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Conserved domains on  [gi|1167803563|ref|NP_057095|]
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enoyl-[acyl-carrier-protein] reductase, mitochondrial isoform a [Homo sapiens]

Protein Classification

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

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

EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0050661
SCOP:  4000090

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
44-373 0e+00

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: 516.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAKVVELKNLELAAVRGSD-VRVKMLAAPINPSDINMIQGNYGFLP----ELPAVGGNEGVAQVVAVGSN 118
Cdd:cd08290     2 KALVYTEHGEPKEVLQLESYEIPPPGPPNeVLVKMLAAPINPADINQIQGVYPIKPpttpEPPAVGGNEGVGEVVKVGSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 119 VTGLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQ 198
Cdd:cd08290    82 VKSLKPGDWVIPLRPGLGTWRTHAVVPADDLIKVPNDVDPEQAATLSVNPCTAYRLLEDFVKLQPGDWVIQNGANSAVGQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 199 AVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLGAEHVITEEELRRPEMKNFFKDMP--QPRLALNCVGGKSSTELLRQL 276
Cdd:cd08290   162 AVIQLAKLLGIKTINVVRDRPDLEELKERLKALGADHVLTEEELRSLLATELLKSAPggRPKLALNCVGGKSATELARLL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 277 ARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQV---PLQDY 353
Cdd:cd08290   242 SPGGTMVTYGGMSGQPVTVPTSLLIFKDITLRGFWLTRWLKRANPEEKEDMLEELAELIREGKLKAPPVEKVtddPLEEF 321
                         330       340
                  ....*....|....*....|
gi 1167803563 354 QSALEASMKPFISSKQILTM 373
Cdd:cd08290   322 KDALANALKGGGGGKQVLVM 341
 
Name Accession Description Interval E-value
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
44-373 0e+00

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: 516.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAKVVELKNLELAAVRGSD-VRVKMLAAPINPSDINMIQGNYGFLP----ELPAVGGNEGVAQVVAVGSN 118
Cdd:cd08290     2 KALVYTEHGEPKEVLQLESYEIPPPGPPNeVLVKMLAAPINPADINQIQGVYPIKPpttpEPPAVGGNEGVGEVVKVGSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 119 VTGLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQ 198
Cdd:cd08290    82 VKSLKPGDWVIPLRPGLGTWRTHAVVPADDLIKVPNDVDPEQAATLSVNPCTAYRLLEDFVKLQPGDWVIQNGANSAVGQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 199 AVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLGAEHVITEEELRRPEMKNFFKDMP--QPRLALNCVGGKSSTELLRQL 276
Cdd:cd08290   162 AVIQLAKLLGIKTINVVRDRPDLEELKERLKALGADHVLTEEELRSLLATELLKSAPggRPKLALNCVGGKSATELARLL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 277 ARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQV---PLQDY 353
Cdd:cd08290   242 SPGGTMVTYGGMSGQPVTVPTSLLIFKDITLRGFWLTRWLKRANPEEKEDMLEELAELIREGKLKAPPVEKVtddPLEEF 321
                         330       340
                  ....*....|....*....|
gi 1167803563 354 QSALEASMKPFISSKQILTM 373
Cdd:cd08290   322 KDALANALKGGGGGKQVLVM 341
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
44-359 9.43e-76

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: 236.97  E-value: 9.43e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPaKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:COG0604     2 KAIVITEFGGP-EVLELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPLPPGLPFIPGSDAAGVVVAVGEGVTGFK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIpANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQI 203
Cdd:COG0604    81 VGDRVA-GLGRGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKPGETVLVHGAAGGVGSAAVQL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 204 AAALGLRTINVVRdRPDiqKLsDRLKSLGAEHVI--TEEELRRPEMKNFFKDmpQPRLALNCVGGKSSTELLRQLARGGT 281
Cdd:COG0604   160 AKALGARVIATAS-SPE--KA-ELLRALGADHVIdyREEDFAERVRALTGGR--GVDVVLDTVGGDTLARSLRALAPGGR 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167803563 282 MVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWKKDHSPDQFKELIltlcDLIRRGQLTAPACSQVPLQDYQSALEA 359
Cdd:COG0604   234 LVSIGAASGAPPPLDLAPLLLKGLTLTGFTLFARDPAERRAALAELA----RLLAAGKLRPVIDRVFPLEEAAEAHRL 307
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
75-358 2.50e-30

