
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
3-297 2.42e-23

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 97.41  E-value: 2.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGlGTWRTEAVFSEEALIQVPSDIPL 82
Cdd:PTZ00354   37 AAGVNRADTLQRQGKYPPPPGSSEILGLEVAGYVEDVGSDVKRFKEGDRVMALLPG-GGYAEYAVAHKGHVMHIPQGYTF 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  83 QSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKlsdrLKSLGAEHVIt 162
Cdd:PTZ00354  116 EEAAAIPEAFLTAWQLLKKHGDVKKGQSVLIHAGASGVGTAAAQLAEKYGAATIITTSSEEKVDF----CKKLAAIILI- 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 163 eeelRRPEMKNF---FKDMPQPR---LALNCVGGKSSTELLRQLARGGTMVTYGGM--AKQPVVASVSLL------IFKD 228
Cdd:PTZ00354  191 ----RYPDEEGFapkVKKLTGEKgvnLVLDCVGGSYLSETAEVLAVDGKWIVYGFMggAKVEKFNLLPLLrkrasiIFST 266
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167503283 229 LKLRGfwlSQWKKDHSpDQFKELILTlcdLIRRGQLTAPACSQVPLQDYQSA---LEASMKpfiSSKQILTM 297
Cdd:PTZ00354  267 LRSRS---DEYKADLV-ASFEREVLP---YMEEGEIKPIVDRTYPLEEVAEAhtfLEQNKN---IGKVVLTV 328
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
19-283 2.99e-23

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: 97.39  E-value: 2.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  19 GFLP--ELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP-ANAGLGTWR-------------------TEAVFSEEA---- 72
Cdd:cd08259    47 GFFPrgKYPLILGHEIVGTVEEVGEGVERFKPGDRVILyYYIPCGKCEyclsgeenlcrnraeygeeVDGGFAEYVkvpe 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  73 --LIQVPSDIPLQSAATLGVNPCTAYRMLmDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiQKLsD 150
Cdd:cd08259   127 rsLVKLPDNVSDESAALAACVVGTAVHAL-KRAGVKKGDTVLVTGAGGGVGIHAIQLAKALGARVIAVTRSP---EKL-K 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 151 RLKSLGAEHVIT----EEElrrpemknfFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIF 226
Cdd:cd08259   202 ILKELGADYVIDgskfSED---------VKKLGGADVVIELVGSPTIEESLRSLNKGGRLVLIGNVTPDPAPLRPGLLIL 272
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1167503283 227 KDLKLRGfwlsqwkkdHSPDQFKELILTLcDLIRRGQLTAPACSQVPLQDYQSALEA 283
Cdd:cd08259   273 KEIRIIG---------SISATKADVEEAL-KLVKEGKIKPVIDRVVSLEDINEALED 319
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
3-296 9.98e-22

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 93.11  E-value: 9.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGNYGfLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVipanAGLGTWRTEAVFSE------EALIQV 76
Cdd:cd08271    36 AAGLNPVDWKVIAWGPP-AWSYPHVPGVDGAGVVVAVGAKVTGWKVGDRV----AYHASLARGGSFAEytvvdaRAVLPL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  77 PSDIPLQSAATLgvnPC---TAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPdiqklSDRLK 153
Cdd:cd08271   111 PDSLSFEEAAAL---PCaglTAYQALFKKLRIEAGRTILITGGAGGVGSFAVQLAKRAGLRVITTCSKRN-----FEYVK 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 154 SLGAEHVITEeelRRPEMKNFFKDMPQPR---LALNCVGGKSSTELLRQLARGGTMVT-YGGMAKQPVVASVSLLIFKDL 229
Cdd:cd08271   183 SLGADHVIDY---NDEDVCERIKEITGGRgvdAVLDTVGGETAAALAPTLAFNGHLVCiQGRPDASPDPPFTRALSVHEV 259
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 230 KLRGFWLSQwkkdhSPDQFKELILT---LCDLIRRGQLTAPACSQVPLQDYQSALEASMKPFISSKQILT 296
Cdd:cd08271   260 ALGAAHDHG-----DPAAWQDLRYAgeeLLELLAAGKLEPLVIEVLPFEQLPEALRALKDRHTRGKIVVT 324
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
1-264 1.03e-21

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: 93.37  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFlpELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI--------------------------- 53
Cdd:cd08279    32 IAAAGLCHSDLHVVTGDLPA--PLPAVLGHEGAGVVEEVGPGVTGVKPGDHVVlswipacgtcrycsrgqpnlcdlgagi 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  54 -------------------PANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLG----------VNpcTAyrmlmdfeQ 104
Cdd:cd08279   110 lggqlpdgtrrftadgepvGAMCGLGTFAEYTVVPEASVVKIDDDIPLDRAALLGcgvttgvgavVN--TA--------R 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 105 LQPGDS--VIqnaSNSGVGQAVIQIAAALGLRTINVVrDrPDIQKLsDRLKSLGAEHVITEEElrrPEMKNFFKDMPQPR 182
Cdd:cd08279   180 VRPGDTvaVI---GCGGVGLNAIQGARIAGASRIIAV-D-PVPEKL-ELARRFGATHTVNASE---DDAVEAVRDLTDGR 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 183 L---ALNCVGGKSSTEL-LRQLARGGTMVTYGGMAKQPVVA-SVSLLIFKDLKLRGFWL--SQWKKDhspdqfkelILTL 255
Cdd:cd08279   251 GadyAFEAVGRAATIRQaLAMTRKGGTAVVVGMGPPGETVSlPALELFLSEKRLQGSLYgsANPRRD---------IPRL 321

                  ....*....
gi 1167503283 256 CDLIRRGQL 264
Cdd:cd08279   322 LDLYRAGRL 330
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
6-264 5.82e-21

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: 90.78  E-value: 5.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   6 INPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVipANAGLGTWRTEAVFSEEALIQVPSDIPlqSA 85
Cdd:cd08250    42 INASDINFTAGRYDPGVKPPFDCGFEGVGEVVAVGEGVTDFKVGDAV--ATMSFGAFAEYQVVPARHAVPVPELKP--EV 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  86 ATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVrDRPDIQKLsdrLKSLGAEHVI--TE 163
Cdd:cd08250   118 LPLLVSGLTASIALEEVGEMKSGETVLVTAAAGGTGQFAVQLAKLAGCHVIGTC-SSDEKAEF---LKSLGCDRPInyKT 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 164 EELRRPEMKNFfkdmpqPR---LALNCVGGKSSTELLRQLARGGTMVTYGGMA-----KQPVVASVSLLIFKDLK----L 231
Cdd:cd08250   194 EDLGEVLKKEY------PKgvdVVYESVGGEMFDTCVDNLALKGRLIVIGFISgyqsgTGPSPVKGATLPPKLLAksasV 267
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1167503283 232 RGFWLSQWKKDhspdqFKELILTLCDLIRRGQL 264
Cdd:cd08250   268 RGFFLPHYAKL-----IPQHLDRLLQLYQRGKL 295
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
3-233 7.65e-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: 90.49  E-value: 7.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGnYGFLPeLPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPAN-----------------------AGL 59
Cdd:cd08264    35 MAGVNPVDYNVINA-VKVKP-MPHIPGAEFAGVVEEVGDHVKGVKKGDRVVVYNrvfdgtcdmclsgnemlcrnggiIGV 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  60 GT---WRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEqLQPGDSVIQNASNSGVGQAVIQIAAALGLRTI 136
Cdd:cd08264   113 VSnggYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYHALKTAG-LGPGETVVVFGASGNTGIFAVQLAKMMGAEVI 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 137 NVVRdrpdiqklSDRLKSLGAEHVITEEELRrPEMKNFFKdmpQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQP 216
Cdd:cd08264   192 AVSR--------KDWLKEFGADEVVDYDEVE-EKVKEITK---MADVVINSLGSSFWDLSLSVLGRGGRLVTFGTLTGGE 259
                         250
                  ....*....|....*..
gi 1167503283 217 VVASVSLLIFKDLKLRG 233
Cdd:cd08264   260 VKLDLSDLYSKQISIIG 276
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
9-233 1.79e-20