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 117.10  E-value: 2.50e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563   75 VKMLAAPINPSDINMIQGNYGFLPELpavgGNEGVAQVVAVGSNVTGLKPGDWVIpanaGL--GTWRTEAVFSEEALIQV 152
Cdd:smart00829   1 IEVRAAGLNFRDVLIALGLYPGEAVL----GGECAGVVTRVGPGVTGLAVGDRVM----GLapGAFATRVVTDARLVVPI 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  153 PSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQAVIQIAAALGLrTINVVRDRPDIQKLsdrLKSL 231
Cdd:smart00829  73 PDGWSFEEAATVPVVFLTAYYALVDLARLRPGESVlIHAAA-GGVGQAAIQLARHLGA-EVFATAGSPEKRDF---LRAL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  232 G--AEHVIT------EEELRRpemknffkdMPQPR---LALNCVGGksstELLRQ----LARGGTMVtygGMAKQPVVA- 295
Cdd:smart00829 148 GipDDHIFSsrdlsfADEILR---------ATGGRgvdVVLNSLSG----EFLDAslrcLAPGGRFV---EIGKRDIRDn 211
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167803563  296 -SVSLLIF-KDLKLRGFWLSQWKKDhsPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALE 358
Cdd:smart00829 212 sQLAMAPFrPNVSYHAVDLDALEEG--PDRIRELLAEVLELFAEGVLRPLPVTVFPISDAEDAFR 274
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
44-373 4.26e-27

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 109.73  E-value: 4.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAkVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:PTZ00354    3 RAVTLKGFGGVD-VLKIGESPKPAPKRNDVLIKVSAAGVNRADTLQRQGKYPPPPGSSEILGLEVAGYVEDVGSDVKRFK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIPANAGlGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQI 203
Cdd:PTZ00354   82 EGDRVMALLPG-GGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQSVLIHAGASGVGTAAAQL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 204 AAALGLRTINVVRDRPDIQKlsdrLKSLGAEHVIteeelRRPEMKNF---FKDMPQPR---LALNCVGGKSSTELLRQLA 277
Cdd:PTZ00354  161 AEKYGAATIITTSSEEKVDF----CKKLAAIILI-----RYPDEEGFapkVKKLTGEKgvnLVLDCVGGSYLSETAEVLA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 278 RGGTMVTYGGM--AKQPVVASVSLL------IFKDLKLRGfwlSQWKKDHSpDQFKELILTlcdLIRRGQLTAPACSQVP 349
Cdd:PTZ00354  232 VDGKWIVYGFMggAKVEKFNLLPLLrkrasiIFSTLRSRS---DEYKADLV-ASFEREVLP---YMEEGEIKPIVDRTYP 304
                         330       340
                  ....*....|....*....|....*..
gi 1167803563 350 LQDYQSA---LEASMKpfiSSKQILTM 373
Cdd:PTZ00354  305 LEEVAEAhtfLEQNKN---IGKVVLTV 328
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
195-328 1.31e-17

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 78.03  E-value: 1.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 195 GVGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSLGAEHVITEEELRRPE-MKNFFKDMpQPRLALNCVG-GKSSTEL 272
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSE---EKL-ELAKELGADHVINPKETDLVEeIKELTGGK-GVDVVFDCVGsPATLEQA 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1167803563 273 LRQLARGGTMVTYgGMAKQPVVASVSLLIFKDLKLRGFWLSqwkkdhSPDQFKELI 328
Cdd:pfam00107  76 LKLLRPGGRVVVV-GLPGGPLPLPLAPLLLKELTILGSFLG------SPEEFPEAL 124
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
51-328 3.41e-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: 63.86  E-value: 3.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  51 HGDPAKV-VELKNLELAAVRGSDVRVKMLAAPINPsdinmiqgnYGFLPELPAVGGNEGVAQVVA--VGSNVTGLKPGDW 127
Cdd:TIGR02825  11 VGYPTDSdFELKTVELPPLNNGEVLLEALFLSVDP---------YMRVAAKRLKEGDTMMGQQVArvVESKNVALPKGTI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 128 VIpanAGLGtWRTEAVFS----EEALIQVPSDIPLQSA-ATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQ 202
Cdd:TIGR02825  82 VL---ASPG-WTSHSISDgkdlEKLLTEWPDTLPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 203 IAAALGLRTINVVRDRPDIqklsDRLKSLGAEHVIT-------EEELRR--PEMKNFFKDMpqprlalncVGGKSSTELL 273
Cdd:TIGR02825 158 IAKLKGCKVVGAAGSDEKV----AYLKKLGFDVAFNyktvkslEETLKKasPDGYDCYFDN---------VGGEFSNTVI 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167803563 274 RQL------ARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWKKDHSPDQFKELI 328
Cdd:TIGR02825 225 GQMkkfgriAICGAISTYNRTGPLPPGPPPEIVIYQELRMEGFIVNRWQGEVRQKALKELL 285
 
Name Accession Description Interval E-value
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
44-373 0e+00

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: 516.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAKVVELKNLELAAVRGSD-VRVKMLAAPINPSDINMIQGNYGFLP----ELPAVGGNEGVAQVVAVGSN 118
Cdd:cd08290     2 KALVYTEHGEPKEVLQLESYEIPPPGPPNeVLVKMLAAPINPADINQIQGVYPIKPpttpEPPAVGGNEGVGEVVKVGSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 119 VTGLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQ 198
Cdd:cd08290    82 VKSLKPGDWVIPLRPGLGTWRTHAVVPADDLIKVPNDVDPEQAATLSVNPCTAYRLLEDFVKLQPGDWVIQNGANSAVGQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 199 AVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLGAEHVITEEELRRPEMKNFFKDMP--QPRLALNCVGGKSSTELLRQL 276
Cdd:cd08290   162 AVIQLAKLLGIKTINVVRDRPDLEELKERLKALGADHVLTEEELRSLLATELLKSAPggRPKLALNCVGGKSATELARLL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 277 ARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQV---PLQDY 353
Cdd:cd08290   242 SPGGTMVTYGGMSGQPVTVPTSLLIFKDITLRGFWLTRWLKRANPEEKEDMLEELAELIREGKLKAPPVEKVtddPLEEF 321
                         330       340
                  ....*....|....*....|
gi 1167803563 354 QSALEASMKPFISSKQILTM 373
Cdd:cd08290   322 KDALANALKGGGGGKQVLVM 341
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
46-372 5.43e-100

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: 299.19  E-value: 5.43e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  46 LVYGHHGDPA-KVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKP 124
Cdd:cd05282     1 VVYTQFGEPLpLVLELVSLPIPPPGPGEVLVRMLAAPINPSDLITISGAYGSRPPLPAVPGNEGVGVVVEVGSGVSGLLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 125 GDWVIPAnAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIA 204
Cdd:cd05282    81 GQRVLPL-GGEGTWQEYVVAPADDLIPVPDSISDEQAAMLYINPLTAWLMLTEYLKLPPGDWVIQNAANSAVGRMLIQLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 205 AALGLRTINVVRDRpdiqKLSDRLKSLGAEHVITEEELR-RPEMKNFFKDMPqPRLALNCVGGKSSTELLRQLARGGTMV 283
Cdd:cd05282   160 KLLGFKTINVVRRD----EQVEELKALGADEVIDSSPEDlAQRVKEATGGAG-ARLALDAVGGESATRLARSLRPGGTLV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 284 TYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEASMKP 363
Cdd:cd05282   235 NYGLLSGEPVPFPRSVFIFKDITVRGFWLRQWLHSATKEAKQETFAEVIKLVEAGVLTTPVGAKFPLEDFEEAVAAAEQP 314

                  ....*....
gi 1167803563 364 FISSKQILT 372
Cdd:cd05282   315 GRGGKVLLT 323
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
44-359 9.43e-76