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 89.76  E-value: 1.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   9 SDINMIQGNYGFLpeLPAVGGNEGVAQVVAVGSNVTGLKPGDWVI-------------------------PANA------ 57
Cdd:COG1062    31 SDLHVRDGDLPVP--LPAVLGHEGAGVVEEVGPGVTGVAPGDHVVlsfipscghcrycasgrpalceagaALNGkgtlpd 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  58 -----------------GLGTWRTEAVFSEEALIQVPSDIPLQSAATLG----------VNpcTAyrmlmdfeQLQPGDS 110
Cdd:COG1062   109 gtsrlssadgepvghffGQSSFAEYAVVPERSVVKVDKDVPLELAALLGcgvqtgagavLN--TA--------KVRPGDT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 111 VIqnasnsGVGQAVIQIAAALGLRTINVVrdrpDIqkLSDRL---KSLGAEHVI--TEEElrrpemknffkdmPQPRL-- 183
Cdd:COG1062   179 VAvfg-lgGVGLSAVQGARIAGASRIIAV----DP--VPEKLelaRELGATHTVnpADED-------------AVEAVre 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167503283 184 --------ALNCVGgksSTELLRQ----LARGGTMVTYG-GMAKQPVVASVSLLIFKDLKLRG 233
Cdd:COG1062   239 ltgggvdyAFETTG---NPAVIRQaleaLRKGGTVVVVGlAPPGAEISLDPFQLLLTGRTIRG 298
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
6-233 5.48e-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: 85.29  E-value: 5.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   6 INPSDINMIQGNYGFLPELPAVGGNEGVAQVVAvgSNVTGLKPGDWVIPANAGLG--TWRTeavFSEeaLIQVPSD---- 79
Cdd:cd05280    39 LNYKDALAATGNGGVTRNYPHTPGIDAAGTVVS--SDDPRFREGDEVLVTGYDLGmnTDGG---FAE--YVRVPADwvvp 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  80 IP----LQSAATLGVNPCTAYRMLMDFEQ--LQPGDSVIQ-NASNSGVGQAVIQIAAALGLRTINVVRDrpdiQKLSDRL 152
Cdd:cd05280   112 LPeglsLREAMILGTAGFTAALSVHRLEDngQTPEDGPVLvTGATGGVGSIAVAILAKLGYTVVALTGK----EEQADYL 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 153 KSLGAEHVITEEEL----RRPEMKNFFKdmpqprLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIfkd 228
Cdd:cd05280   188 KSLGASEVLDREDLldesKKPLLKARWA------GAIDTVGGDVLANLLKQTKYGGVVASCGNAAGPELTTTVLPFI--- 258

                  ....*
gi 1167503283 229 lkLRG 233
Cdd:cd05280   259 --LRG 261
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
9-233 2.35e-18

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: 83.52  E-value: 2.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   9 SDINMIQGNYGFlPELPAVGGNEGVAQVVAVGSNVTGLKPGD-----WVIPA-------------------NAGL---GT 61
Cdd:cd08245    39 TDLHAAEGDWGG-SKYPLVPGHEIVGEVVEVGAGVEGRKVGDrvgvgWLVGScgrceycrrglenlcqkavNTGYttqGG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  62 WRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEqLQPGDSV----IqnasnSGVGQAVIQIAAALGLRTIN 137
Cdd:cd08245   118 YAEYMVADAEYTVLLPDGLPLAQAAPLLCAGITVYSALRDAG-PRPGERVavlgI-----GGLGHLAVQYARAMGFETVA 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 138 VVRDrPDIQKLSdrlKSLGAEHVI-TEEELRRPEMKNFFkdmpqpRLALNCV-GGKSSTELLRQLARGGTMVTYGGMAKQ 215
Cdd:cd08245   192 ITRS-PDKRELA---RKLGADEVVdSGAELDEQAAAGGA------DVILVTVvSGAAAEAALGGLRRGGRIVLVGLPESP 261
                         250
                  ....*....|....*...
gi 1167503283 216 PVVASVSLLIFKDLKLRG 233
Cdd:cd08245   262 PFSPDIFPLIMKRQSIAG 279
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
119-252 4.65e-18

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 78.42  E-value: 4.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 119 GVGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSLGAEHVITEEELRRPE-MKNFFKDMpQPRLALNCVG-GKSSTEL 196
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSE---EKL-ELAKELGADHVINPKETDLVEeIKELTGGK-GVDVVFDCVGsPATLEQA 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1167503283 197 LRQLARGGTMVTYgGMAKQPVVASVSLLIFKDLKLRGFWLSqwkkdhSPDQFKELI 252
Cdd:pfam00107  76 LKLLRPGGRVVVV-GLPGGPLPLPLAPLLLKELTILGSFLG------SPEEFPEAL 124
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
38-297 6.73e-18

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


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 82.03  E-value: 6.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  38 AVGSNVTGLKPGdwvipanaglGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQpGDSVIQNASN 117
Cdd:cd08270    74 AVGARVVGLGAM----------GAWAELVAVPTGWLAVLPDGVSFAQAATLPVAGVTALRALRRGGPLL-GRRVLVTGAS 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 118 SGVGQAVIQIAAALGLRTINVVRDRPDiqklSDRLKSLGAEH-VITEEELRRPEMKnffkdmpqprLALNCVGGKSSTEL 196
Cdd:cd08270   143 GGVGRFAVQLAALAGAHVVAVVGSPAR----AEGLRELGAAEvVVGGSELSGAPVD----------LVVDSVGGPQLARA 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 197 LRQLARGGTMVTYGGMAKQPVVASVSLLIFK--DLKLRGFWLSQwKKDHSPDqfkelILTLCDLIRRGQLTAPACSQVPL 274
Cdd:cd08270   209 LELLAPGGTVVSVGSSSGEPAVFNPAAFVGGggGRRLYTFFLYD-GEPLAAD-----LARLLGLVAAGRLDPRIGWRGSW 282
                         250       260
                  ....*....|....*....|...
gi 1167503283 275 QDYQSALEASMKPFISSKQILTM 297
Cdd:cd08270   283 TEIDEAAEALLARRFRGKAVLDV 305
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
9-283 1.32e-17

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: 81.52  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   9 SDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI--------------------------PANAGLGTW 62
Cdd:cd08254    41 SDLHILDGGVPTLTKLPLTLGHEIAGTVVEVGAGVTNFKVGDRVAvpavipcgacalcrrgrgnlclnqgmPGLGIDGGF 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  63 RTEAVFSEEALIQVPSDIPLQ--SAATLGVNpcTAYRMLMDFEQLQPGDSV-IQNAsnSGVGQAVIQIAAALGLRTINVV 139
Cdd:cd08254   121 AEYIVVPARALVPVPDGVPFAqaAVATDAVL--TPYHAVVRAGEVKPGETVlVIGL--GGLGLNAVQIAKAMGAAVIAVD 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 140 RDRpdiQKLsDRLKSLGA-EHVITEEELRRPEMKNffkdmPQPR---LALNCVGGKSSTEL-LRQLARGGTMVTYG-GMA 213
Cdd:cd08254   197 IKE---EKL-ELAKELGAdEVLNSLDDSPKDKKAA-----GLGGgfdVIFDFVGTQPTFEDaQKAVKPGGRIVVVGlGRD 267
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 214 KQPVvaSVSLLIFKDLKLRGFWlsqwkkDHSPDQFKELIltlcDLIRRGQLTaPACSQVPLQDYQSALEA 283
Cdd:cd08254   268 KLTV--DLSDLIARELRIIGSF------GGTPEDLPEVL----DLIAKGKLD-PQVETRPLDEIPEVLER 324
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
19-242 2.74e-17

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 80.47  E-value: 2.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  19 GFLP--ELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPA-NAGLGTW-----------RTEAVFSEE------------- 71
Cdd:PRK13771   47 GFYPrmKYPVILGHEVVGTVEEVGENVKGFKPGDRVASLlYAPDGTCeycrsgeeaycKNRLGYGEEldgffaeyakvkv 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  72 -ALIQVPSDIPLQSAAtlgVNPC---TAYRMLMDFEqLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDrpdiqk 147
Cdd:PRK13771  127 tSLVKVPPNVSDEGAV---IVPCvtgMVYRGLRRAG-VKKGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSS------ 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 148 lSDRLKSLG--AEHVITEEELRRpEMKNFfkdmPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVA-SVSLL 224
Cdd:PRK13771  197 -ESKAKIVSkyADYVIVGSKFSE-EVKKI----GGADIVIETVGTPTLEESLRSLNMGGKIIQIGNVDPSPTYSlRLGYI 270
                         250
                  ....*....|....*...
gi 1167503283 225 IFKDLKLRGFwLSQWKKD 242
Cdd:PRK13771  271 ILKDIEIIGH-ISATKRD 287
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
32-264 4.36e-17

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: 79.83  E-value: 4.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  32 GVAQVVAvgSNVTGLKPGDWVIpanaGLGTWRTEAVFSEEALIQV---PSDIPLQSAA-TLGVNPCTAYRMLMDFEQLQP 107
Cdd:cd05288    72 GVGEVVE--SRSPDFKVGDLVS----GFLGWQEYAVVDGASGLRKldpSLGLPLSAYLgVLGMTGLTAYFGLTEIGKPKP 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 108 GDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKS-LGAEHVITeeelRRPEmkNFFKDmpqprLALN 186
Cdd:cd05288   146 GETVVVSAAAGAVGSVVGQIAKLLGARVVGIAGSD---EKC-RWLVEeLGFDAAIN----YKTP--DLAEA-----LKEA 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 187 C----------VGGKSSTELLRQLARGGTMVTYGGMA-----KQPVVASVSLLIFKDLKLRGFWLSQWKkdhspDQFKEL 251
Cdd:cd05288   211 ApdgidvyfdnVGGEILDAALTLLNKGGRIALCGAISqynatEPPGPKNLGNIITKRLTMQGFIVSDYA-----DRFPEA 285
                         250
                  ....*....|...
gi 1167503283 252 ILTLCDLIRRGQL 264
Cdd:cd05288   286 LAELAKWLAEGKL 298
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
3-286 1.05e-16