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: 236.97  E-value: 9.43e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPaKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:COG0604     2 KAIVITEFGGP-EVLELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPLPPGLPFIPGSDAAGVVVAVGEGVTGFK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIpANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQI 203
Cdd:COG0604    81 VGDRVA-GLGRGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKPGETVLVHGAAGGVGSAAVQL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 204 AAALGLRTINVVRdRPDiqKLsDRLKSLGAEHVI--TEEELRRPEMKNFFKDmpQPRLALNCVGGKSSTELLRQLARGGT 281
Cdd:COG0604   160 AKALGARVIATAS-SPE--KA-ELLRALGADHVIdyREEDFAERVRALTGGR--GVDVVLDTVGGDTLARSLRALAPGGR 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167803563 282 MVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWKKDHSPDQFKELIltlcDLIRRGQLTAPACSQVPLQDYQSALEA 359
Cdd:COG0604   234 LVSIGAASGAPPPLDLAPLLLKGLTLTGFTLFARDPAERRAALAELA----RLLAAGKLRPVIDRVFPLEEAAEAHRL 307
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
44-363 1.74e-68

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: 218.36  E-value: 1.74e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08292     2 RAAVHTQFGDPADVLEIGEVPKPTPGAGEVLVRTTLSPIHNHDLWTIRGTYGYKPELPAIGGSEAVGVVDAVGEGVKGLQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIPAnAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYrMLMDFEQLQPGDSVIQNASNSGVGQAVIQI 203
Cdd:cd08292    82 VGQRVAVA-PVHGTWAEYFVAPADGLVPLPDGISDEVAAQLIAMPLSAL-MLLDFLGVKPGQWLIQNAAGGAVGKLVAML 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 204 AAALGLRTINVVRDRPDIQKLsdrlKSLGAEHVITEEElrrPEMKNFFKDMPQPRL---ALNCVGGKSSTELLRQLARGG 280
Cdd:cd08292   160 AAARGINVINLVRRDAGVAEL----RALGIGPVVSTEQ---PGWQDKVREAAGGAPisvALDSVGGKLAGELLSLLGEGG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 281 TMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEAS 360
Cdd:cd08292   233 TLVSFGSMSGEPMQISSGDLIFKQATVRGFWGGRWSQEMSVEYRKRMIAELLTLALKGQLLLPVEAVFDLGDAAKAAAAS 312

                  ...
gi 1167803563 361 MKP 363
Cdd:cd08292   313 MRP 315
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
44-359 1.78e-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: 174.22  E-value: 1.78e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAkVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08241     2 KAVVCKELGGPE-DLVLEEVPPEPGAPGEVRIRVEAAGVNFPDLLMIQGKYQVKPPLPFVPGSEVAGVVEAVGEGVTGFK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIpANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQI 203
Cdd:cd08241    81 VGDRVV-ALTGQGGFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALVRRARLQPGETVLVLGAAGGVGLAAVQL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 204 AAALGLRTINVVRDRpdiQKLsDRLKSLGAEHVITeeeLRRPEMKNFFKDMPQPR---LALNCVGGKSSTELLRQLARGG 280
Cdd:cd08241   160 AKALGARVIAAASSE---EKL-ALARALGADHVID---YRDPDLRERVKALTGGRgvdVVYDPVGGDVFEASLRSLAWGG 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167803563 281 TMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWKKdHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEA 359
Cdd:cd08241   233 RLLVIGFASGEIPQIPANLLLLKNISVVGVYWGAYAR-REPELLRANLAELFDLLAEGKIRPHVSAVFPLEQAAEALRA 310
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
44-372 1.30e-47