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


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 79.26  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGNYGFLPELPAVGGNEG-------------------VAQVVAVGSNVTGLKPGDWVIpanagLGTWR 63
Cdd:cd08274    37 ACGVNNTDINTREGWYSTEVDGATDSTGAGeagwwggtlsfpriqgadiVGRVVAVGEGVDTARIGERVL-----VDPSI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  64 TEAVFSEEALIQ---------------VPSD-----IPLQSAATLGVNPC---TAYRMLmDFEQLQPGDSVIQNASNSGV 120
Cdd:cd08274   112 RDPPEDDPADIDyigserdggfaeytvVPAEnaypvNSPLSDVELATFPCsysTAENML-ERAGVGAGETVLVTGASGGV 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 121 GQAVIQIAAALGLRTINVVRDRPDiqklsDRLKSLGAEHVITEEELRRPEMKNFFKdmPQPRLALNCVGGKSSTELLRQL 200
Cdd:cd08274   191 GSALVQLAKRRGAIVIAVAGAAKE-----EAVRALGADTVILRDAPLLADAKALGG--EPVDVVADVVGGPLFPDLLRLL 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 201 ARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGfwLSQWkkdhSPDQFKELIltlcDLIRRGQLTaPACSQV-PLQDYQS 279
Cdd:cd08274   264 RPGGRYVTAGAIAGPVVELDLRTLYLKDLTLFG--STLG----TREVFRRLV----RYIEEGEIR-PVVAKTfPLSEIRE 332

                  ....*..
gi 1167503283 280 ALEASMK 286
Cdd:cd08274   333 AQAEFLE 339
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
3-281 4.64e-16

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: 76.70  E-value: 4.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpANAG--LGTWRTEAVFSEEALIQVPSDI 80
Cdd:cd08251    16 AFSLNFGDLLCVRGLYPTMPPYPFTPGFEASGVVRAVGPHVTRLAVGDEVI-AGTGesMGGHATLVTVPEDQVVRKPASL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  81 PLQSAATLgvnPCTAYRMLMDFEQ--LQPGDSV-IQNASnSGVGQAVIQIAAALGLrTINVVRDRPDiqKLsDRLKSLGA 157
Cdd:cd08251    95 SFEEACAL---PVVFLTVIDAFARagLAKGEHIlIQTAT-GGTGLMAVQLARLKGA-EIYATASSDD--KL-EYLKQLGV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 158 EHVIT------EEELRRpemknffkdMPQPR---LALNCVGGKSSTELLRQLARGGTMVTYGGMA-KQPVVASVSLLI-- 225
Cdd:cd08251   167 PHVINyveedfEEEIMR---------LTGGRgvdVVINTLSGEAIQKGLNCLAPGGRYVEIAMTAlKSAPSVDLSVLSnn 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1167503283 226 --FKDLKLRGFWLSqwkkdhSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSAL 281
Cdd:cd08251   238 qsFHSVDLRKLLLL------DPEFIADYQAEMVSLVEEGELRPTVSRIFPFDDIGEAY 289
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
16-216 1.94e-15

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: 75.10  E-value: 1.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  16 GNYGFLPELPAVGGNEGVAQVVAVGSNV-TGLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCT 94
Cdd:cd08244    51 GPGPFPPELPYVPGGEVAGVVDAVGPGVdPAWLGRRVVAHTGRAGGGYAELAVADVDSLHPVPDGLDLEAAVAVVHDGRT 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  95 AYRMLmDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVR-DRpdiqKLsDRLKSLGAEHVITEEELRRPEMKN 173
Cdd:cd08244   131 ALGLL-DLATLTPGDVVLVTAAAGGLGSLLVQLAKAAGATVVGAAGgPA----KT-ALVRALGADVAVDYTRPDWPDQVR 204
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1167503283 174 FFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQP 216
Cdd:cd08244   205 EALGGGGVTVVLDGVGGAIGRAALALLAPGGRFLTYGWASGEW 247
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
9-210 3.59e-15

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: 74.71  E-value: 3.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   9 SDINMIQGNYGFLPelPAVGGNEGVAQVVAVGSNVT---GLKPGD-----WVIP--------------------ANAGLG 60
Cdd:cd08263    40 SDLHVLKGELPFPP--PFVLGHEISGEVVEVGPNVEnpyGLSVGDrvvgsFIMPcgkcrycargkenlcedffaYNRLKG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  61 T-----------------------WRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASn 117
Cdd:cd08263   118 TlydgttrlfrldggpvymysmggLAEYAVVPATALAPLPESLDYTESAVLGCAGFTAYGALKHAADVRPGETVAVIGV- 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 118 SGVGQAVIQIAAALGLRTINVVrdrpDIQKlsDRLKS---LGAEHVITEEELRRPEMknfFKDMPQPRLALNCVGGKSST 194
Cdd:cd08263   197 GGVGSSAIQLAKAFGASPIIAV----DVRD--EKLAKakeLGATHTVNAAKEDAVAA---IREITGGRGVDVVVEALGKP 267
                         250       260
                  ....*....|....*....|
gi 1167503283 195 ELLRQ----LARGGTMVTYG 210
Cdd:cd08263   268 ETFKLaldvVRDGGRAVVVG 287
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
21-233 1.06e-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. 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: 73.40  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  21 LPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI-PANAGLGTWR-------------------TEAVFSEEA-------- 72
Cdd:cd08260    51 DVTLPHVPGHEFAGVVVEVGEDVSRWRVGDRVTvPFVLGCGTCPycragdsnvcehqvqpgftHPGSFAEYVavpradvn 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  73 LIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNAsnSGVGQAVIQIAAALGLRTINVvrdrpDI--QKLs 149
Cdd:cd08260   131 LVRLPDDVDFVTAAGLGCRFATAFRALVHQARVKPGEWVaVHGC--GGVGLSAVMIASALGARVIAV-----DIddDKL- 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 150 DRLKSLGAEHVI--TEEELRRPEMKNFFKDMPQPRL-ALncvgGKSSTEL--LRQLARGGTMVTYGGMAKQPVVAS--VS 222
Cdd:cd08260   203 ELARELGAVATVnaSEVEDVAAAVRDLTGGGAHVSVdAL----GIPETCRnsVASLRKRGRHVQVGLTLGEEAGVAlpMD 278
                         250
                  ....*....|.
gi 1167503283 223 LLIFKDLKLRG 233
Cdd:cd08260   279 RVVARELEIVG 289
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
27-265 1.98e-14

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: 72.40  E-value: 1.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  27 VGGneGVAQVVAvgSNVTGLKPGDWVIpanaGLGTWRTEAVFSEEALIQV-PSDIPLQSA-ATLGVNPCTAYRMLMDFEQ 104
Cdd:COG2130    72 RGG--AVGEVVE--SRHPDFAVGDLVL----GMLGWQDYAVSDGAGLRKVdPSLAPLSAYlGVLGMPGLTAYFGLLDIGK 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 105 LQPGDSVIQNASNSGVGQAVIQIAAALGLRTINV---------VRDRpdiqklsdrlksLGAEHVI---TEeelrrpemk 172
Cdd:COG2130   144 PKAGETVVVSAAAGAVGSVVGQIAKLKGCRVVGIaggaekcryLVEE------------LGFDAAIdykAG--------- 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 173 nffkDMPQpRLALNC----------VGGKSSTELLRQLARGGTMV------TYGGMAKQPVVASVSLLIFKDLKLRGFWL 236
Cdd:COG2130   203 ----DLAA-ALAAACpdgidvyfdnVGGEILDAVLPLLNTFARIAvcgaisQYNATEPPPGPRNLGQLLVKRLRMQGFIV 277
                         250       260
                  ....*....|....*....|....*....
gi 1167503283 237 SqwkkDHsPDQFKELILTLCDLIRRGQLT 265
Cdd:COG2130   278 F----DH-ADRFPEFLAELAGWVAEGKLK 301
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
9-282 2.63e-14

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: 72.26  E-value: 2.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   9 SDINMIQGNY----GFL-------PELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI-----------------------P 54
Cdd:cd08240    40 SDLHIWDGGYdlggGKTmslddrgVKLPLVLGHEIVGEVVAVGPDAADVKVGDKVLvypwigcgecpvclagdenlcakG 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  55 ANAGL---GTWRTEAVFSEEALIQVPSDIPLQSAATLgvnPC---TAY---RMLMDFEQLQPgdSVIQNAsnSGVGQAVI 125
Cdd:cd08240   120 RALGIfqdGGYAEYVIVPHSRYLVDPGGLDPALAATL---ACsglTAYsavKKLMPLVADEP--VVIIGA--GGLGLMAL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 126 QIAAALGLRTInVVRDrPDIQKLsDRLKSLGAEHVITEEELRrpEMKNFFKDMP-QPRLALNCVGGKSSTEL-LRQLARG 203
Cdd:cd08240   193 ALLKALGPANI-IVVD-IDEAKL-EAAKAAGADVVVNGSDPD--AAKRIIKAAGgGVDAVIDFVNNSATASLaFDILAKG 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 204 GTMVT---YGGMAKQPVVasvsLLIFKDLKLRGFWLSqwkkdhSPDQFKELIltlcDLIRRGQLTAPACSQVPLQDYQSA 280
Cdd:cd08240   268 GKLVLvglFGGEATLPLP----LLPLRALTIQGSYVG------SLEELRELV----ALAKAGKLKPIPLTERPLSDVNDA 333

                  ..
gi 1167503283 281 LE 282
Cdd:cd08240   334 LD 335
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
24-164 3.96e-14

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: 70.76  E-value: 3.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  24 LPAVGGNEGVAQVVAVGSNVTGLKPGDWVipanAGLGTWRTEAVFSEEALIQVPSDIPLQSAAtLGVNPCTAYRMLMDFE 103
Cdd:cd08255    20 LPLPPGYSSVGRVVEVGSGVTGFKPGDRV----FCFGPHAERVVVPANLLVPLPDGLPPERAA-LTALAATALNGVRDAE 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167503283 104 qLQPGDSVI---QNAsnsgVGQAVIQIAAALGLRTInVVRDRpdiqkLSDRL---KSLGAEHVITEE 164
Cdd:cd08255    95 -PRLGERVAvvgLGL----VGLLAAQLAKAAGAREV-VGVDP-----DAARRelaEALGPADPVAAD 150
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
3-208 1.02e-13

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: 70.33  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGnYG--FL-------------PELPAVGGNEGVAQVVAVGSNVTGLKPGD--WVIPANAGLGTWRTE 65
Cdd:cd08248    38 AASVNPIDVLMRSG-YGrtLLnkkrkpqsckysgIEFPLTLGRDCSGVVVDIGSGVKSFEIGDevWGAVPPWSQGTHAEY 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  66 AVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQP----GDSVIQNASNSGVGQAVIQIAAALGlrtINVV-- 139
Cdd:cd08248   117 VVVPENEVSKKPKNLSHEEAASLPYAGLTAWSALVNVGGLNPknaaGKRVLILGGSGGVGTFAIQLLKAWG---AHVTtt 193
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167503283 140 ---RDRPDIqklsdrlKSLGAEHVIT------EEELRRPEMKNFFkdmpqprlaLNCVGGKSSTELLRQLARGGTMVT 208
Cdd:cd08248   194 cstDAIPLV-------KSLGADDVIDynnedfEEELTERGKFDVI---------LDTVGGDTEKWALKLLKKGGTYVT 255
PRK10754 PRK10754
NADPH:quinone reductase;
22-217 1.58e-13

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 69.76  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  22 PELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMD 101
Cdd:PRK10754   55 PSLPSGLGTEAAGVVSKVGSGVKHIKVGDRVVYAQSALGAYSSVHNVPADKAAILPDAISFEQAAASFLKGLTVYYLLRK 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 102 FEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQklsdRLKSLGAEHVITEEELRRPEMKNFFKDMPQP 181
Cdd:PRK10754  135 TYEIKPDEQFLFHAAAGGVGLIACQWAKALGAKLIGTVGSAQKAQ----RAKKAGAWQVINYREENIVERVKEITGGKKV 210
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1167503283 182 RLALNCVGGKSSTELLRQLARGGTMVTYGGmAKQPV 217
Cdd:PRK10754  211 RVVYDSVGKDTWEASLDCLQRRGLMVSFGN-ASGPV 245
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
9-282 1.99e-13

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


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 69.53  E-value: 1.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   9 SDINMIQGNYGFLpELPAVGGNEGVAQVVAVGSNVTGLKPGDWV--IP-------------------ANAGLGTWRTEAv 67
Cdd:cd08261    39 SDLHIYHGRNPFA-SYPRILGHELSGEVVEVGEGVAGLKVGDRVvvDPyiscgecyacrkgrpncceNLQVLGVHRDGG- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  68 FSE-----EALIQVPSDIPLQSAA-----TLGVNpcTAYRMlmdfeQLQPGDSV-IQNAsnSGVGQAVIQIAAALGLRTI 136
Cdd:cd08261   117 FAEyivvpADALLVPEGLSLDQAAlveplAIGAH--AVRRA-----GVTAGDTVlVVGA--GPIGLGVIQVAKARGARVI 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 137 nvVRDRPDiqklsDRL---KSLGAEHVI------TEEELRrpEMKNffKDMPQprLALNCVGGKSS-TELLRQLARGGTM 206
Cdd:cd08261   188 --VVDIDD-----ERLefaRELGADDTInvgdedVAARLR--ELTD--GEGAD--VVIDATGNPASmEEAVELVAHGGRV 254
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167503283 207 VtYGGMAKQPVVASVSLLIFKDLKLRGFWLSQwkkdhsPDQFKELIltlcDLIRRGQLTAPA-CSQ-VPLQDYQSALE 282
Cdd:cd08261   255 V-LVGLSKGPVTFPDPEFHKKELTILGSRNAT------REDFPDVI----DLLESGKVDPEAlITHrFPFEDVPEAFD 321
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
1-252 2.34e-13

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: 69.39  E-value: 2.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLpeLPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANA----------------------- 57
Cdd:cd05279    32 VVATGVCHTDLHVIDGKLPTP--LPVILGHEGAGIVESIGPGVTTLKPGDKVIPLFGpqcgkckqclnprpnlcsksrgt 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  58 ------------------------GLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQ 113
Cdd:cd05279   110 ngrglmsdgtsrftckgkpihhflGTSTFAEYTVVSEISLAKIDPDAPLEKVCLIGCGFSTGYGAAVNTAKVTPGSTCAV 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 114 NASnSGVGQAVIQIAAALGLRTINVVrdrpDIQKlsDRL---KSLGAEHVITEEELRRP------EMKNFFKDmpqprLA 184
Cdd:cd05279   190 FGL-GGVGLSVIMGCKAAGASRIIAV----DINK--DKFekaKQLGATECINPRDQDKPivevltEMTDGGVD-----YA 257
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167503283 185 LNCVGgksSTELLRQL-----ARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWKkdhSPDQFKELI 252
Cdd:cd05279   258 FEVIG---SADTLKQAldatrLGGGTSVVVGVPPSGTEATLDPNDLLTGRTIKGTVFGGWK---SKDSVPKLV 324
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
6-205 5.90e-13

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: 68.02  E-value: 5.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   6 INPSDINMIQGNYGFLpELPAVGGNEGVAQVVAVGSNvtGLKPGDWVIPANAGLGtwRT-------EAVFSEEALIQVPS 78
Cdd:cd08243    39 LNRSEIFTRQGHSPSV-KFPRVLGIEAVGEVEEAPGG--TFTPGQRVATAMGGMG--RTfdgsyaeYTLVPNEQVYAIDS 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  79 DIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDrpdiQKLSDRLKSLGAE 158
Cdd:cd08243   114 DLSWAELAALPETYYTAWGSLFRSLGLQPGDTLLIRGGTSSVGLAALKLAKALGATVTATTRS----PERAALLKELGAD 189
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1167503283 159 HVITE-----EELRRpEMKNFFKdmpqprlALNCVGGKSSTELLRQLARGGT 205
Cdd:cd08243   190 EVVIDdgaiaEQLRA-APGGFDK-------VLELVGTATLKDSLRHLRPGGI 233
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
9-283 1.19e-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: 67.20  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   9 SDINMIQGNYG--FLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI-----------------------PANAGLGTWR 63
Cdd:cd05284    40 SDLHVIDGVWGgiLPYKLPFTLGHENAGWVEEVGSGVDGLKEGDPVVvhppwgcgtcrycrrgeenycenARFPGIGTDG 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  64 TEA---VFSEEALIQVPSDIPLQSAATLGVNPCTAYRML---MDFeqLQPGDSVIQNASnSGVGQAVIQIAAALGLRTIN 137
Cdd:cd05284   120 GFAeylLVPSRRLVKLPRGLDPVEAAPLADAGLTAYHAVkkaLPY--LDPGSTVVVIGV-GGLGHIAVQILRALTPATVI 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 138 VVRDRPDIQKLSDRlksLGAEHVI-----TEEELRRpemknfFKDMPQPRLALNCVGGKSSTEL-LRQLARGG--TMVTY 209
Cdd:cd05284   197 AVDRSEEALKLAER---LGADHVLnasddVVEEVRE------LTGGRGADAVIDFVGSDETLALaAKLLAKGGryVIVGY 267
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167503283 210 GGMAKQPVVAsvslLIFKDLKLRG-FWLSQwkkdhspDQFKELIltlcDLIRRGQLTaPACSQVPLQDYQSALEA 283
Cdd:cd05284   268 GGHGRLPTSD----LVPTEISVIGsLWGTR-------AELVEVV----ALAESGKVK-VEITKFPLEDANEALDR 326
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
31-264 1.56e-12