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: 164.31  E-value: 1.30e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAKVVE--LKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTG 121
Cdd:cd08291     2 KALLLEEYGKPLEVKElsLPEPEVPEPGPGEVLIKVEAAPINPSDLGFLKGQYGSTKALPVPPGFEGSGTVVAAGGGPLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 122 -LKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLmDFEQLQPGDSVIQNASNSGVGQAV 200
Cdd:cd08291    82 qSLIGKRVAFLAGSYGTYAEYAVADAQQCLPLPDGVSFEQGASSFVNPLTALGML-ETAREEGAKAVVHTAAASALGRML 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 201 IQIAAALGLRTINVVRdRPDIQKLsdrLKSLGAEHVITEEElrrpemKNFFKDMP------QPRLALNCVGGKSSTELLR 274
Cdd:cd08291   161 VRLCKADGIKVINIVR-RKEQVDL---LKKIGAEYVLNSSD------PDFLEDLKeliaklNATIFFDAVGGGLTGQILL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 275 QLARGGTMVTYGGM-AKQPVVASVSLLIFKDLKLRGFWLSQWKKDHSPD---QFKELILTlcdlirrgQLTAPACSQVPL 350
Cdd:cd08291   231 AMPYGSTLYVYGYLsGKLDEPIDPVDLIFKNKSIEGFWLTTWLQKLGPEvvkKLKKLVKT--------ELKTTFASRYPL 302
                         330       340
                  ....*....|....*....|..
gi 1167803563 351 QDYQSALEASMKPFISSKQILT 372
Cdd:cd08291   303 ALTLEAIAFYSKNMSTGKKLLI 324
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
72-328 3.16e-47

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: 161.72  E-value: 3.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  72 DVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIPANA------------------ 133
Cdd:cd05188     1 EVLVRVEAAGLCGTDLHIRRGGYPPPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNlgcgtcelcrelcpgggi 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 134 ----GLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNAsnSGVGQAVIQIAAALG 208
Cdd:cd05188    81 lgegLDGGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVLKPGDTVlVLGA--GGVGLLAAQLAKAAG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 209 LRTInvVRDRPDiQKLsDRLKSLGAEHVI--TEEELRRPEMKNFFKDmpqPRLALNCVGGKSS-TELLRQLARGGTMVTY 285
Cdd:cd05188   159 ARVI--VTDRSD-EKL-ELAKELGADHVIdyKEEDLEEELRLTGGGG---ADVVIDAVGGPETlAQALRLLRPGGRIVVV 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1167803563 286 GGMAKQPVVASVSLLIFKDLKLRGFWLSqwkkdhSPDQFKELI 328
Cdd:cd05188   232 GGTSGGPPLDDLRRLLFKELTIIGSTGG------TREDFEEAL 268
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
44-356 4.67e-45

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: 157.76  E-value: 4.67e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPaKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08268     2 RAVRFHQFGGP-EVLRIEELPVPAPGAGEVLIRVEAIGLNRADAMFRRGAYIEPPPLPARLGYEAAGVVEAVGAGVTGFA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVI---PANAGL-GTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQA 199
Cdd:cd08268    81 VGDRVSvipAADLGQyGTYAEYALVPAAAVVKLPDGLSFVEAAALWMQYLTAYGALVELAGLRPGDSVLITAASSSVGLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 200 VIQIAAALGLRTINVVRDRpdiQKlSDRLKSLGAEHVI--TEEELRRPEMKnfFKDMPQPRLALNCVGGKSSTELLRQLA 277
Cdd:cd08268   161 AIQIANAAGATVIATTRTS---EK-RDALLALGAAHVIvtDEEDLVAEVLR--ITGGKGVDVVFDPVGGPQFAKLADALA 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167803563 278 RGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWKKDhsPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSA 356
Cdd:cd08268   235 PGGTLVVYGALSGEPTPFPLKAALKKSLTFRGYSLDEITLD--PEARRRAIAFILDGLASGALKPVVDRVFPFDDIVEA 311
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
44-360 2.12e-42

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: 150.02  E-value: 2.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPaKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLP--ELPAVGGNEGVAQVVAVGSNVTG 121
Cdd:cd05289     2 KAVRIHEYGGP-EVLELADVPTPEPGPGEVLVKVHAAGVNPVDLKIREGLLKAAFplTLPLIPGHDVAGVVVAVGPGVTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 122 LKPGDWVI--PANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQ 198
Cdd:cd05289    81 FKVGDEVFgmTPFTRGGAYAEYVVVPADELALKPANLSFEEAAALPLAGLTAWQALFELGGLKAGQTVlIHGAA-GGVGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 199 AVIQIAAALGLRTINVVRDRpdiqkLSDRLKSLGAEHVI--TEEELRRPEMKNFFKdmpqprLALNCVGGKSSTELLRQL 276
Cdd:cd05289   160 FAVQLAKARGARVIATASAA-----NADFLRSLGADEVIdyTKGDFERAAAPGGVD------AVLDTVGGETLARSLALV 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 277 ARGGTMVTYGGMAKQPVVASvslliFKDLKLRGFWLSQwkkdhSPDQFKEliltLCDLIRRGQLTAPACSQVPLQDYQSA 356
Cdd:cd05289   229 KPGGRLVSIAGPPPAEQAAK-----RRGVRAGFVFVEP-----DGEQLAE----LAELVEAGKLRPVVDRVFPLEDAAEA 294

                  ....
gi 1167803563 357 LEAS 360
Cdd:cd05289   295 HERL 298
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
44-358 6.10e-39

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: 141.63  E-value: 6.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPaKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08266     2 KAVVIRGHGGP-EVLEYGDLPEPEPGPDEVLVRVKAAALNHLDLWVRRGMPGIKLPLPHILGSDGAGVVEAVGPGVTNVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIpANAGLGTWRTE---------------------------AVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLM 176
Cdd:cd08266    81 PGQRVV-IYPGISCGRCEyclagrenlcaqygilgehvdggyaeyVAVPARNLLPIPDNLSFEEAAAAPLTFLTAWHMLV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 177 DFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSLGAEHVI--TEEELRRPEMKNFFKdm 254
Cdd:cd08266   160 TRARLRPGETVLVHGAGSGVGSAAIQIAKLFGATVIATAGSE---DKL-ERAKELGADYVIdyRKEDFVREVRELTGK-- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 255 PQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSqwkkdhSPDQFKELIltlcDL 334
Cdd:cd08266   234 RGVDVVVEHVGAATWEKSLKSLARGGRLVTCGATTGYEAPIDLRHVFWRQLSILGSTMG------TKAELDEAL----RL 303
                         330       340
                  ....*....|....*....|....
gi 1167803563 335 IRRGQLTAPACSQVPLQDYQSALE 358
Cdd:cd08266   304 VFRGKLKPVIDSVFPLEEAAEAHR 327
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
43-359 8.65e-38

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 138.32  E-value: 8.65e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  43 VRALVYGHHGDPAKVVELknlELAAVRGSDVRVKMLAAPINPSDINMIQGNYGfLPELPAVGGNEGVAQVVAVGSNVTGL 122
Cdd:COG1064     1 MKAAVLTEPGGPLELEEV---PRPEPGPGEVLVKVEACGVCHSDLHVAEGEWP-VPKLPLVPGHEIVGRVVAVGPGVTGF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 123 KPGDWVI-----------------------PANAGLGTW---RTEAVFSEEALIQVPSDIPLQSAATLGvnpC---TAYR 173
Cdd:COG1064    77 KVGDRVGvgwvdscgtceycrsgrenlcenGRFTGYTTDggyAEYVVVPARFLVKLPDGLDPAEAAPLL---CagiTAYR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 174 MLMDFEqLQPGDSV-IQNAsnSGVGQAVIQIAAALGLRTInVVrDRPDiQKLsDRLKSLGAEHVITEEElrRPEMKNfFK 252
Cdd:COG1064   154 ALRRAG-VGPGDRVaVIGA--GGLGHLAVQIAKALGAEVI-AV-DRSP-EKL-ELARELGADHVVNSSD--EDPVEA-VR 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 253 DMPQPRLALNCVGGKSSTEL-LRQLARGGTMVTyGGMAKQPVVASVSLLIFKDLKLRGfwlSQWkkdHSPDQFKELIltl 331
Cdd:COG1064   224 ELTGADVVIDTVGAPATVNAaLALLRRGGRLVL-VGLPGGPIPLPPFDLILKERSIRG---SLI---GTRADLQEML--- 293
                         330       340
                  ....*....|....*....|....*...
gi 1167803563 332 cDLIRRGQLTaPACSQVPLQDYQSALEA 359
Cdd:COG1064   294 -DLAAEGKIK-PEVETIPLEEANEALER 319
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
44-373 4.00e-37