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: 66.90  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  31 EGVAQVVAvgSNVTGLKPGDWVIpANAGlgtWRTEAVFSEEA---LIQVPSDIPLQ---SAA--TLGVNPCTAYRMLMDF 102
Cdd:cd08294    65 TQVAKVIE--SKNSKFPVGTIVV-ASFG---WRTHTVSDGKDqpdLYKLPADLPDDlppSLAlgVLGMPGLTAYFGLLEI 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 103 EQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRdrpdiqklSD----RLKSLGAEHVIT------EEELRR--PE 170
Cdd:cd08294   139 CKPKAGETVVVNGAAGAVGSLVGQIAKIKGCKVIGCAG--------SDdkvaWLKELGFDAVFNyktvslEEALKEaaPD 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 171 MKNFFKDmpqprlalNcVGGKSSTELLRQLARGGTMV------TYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWkKDHS 244
Cdd:cd08294   211 GIDCYFD--------N-VGGEFSSTVLSHMNDFGRVAvcgsisTYNDKEPKKGPYVQETIIFKQLKMEGFIVYRW-QDRW 280
                         250       260
                  ....*....|....*....|
gi 1167503283 245 PDQFKELIltlcDLIRRGQL 264
Cdd:cd08294   281 PEALKQLL----KWIKEGKL 296
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
9-233 2.48e-12

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: 66.37  E-value: 2.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   9 SDINMIQGNYGFlPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVipanaGLGTWR------------------------- 63
Cdd:cd05283    39 SDLHTLRNEWGP-TKYPLVPGHEIVGIVVAVGSKVTKFKVGDRV-----GVGCQVdscgtceqcksgeeqycpkgvvtyn 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  64 --------------TEAVFSEEALIQVPSDIPLQSAATL---GVnpcTAYRMLMDFeQLQPGDSViqnasnsGV------ 120
Cdd:cd05283   113 gkypdgtitqggyaDHIVVDERFVFKIPEGLDSAAAAPLlcaGI---TVYSPLKRN-GVGPGKRV-------GVvgiggl 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 121 GQAVIQIAAALGLRTinVVRDRPDIQKlsDRLKSLGAEHVI-TEEElrrPEMKNFFKDMpqpRLALNCVGGKSS-TELLR 198
Cdd:cd05283   182 GHLAVKFAKALGAEV--TAFSRSPSKK--EDALKLGADEFIaTKDP---EAMKKAAGSL---DLIIDTVSASHDlDPYLS 251
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1167503283 199 QLARGGTMVTYgGMAKQPVVASVSLLIFKDLKLRG 233
Cdd:cd05283   252 LLKPGGTLVLV-GAPEEPLPVPPFPLIFGRKSVAG 285
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
27-161 4.51e-12

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: 65.90  E-value: 4.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  27 VGGNEGVAQVVAVGSNVTGLKPGDWVI----------PANAGLGT--------WRTE---AVFSEEALIQV------PSD 79
Cdd:cd08246    84 IGGSDASGIVWAVGEGVKNWKVGDEVVvhcsvwdgndPERAGGDPmfdpsqriWGYEtnyGSFAQFALVQAtqlmpkPKH 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  80 IPLQSAATLGVNPCTAYRMLMDFE--QLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiQKlSDRLKSLGA 157
Cdd:cd08246   164 LSWEEAAAYMLVGATAYRMLFGWNpnTVKPGDNVLIWGASGGLGSMAIQLARAAGANPVAVVSSE---EK-AEYCRALGA 239

                  ....
gi 1167503283 158 EHVI 161
Cdd:cd08246   240 EGVI 243
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
1-283 5.53e-12

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: 65.36  E-value: 5.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLPeLPAVGGNEGVAQVVAVGSNVT------GLKPGDWVI-----------------PA-- 55
Cdd:cd08231    32 VRLAGVCGSDVHTVAGRRPRVP-LPIILGHEGVGRVVALGGGVTtdvagePLKVGDRVTwsvgapcgrcyrclvgdPTkc 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  56 --------NAGLGTWRTEAVFSEEALIQ-------VPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNAsnSG 119
Cdd:cd08231   111 enrkkyghEASCDDPHLSGGYAEHIYLPpgtaivrVPDNVPDEVAAPANCALATVLAALDRAGPVGAGDTVvVQGA--GP 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 120 VGQAVIQIAAALGLRTInVVRDRPDiqklsDRLK---SLGAEHVITEEELRRPEMKNFFKDMPQPR---LALNCVGGKSS 193
Cdd:cd08231   189 LGLYAVAAAKLAGARRV-IVIDGSP-----ERLElarEFGADATIDIDELPDPQRRAIVRDITGGRgadVVIEASGHPAA 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 194 -TELLRQLARGGTMVTYGGMAKQPVVA-SVSLLIFKDLKLRGFWLSqwkkdhSPDQFKELILTLCDLIRR----GQLTAP 267
Cdd:cd08231   263 vPEGLELLRRGGTYVLVGSVAPAGTVPlDPERIVRKNLTIIGVHNY------DPSHLYRAVRFLERTQDRfpfaELVTHR 336
                         330
                  ....*....|....*.
gi 1167503283 268 acsqVPLQDYQSALEA 283
Cdd:cd08231   337 ----YPLEDINEALEL 348
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
3-233 8.57e-12

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: 64.64  E-value: 8.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDINMIQGNYGFlPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI----------------------PANAGLG 60
Cdd:cd08258    35 AAGICGSDLHIYKGDYDP-VETPVVLGHEFSGTIVEVGPDVEGWKVGDRVVsettfstcgrcpycrrgdynlcPHRKGIG 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  61 TWR----TEAVFS-EEALIQVPSDIPLQSAATLgvNP-CTAYRMLMDFEQLQPGDSVIqnASNSG-VGQAVIQIAAALGL 133
Cdd:cd08258   114 TQAdggfAEYVLVpEESLHELPENLSLEAAALT--EPlAVAVHAVAERSGIRPGDTVV--VFGPGpIGLLAAQVAKLQGA 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 134 RTINVvrdrpDIQKLSDRL---KSLGAEHVITEEELRRpEMKNFFKDMPQPRLALNCVGG----KSSTELLRqlaRGGTM 206
Cdd:cd08258   190 TVVVV-----GTEKDEVRLdvaKELGADAVNGGEEDLA-ELVNEITDGDGADVVIECSGAvpalEQALELLR---KGGRI 260
                         250       260
                  ....*....|....*....|....*..
gi 1167503283 207 VTYGGMAKQPVVASVSLLIFKDLKLRG 233
Cdd:cd08258   261 VQVGIFGPLAASIDVERIIQKELSVIG 287
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
3-282 2.12e-11

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: 63.44  E-value: 2.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   3 AAPINPSDInMIQGNYGFLPELPAVG-GNE--GVaqVVAVGSNV-TGLKPGDWV----IPANAGLGTWRTEAVF----SE 70
Cdd:cd08247    37 AAALNPVDL-KLYNSYTFHFKVKEKGlGRDysGV--IVKVGSNVaSEWKVGDEVcgiyPHPYGGQGTLSQYLLVdpkkDK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  71 EALIQVPSDIPLQSAA----TLGvnpcTAYRMLMDFEQ-LQPGDSVIQNASNSGVGQAVIQIaAALGLRTINVV---RDR 142
Cdd:cd08247   114 KSITRKPENISLEEAAawplVLG----TAYQILEDLGQkLGPDSKVLVLGGSTSVGRFAIQL-AKNHYNIGTVVgtcSSR 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 143 PdiqklSDRLKSLGAEHVI-----TEEELRRPEMKNfFKDMPQPRLALNCVGG----KSSTELLRQLARGGTMVT----Y 209
Cdd:cd08247   189 S-----AELNKKLGADHFIdydahSGVKLLKPVLEN-VKGQGKFDLILDCVGGydlfPHINSILKPKSKNGHYVTivgdY 262
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167503283 210 GGMAKQPVVASVSLLIFKDLKLRG---FWLSQWKKDHsPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALE 282
Cdd:cd08247   263 KANYKKDTFNSWDNPSANARKLFGslgLWSYNYQFFL-LDPNADWIEKCAELIADGKVKPPIDSVYPFEDYKEAFE 337
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
18-233 6.52e-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: 61.96  E-value: 6.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  18 YGFLPELPAVGgnegvaqvVAVGSNVTGLKPGDWVIPANAGLGTWRtEAVFSEEA------LIQVPSDIPLQSAATLGVN 91
Cdd:cd08289    57 YPFIPGIDLAG--------TVVESNDPRFKPGDEVIVTSYDLGVSH-HGGYSEYArvpaewVVPLPKGLTLKEAMILGTA 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  92 PCTAYRMLMDFEQ--LQP-GDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDiqklSDRLKSLGAEHVITEEELRR 168
Cdd:cd08289   128 GFTAALSIHRLEEngLTPeQGPVLVTGATGGVGSLAVSILAKLGYEVVASTGKADA----ADYLKKLGAKEVIPREELQE 203
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167503283 169 PEMKNFFKDMPQPrlALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRG 233
Cdd:cd08289   204 ESIKPLEKQRWAG--AVDPVGGKTLAYLLSTLQYGGSVAVSGLTGGGEVETTVFPFILRGVNLLG 266
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
70-252 7.82e-11

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: 61.94  E-value: 7.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  70 EEALIQVPSDIPLQSA-ATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIqkl 148
Cdd:TIGR02825 100 EKLLTEWPDTLPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKV--- 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 149 sDRLKSLGAEHVIT-------EEELRR--PEMKNFFKDMpqprlalncVGGKSSTELLRQL------ARGGTMVTYGGMA 213
Cdd:TIGR02825 177 -AYLKKLGFDVAFNyktvkslEETLKKasPDGYDCYFDN---------VGGEFSNTVIGQMkkfgriAICGAISTYNRTG 246
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1167503283 214 KQPVVASVSLLIFKDLKLRGFWLSQWKKDHSPDQFKELI 252
Cdd:TIGR02825 247 PLPPGPPPEIVIYQELRMEGFIVNRWQGEVRQKALKELL 285
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
10-284 1.37e-10

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: 61.36  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  10 DINMIQGNYGflPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI----------------PA---------NAGL---GT 61
Cdd:cd08278    43 DLVVRDGGLP--TPLPAVLGHEGAGVVEAVGSAVTGLKPGDHVVlsfascgecanclsghPAycenffplnFSGRrpdGS 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  62 WR--------------------TEAVFSEEALIQVPSDIPLQSAATLGvnpC-------TAYRMLmdfeQLQPGDSV-IQ 113
Cdd:cd08278   121 TPlslddgtpvhghffgqssfaTYAVVHERNVVKVDKDVPLELLAPLG---CgiqtgagAVLNVL----KPRPGSSIaVF 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 114 NAsnSGVGQAVIQIAAALGLRTINVVrdrpDIQklSDRL---KSLGAEHVI------TEEELRR--PEMKNFfkdmpqpr 182
Cdd:cd08278   194 GA--GAVGLAAVMAAKIAGCTTIIAV----DIV--DSRLelaKELGATHVInpkeedLVAAIREitGGGVDY-------- 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 183 lALNCVGgksSTELLRQ----LARGGTMVTYgGMAKQPVVASVSLLifkDLKLRGfwlsqwKK-------DHSPDQFkel 251
Cdd:cd08278   258 -ALDTTG---VPAVIEQavdaLAPRGTLALV-GAPPPGAEVTLDVN---DLLVSG------KTirgviegDSVPQEF--- 320
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1167503283 252 ILTLCDLIRRGQLtaPA---CSQVPLQDYQSALEAS 284
Cdd:cd08278   321 IPRLIELYRQGKF--PFdklVTFYPFEDINQAIADS 354
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
1-210 1.56e-10

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: 61.24  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYgflPE-LPAVGGNEGVAQVVAVGSNVTGLKPGDWVI-------------------------P 54
Cdd:cd08281    40 IAAAGLCHSDLSVINGDR---PRpLPMALGHEAAGVVVEVGEGVTDLEVGDHVVlvfvpscghcrpcaegrpalcepgaA 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  55 ANA----------------------GLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVI 112
Cdd:cd08281   117 ANGagtllsggrrlrlrggeinhhlGVSAFAEYAVVSRRSVVKIDKDVPLEIAALFGCAVLTGVGAVVNTAGVRPGQSVA 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 113 QnASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSdrlKSLGAEHVITEEElrrPEMKNFFKDMPQ--PRLALNCVGG 190
Cdd:cd08281   197 V-VGLGGVGLSALLGAVAAGASQVVAVDLNEDKLALA---RELGATATVNAGD---PNAVEQVRELTGggVDYAFEMAGS 269
                         250       260
                  ....*....|....*....|.
gi 1167503283 191 KSSTEL-LRQLARGGTMVTYG 210
Cdd:cd08281   270 VPALETaYEITRRGGTTVTAG 290
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
22-165 3.32e-10

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: 59.68  E-value: 3.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  22 PELPAVGGNEGVAQVVAVGSNVTGLKPGDWVipanAGL--GTWRTEAVFSEEALIQVPSD-----IPLQSAATlGVNpct 94
Cdd:cd08269    49 PAEPGGPGHEGWGRVVALGPGVRGLAVGDRV----AGLsgGAFAEYDLADADHAVPLPSLldgqaFPGEPLGC-ALN--- 120
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167503283  95 ayrmLMDFEQLQPGDSVIQNASNSgVGQAVIQIAAALGLRTINVVRDRPDIQKLSdrlKSLGAEHVITEEE 165
Cdd:cd08269   121 ----VFRRGWIRAGKTVAVIGAGF-IGLLFLQLAAAAGARRVIAIDRRPARLALA---RELGATEVVTDDS 183
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
1-172 3.86e-10

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: 59.85  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLPElPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPA--------NAGLgtwrtEAVfsEEA 72
Cdd:cd08252    37 VEAVSVNPVDTKVRAGGAPVPGQ-PKILGWDASGVVEAVGSEVTLFKVGDEVYYAgditrpgsNAEY-----QLV--DER 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  73 LI-QVPSDIPLQSAATLGVNPCTAYRMLmdFEQLQpGDSVIQNASNS--------GVGQAVIQIAAALGLRTINVVRDRP 143
Cdd:cd08252   109 IVgHKPKSLSFAEAAALPLTSLTAWEAL--FDRLG-ISEDAENEGKTlliiggagGVGSIAIQLAKQLTGLTVIATASRP 185
                         170       180
                  ....*....|....*....|....*....
gi 1167503283 144 DIQklsDRLKSLGAEHVITEEELRRPEMK 172
Cdd:cd08252   186 ESI---AWVKELGADHVINHHQDLAEQLE 211
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
9-158 6.46e-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: 59.19  E-value: 6.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   9 SDINMIQGNYGFLPelPAVGGNEGVAQVVAVGSNVTGLKPGDWVI-PANAGLG---------TWR--------------- 63
Cdd:cd08284    40 SDLHIYRGHIPSTP--GFVLGHEFVGEVVEVGPEVRTLKVGDRVVsPFTIACGecfycrrgqSGRcakgglfgyagspnl 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  64 ----TEAV---FSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFeQLQPGDSVIQNASNSgVGQAVIQIAAALGLRTI 136
Cdd:cd08284   118 dgaqAEYVrvpFADGTLLKLPDGLSDEAALLLGDILPTGYFGAKRA-QVRPGDTVAVIGCGP-VGLCAVLSAQVLGAARV 195
                         170       180
                  ....*....|....*....|....*
gi 1167503283 137 NVVrDRpdiqkLSDRL---KSLGAE 158
Cdd:cd08284   196 FAV-DP-----VPERLeraAALGAE 214
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
1-169 6.85e-10

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


Pssm-ID: 176238 [Multi-domain]  Cd Length: 365  Bit Score: 59.27  E-value: 6.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGnyGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP-------------------------- 54
Cdd:cd08277    34 MLATSVCHTDILAIEG--FKATLFPVILGHEGAGIVESVGEGVTNLKPGDKVIPlfigqcgecsncrsgktnlcqkyran 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  55 --------------------ANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSViqn 114
Cdd:cd08277   112 esglmpdgtsrftckgkkiyHFLGTSTFSQYTVVDENYVAKIDPAAPLEHVCLLGCGFSTGYGAAWNTAKVEPGSTV--- 188
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1167503283 115 A--SNSGVGQAVIQIAAALGLRTINVVrdrpDIQKLSD-RLKSLGAEHVITEEELRRP 169
Cdd:cd08277   189 AvfGLGAVGLSAIMGAKIAGASRIIGV----DINEDKFeKAKEFGATDFINPKDSDKP 242
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
1-53 1.89e-08

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: 51.46  E-value: 1.89e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1167503283   1 MLAAPINPSDINMIQGNYgFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI 53
Cdd:pfam08240   7 VKAAGICGSDLHIYKGGN-PPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVV 58
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
10-287 3.86e-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: 53.68  E-value: 3.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  10 DINMIQGNYGflPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV-----IPAN----------------AGLGTWRT---- 64
Cdd:cd08234    40 DLHIYEGEFG--AAPPLVPGHEFAGVVVAVGSKVTGFKVGDRVavdpnIYCGecfycrrgrpnlcenlTAVGVTRNggfa 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  65 E-AVFSEEALIQVPSDIPLQSAATL--------GVNPCtayrmlmdfeQLQPGDSV-IQNAsnsGV-GQAVIQIAAALGL 133
Cdd:cd08234   118 EyVVVPAKQVYKIPDNLSFEEAALAeplscavhGLDLL----------GIKPGDSVlVFGA---GPiGLLLAQLLKLNGA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 134 RTINVVrDRPDIqKLsDRLKSLGAEHVITEEELRRPEMKNffkdmPQPR---LALNCVGGKSSTEL-LRQLARGGTMVTY 209
Cdd:cd08234   185 SRVTVA-EPNEE-KL-ELAKKLGATETVDPSREDPEAQKE-----DNPYgfdVVIEATGVPKTLEQaIEYARRGGTVLVF 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 210 G-GMAKQPVVASVSLLIFKDLKLRGFWLsqwkkdhSPDQFKELIltlcDLIRRGQL-TAPACS-QVPLQDYQSALEASMK 286
Cdd:cd08234   257 GvYAPDARVSISPFEIFQKELTIIGSFI-------NPYTFPRAI----ALLESGKIdVKGLVShRLPLEEVPEALEGMRS 325

                  .
gi 1167503283 287 P 287
Cdd:cd08234   326 G 326
MDR_yhdh cd08288
Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR ...
14-213 6.96e-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: 52.92  E-value: 6.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  14 IQGNYGFLPELPAVGGNEGVAQVVAVGSNvtGLKPGDWVIPANAGLGTWR-----TEAVFSEEALIQVPSDIPLQSAATL 88
Cdd:cd08288    47 ITGKGGIVRTFPLVPGIDLAGTVVESSSP--RFKPGDRVVLTGWGVGERHwggyaQRARVKADWLVPLPEGLSARQAMAI 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  89 GVNPCTAyrML--MDFEQ--LQPGDS-VIQNASNSGVGQAVIQIAAALGLRTInVVRDRPDiqkLSDRLKSLGAEHVITE 163
Cdd:cd08288   125 GTAGFTA--MLcvMALEDhgVTPGDGpVLVTGAAGGVGSVAVALLARLGYEVV-ASTGRPE---EADYLRSLGASEIIDR 198
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1167503283 164 EELRRPEmknffKDMPQPRLA--LNCVGGKSSTELLRQLARGGTmVTYGGMA 213
Cdd:cd08288   199 AELSEPG-----RPLQKERWAgaVDTVGGHTLANVLAQTRYGGA-VAACGLA 244
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
1-161 1.47e-07

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: 51.87  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNygfLPELPA--VGGNEGVAQVVAVGSNVTGLKPGDWVIPA-----------NAGL------GT 61
Cdd:cd08286    32 MLKTTICGTDLHILKGD---VPTVTPgrILGHEGVGVVEEVGSAVTNFKVGDRVLIScisscgtcgycRKGLyshcesGG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  62 WR-------TEAVF-----SEEALIQVPSDIPLQSAATLG-VNPcTAYRMLMDFEQLQPGDSV-IQNAsnsG-VGQAVIQ 126
Cdd:cd08286   109 WIlgnlidgTQAEYvriphADNSLYKLPEGVDEEAAVMLSdILP-TGYECGVLNGKVKPGDTVaIVGA---GpVGLAALL 184
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1167503283 127 IAAALGLRTINVVrDRPDiqklsDRL---KSLGAEHVI 161
Cdd:cd08286   185 TAQLYSPSKIIMV-DLDD-----NRLevaKKLGATHTV 216
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
1-235 9.86e-07

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: 49.63  E-value: 9.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPAN-AGLGTWRT--------------- 64
Cdd:cd08239    31 VKASGLCGSDLHYYYHGHRAPAYQGVIPGHEPAGVVVAVGPGVTHFRVGDRVMVYHyVGCGACRNcrrgwmqlctskraa 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  65 --------EAVF---SEEALIQVPSDIPLQSAATLGVNPCTAYRMLmDFEQLQPGDSVIqnASNSG-VGQAVIQIAAALG 132
Cdd:cd08239   111 ygwnrdggHAEYmlvPEKTLIPLPDDLSFADGALLLCGIGTAYHAL-RRVGVSGRDTVL--VVGAGpVGLGALMLARALG 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 133 LRTINVVrdRPDIQKLsDRLKSLGAEHVITEEELRRPEMKNFFKDMPQpRLALNCVGGKSSTEL-LRQLARGGTMVtYGG 211
Cdd:cd08239   188 AEDVIGV--DPSPERL-ELAKALGADFVINSGQDDVQEIRELTSGAGA-DVAIECSGNTAARRLaLEAVRPWGRLV-LVG 262
                         250       260
                  ....*....|....*....|....
gi 1167503283 212 MAKQPVVASVSLLIFKDLKLRGFW 235
Cdd:cd08239   263 EGGELTIEVSNDLIRKQRTLIGSW 286
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
1-54 1.41e-06

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: 49.23  E-value: 1.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1167503283   1 MLAAPINPSDINMIQGNygFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP 54
Cdd:cd08299    39 IVATGICRSDDHVVSGK--LVTPFPVILGHEAAGIVESVGEGVTTVKPGDKVIP 90
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
91-165 1.87e-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: 48.28  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  91 NPC------TAYRMLMDFEQ---LQPGDSVIQNAS-NSGVGQAVIqiAAALGLRTINVVRDRPDIQKLsDRLKSLGAEHV 160
Cdd:cd01561    27 NPGgsvkdrIALYMIEDAEKrglLKPGTTIIEPTSgNTGIGLAMV--AAAKGYRFIIVMPETMSEEKR-KLLRALGAEVI 103

                  ....*
gi 1167503283 161 ITEEE 165
Cdd:cd01561   104 LTPEA 108
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
1-66 3.67e-06

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: 47.62  E-value: 3.67e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167503283   1 MLAAPINPSDINMIQGNYGFLPElPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpANAGLGTWRTEA 66
Cdd:cd08285    31 PTAVAPCTSDVHTVWGGAPGERH-GMILGHEAVGVVEEVGSEVKDFKPGDRVI-VPAITPDWRSVA 94
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
1-289 4.14e-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: 47.59  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   1 MLAAPINPSDINMIQGNYgFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPA-NAGLGTWR-----TEAVFSEEALI 74
Cdd:cd08235    31 VRACGICGTDVKKIRGGH-TDLKPPRILGHEIAGEIVEVGDGVTGFKVGDRVFVApHVPCGECHyclrgNENMCPNYKKF 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  75 QVPSD--------IPLQSAATLGVNPCTAYrmlMDFEQL---QPGDSVIQNASNSGV--GQAV------------IQIAA 129
Cdd:cd08235   110 GNLYDggfaeyvrVPAWAVKRGGVLKLPDN---VSFEEAalvEPLACCINAQRKAGIkpGDTVlvigagpigllhAMLAK 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 130 ALGLRTINVVrdrpDIqkLSDRL---KSLGAEHVI-TEEELRRPEMKNFFK----DmpqprLALNCVGGKSSTEL-LRQL 200
Cdd:cd08235   187 ASGARKVIVS----DL--NEFRLefaKKLGADYTIdAAEEDLVEKVRELTDgrgaD-----VVIVATGSPEAQAQaLELV 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 201 ARGGTMVTYGGMAK-QPVVASVSLLIFKDLKLRGFWLSqwkkdhSPDQFKELIltlcDLIRRGQLTAPA--CSQVPLQDY 277
Cdd:cd08235   256 RKGGRILFFGGLPKgSTVNIDPNLIHYREITITGSYAA------SPEDYKEAL----ELIASGKIDVKDliTHRFPLEDI 325
                         330
                  ....*....|....*..
gi 1167503283 278 QSALE-----ASMKPFI 289
Cdd:cd08235   326 EEAFElaadgKSLKIVI 342
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
155-285 6.21e-06

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 45.01  E-value: 6.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 155 LGAEHVI--TEEELRRPEMKNFFKdmpqprLALNCVGGKSSTELLRQLARGGTMVTYGGmakqPVVASVSLLIFKDLKLR 232
Cdd:pfam13602   1 LGADEVIdyRTTDFVQATGGEGVD------VVLDTVGGEAFEASLRVLPGGGRLVTIGG----PPLSAGLLLPARKRGGR 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1167503283 233 GFWLSQWKkdHSPDQFKELILTLCDLIRRGQLTaPACSQV-PLQDYQSALEASM 285
Cdd:pfam13602  71 GVKYLFLF--VRPNLGADILQELADLIEEGKLR-PVIDRVfPLEEAAEAHRYLE 121
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
25-233 9.07e-06

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: 46.33  E-value: 9.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  25 PAVGGNEGVAQVVAVGSNVTGLKPGDWV-----IPAN------AGL----------------GTWRTEAVFSEEALIQVP 77
Cdd:cd05285    55 PMVLGHESAGTVVAVGSGVTHLKVGDRVaiepgVPCRtcefckSGRynlcpdmrfaatppvdGTLCRYVNHPADFCHKLP 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  78 SDIPLQSAA---TLGVNPCTAYRMlmdfeQLQPGDSV-IQNAsnsG-VGQAVIQIAAALGLRTINVVrdrpDIQKlsDRL 152
Cdd:cd05285   135 DNVSLEEGAlvePLSVGVHACRRA-----GVRPGDTVlVFGA---GpIGLLTAAVAKAFGATKVVVT----DIDP--SRL 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 153 ---KSLGAEHVI----TEEELRRPEMKNFFKDMpQPRLALNCVGGKSSTEL-LRQLARGGTMVTyGGMAKQPVVASVSLL 224
Cdd:cd05285   201 efaKELGATHTVnvrtEDTPESAEKIAELLGGK-GPDVVIECTGAESCIQTaIYATRPGGTVVL-VGMGKPEVTLPLSAA 278

                  ....*....
gi 1167503283 225 IFKDLKLRG 233
Cdd:cd05285   279 SLREIDIRG 287
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
9-61 9.64e-06

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


Pssm-ID: 176242 [Multi-domain]  Cd Length: 375  Bit Score: 46.43  E-value: 9.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1167503283   9 SDINMIQGNYGflPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV-IPANAGLGT 61
Cdd:cd08282    40 SDLHMYRGRTG--AEPGLVLGHEAMGEVEEVGSAVESLKVGDRVvVPFNVACGR 91
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
48-233 1.50e-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: 45.63  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  48 PGDWVIPanaglgtwrteavfseealiqVPSDIPLQSAATLGVNPCTAYRMLMDFEQ--LQPGD-SVIQNASNSGVGQAV 124
Cdd:TIGR02823 104 PADWLVP---------------------LPEGLSLREAMALGTAGFTAALSVMALERngLTPEDgPVLVTGATGGVGSLA 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 125 IQIAAALGLRTInVVRDRPDiqkLSDRLKSLGAEHVITEEELR---RPEMKNFFKDmpqprlALNCVGGKSSTELLRQLA 201
Cdd:TIGR02823 163 VAILSKLGYEVV-ASTGKAE---EEDYLKELGASEVIDREDLSppgKPLEKERWAG------AVDTVGGHTLANVLAQLK 232
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1167503283 202 RGGTMVTYGGMAKQPVVASVSLLIfkdlkLRG 233
Cdd:TIGR02823 233 YGGAVAACGLAGGPDLPTTVLPFI-----LRG 259
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
2-282 4.09e-05

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: 44.57  E-value: 4.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   2 LAAPINPSDINMIQGNyGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV-IPANA------------------GLGTW 62
Cdd:cd05278    33 TATSICGSDLHIYRGG-VPGAKHGMILGHEFVGEVVEVGSDVKRLKPGDRVsVPCITfcgrcrfcrrgyhahcenGLWGW 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  63 ----RTEAVFSE--------EALIQVPSDIPLQSAATLGVNPCTAY---RMlmdfEQLQPGDSVIqnASNSG-VGQAVIQ 126
Cdd:cd05278   112 klgnRIDGGQAEyvrvpyadMNLAKIPDGLPDEDALMLSDILPTGFhgaEL----AGIKPGSTVA--VIGAGpVGLCAVA 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 127 IAAALGLRTINVVRDRPDIQKLsdrLKSLGAEHVITeeeLRRPEMKNFFKDMPQPRLA---LNCVGGKSSTELLRQLARG 203
Cdd:cd05278   186 GARLLGAARIIAVDSNPERLDL---AKEAGATDIIN---PKNGDIVEQILELTGGRGVdcvIEAVGFEETFEQAVKVVRP 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 204 GTMVTYGGMAKQPVvasvsllifkDLKLRGFWlsqWKKDHS--------PDQFKELIltlcDLIRRGQL-TAPACSQV-P 273
Cdd:cd05278   260 GGTIANVGVYGKPD----------PLPLLGEW---FGKNLTfktglvpvRARMPELL----DLIEEGKIdPSKLITHRfP 322

                  ....*....
gi 1167503283 274 LQDYQSALE 282
Cdd:cd05278   323 LDDILKAYR 331
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
32-239 4.45e-05

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 44.45  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  32 GVAQVVAvgSNVTGLKPGDWVipanAGLGTWRTEAVF--SEEAL--IQVPSDIPLQ-SAATLGVNPCTAYRMLMDFEQLQ 106
Cdd:PLN03154   84 GVSKVVD--SDDPNFKPGDLI----SGITGWEEYSLIrsSDNQLrkIQLQDDIPLSyHLGLLGMAGFTAYAGFYEVCSPK 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283 107 PGDSVIQNASNSGVGQAVIQIAAalgLRTINVVRDRPDIQKLsDRLKS-LGAEHVITEEE-------LRR--PEMKNFFK 176
Cdd:PLN03154  158 KGDSVFVSAASGAVGQLVGQLAK---LHGCYVVGSAGSSQKV-DLLKNkLGFDEAFNYKEepdldaaLKRyfPEGIDIYF 233
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167503283 177 DMpqprlalncVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSL-----LIFKDLKLRGFWLSQW 239
Cdd:PLN03154  234 DN---------VGGDMLDAALLNMKIHGRIAVCGMVSLNSLSASQGIhnlynLISKRIRMQGFLQSDY 292
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
19-54 5.81e-05

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: 44.14  E-value: 5.81e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1167503283  19 GFLPE--LPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP 54
Cdd:cd08300    49 GADPEglFPVILGHEGAGIVESVGEGVTSVKPGDHVIP 86
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
95-165 3.05e-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: 41.53  E-value: 3.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167503283  95 AYRMLMDFEQLQPGDSVIQnASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLsDRLKSLGAEHVITEEE 165
Cdd:pfam00291  42 ALNLLLRLKEGEGGKTVVE-ASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKL-LLMRALGAEVVLVGGD 110
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
9-52 4.88e-04

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: 41.01  E-value: 4.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1167503283   9 SDINMIQGNYGfLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV 52
Cdd:cd08298    44 TDLHIVEGDLP-PPKLPLIPGHEIVGRVEAVGPGVTRFSVGDRV 86
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
32-136 8.09e-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: 40.38  E-value: 8.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  32 GVAQVVAvgSNVTGLKPGDWVipanAGLGTWRTEAVFS-EEALIQV-PSDIPLQS-AATLGVNPCTAYRMLMDFEQLQPG 108
Cdd:cd08295    79 GVAKVVD--SGNPDFKVGDLV----WGFTGWEEYSLIPrGQDLRKIdHTDVPLSYyLGLLGMPGLTAYAGFYEVCKPKKG 152
                          90       100
                  ....*....|....*....|....*...
gi 1167503283 109 DSVIQNASNSGVGQAVIQIAAALGLRTI 136
Cdd:cd08295   153 ETVFVSAASGAVGQLVGQLAKLKGCYVV 180
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
9-169 1.37e-03

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: 39.83  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283   9 SDINMIQGnygFLPELPA--VGGNEGVAQVVAVGSNVTGLKPGDWV-IPANAGLGT------------------------ 61
Cdd:cd08283    40 SDLHLYHG---YIPGMKKgdILGHEFMGVVEEVGPEVRNLKVGDRVvVPFTIACGEcfyckrglysqcdntnpsaemakl 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503283  62 --WRTEAVF---------------------SEEALIQVPSDIPLQSAATLGVNPCTAYrMLMDFEQLQPGDSV-IQNAsn 117
Cdd:cd08283   117 ygHAGAGIFgyshltggyaggqaeyvrvpfADVGPFKIPDDLSDEKALFLSDILPTGY-HAAELAEVKPGDTVaVWGC-- 193
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1167503283 118 SGVGQAVIQIAAALGLRTINVVrDRPDiqklsDRL----KSLGAEhVITEEELRRP 169
Cdd:cd08283   194 GPVGLFAARSAKLLGAERVIAI-DRVP-----ERLemarSHLGAE-TINFEEVDDV 242
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
19-54 1.97e-03

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: 39.20  E-value: 1.97e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1167503283  19 GFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP 54
Cdd:cd08301    51 GQTPLFPRILGHEAAGIVESVGEGVTDLKPGDHVLP 86
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
25-52 2.69e-03

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 39.04  E-value: 2.69e-03
                          10        20
                  ....*....|....*....|....*...
gi 1167503283  25 PAVGGNEGVAQVVAVGSNVTGLKPGDWV 52
Cdd:PRK05396   58 PMVVGHEFVGEVVEVGSEVTGFKVGDRV 85
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
94-166 6.96e-03

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


Pssm-ID: 107202 [Multi-domain]  Cd Length: 244  Bit Score: 37.11  E-value: 6.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167503283  94 TAYRMLMDFEQ--LQPGDSVIqnASNSG-VGQAVIQIAAALGLR-TINVVRDRPDIQKlsDRLKSLGAEHVITEEEL 166
Cdd:cd00640    34 GALNLILLAEEegKLPKGVII--ESTGGnTGIALAAAAARLGLKcTIVMPEGASPEKV--AQMRALGAEVVLVPGDF 106
 
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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