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: 136.56  E-value: 4.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAkVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08253     2 RAIRYHEFGAPD-VLRLGDLPVPTPGPGEVLVRVHASGVNPVDTYIRAGAYPGLPPLPYVPGSDGAGVVEAVGEGVDGLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIPANAGL----GTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQA 199
Cdd:cd08253    81 VGDRVWLTNLGWgrrqGTAAEYVVVPADQLVPLPDGVSFEQGAALGIPALTAYRALFHRAGAKAGETVLVHGGSGAVGHA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 200 VIQIAAALGLRTINVVRDRPDIQklsdRLKSLGAEHVI--TEEELrRPEMKNfFKDMPQPRLALNCVGGKSSTELLRQLA 277
Cdd:cd08253   161 AVQLARWAGARVIATASSAEGAE----LVRQAGADAVFnyRAEDL-ADRILA-ATAGQGVDVIIEVLANVNLAKDLDVLA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 278 RGGTMVTYGGMAKQPVVASVSLLiFKDLKLRGFWLSQwkkdHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSAL 357
Cdd:cd08253   235 PGGRIVVYGSGGLRGTIPINPLM-AKEASIRGVLLYT----ATPEERAAAAEAIAAGLADGALRPVIAREYPLEEAAAAH 309
                         330
                  ....*....|....*.
gi 1167803563 358 EASMKPFISSKQILTM 373
Cdd:cd08253   310 EAVESGGAIGKVVLDP 325
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
44-359 5.52e-37

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: 136.24  E-value: 5.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAkVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08273     2 REVVVTRRGGPE-VLKVVEADLPEPAAGEVVVKVEASGVSFADVQMRRGLYPDQPPLPFTPGYDLVGRVDALGSGVTGFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVipanAGL---GTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQA 199
Cdd:cd08273    81 VGDRV----AALtrvGGNAEYINLDAKYLVPVPEGVDAAEAVCLVLNYVTAYQMLHRAAKVLTGQRVlIHGAS-GGVGQA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 200 VIQIAAALGLRTINVVRDRpdiqkLSDRLKSLGAEHViteeeLRRPemKNFFKDMPQPRLA---LNCVGGKSSTELLRQL 276
Cdd:cd08273   156 LLELALLAGAEVYGTASER-----NHAALRELGATPI-----DYRT--KDWLPAMLTPGGVdvvFDGVGGESYEESYAAL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 277 ARGGTMVTYG-------GMAKQPVVASVSLLIFK------DLKLRGFWLSQWKKDHsPDQFKELILTLCDLIRRGQLTAP 343
Cdd:cd08273   224 APGGTLVCYGgnssllqGRRSLAALGSLLARLAKlkllptGRRATFYYVWRDRAED-PKLFRQDLTELLDLLAKGKIRPK 302
                         330
                  ....*....|....*.
gi 1167803563 344 ACSQVPLQDYQSALEA 359
Cdd:cd08273   303 IAKRLPLSEVAEAHRL 318
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
44-359 5.28e-31

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: 119.85  E-value: 5.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPaKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGflPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd05286     1 KAVRIHKTGGP-EVLEYEDVPVPEPGPGEVLVRNTAIGVNFIDTYFRSGLYP--LPLPFVLGVEGAGVVEAVGPGVTGFK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIPANAgLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQI 203
Cdd:cd05286    78 VGDRVAYAGP-PGAYAEYRVVPASRLVKLPDGISDETAAALLLQGLTAHYLLRETYPVKPGDTVLVHAAAGGVGLLLTQW 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 204 AAALGLRTINVVrDRPDIQKLSdrlKSLGAEHVI--TEEELrRPEMKnffkdmpqpRL--------ALNCVGGKSSTELL 273
Cdd:cd05286   157 AKALGATVIGTV-SSEEKAELA---RAAGADHVInyRDEDF-VERVR---------EItggrgvdvVYDGVGKDTFEGSL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 274 RQLARGGTMVTYgGMAKQPVVA-SVSLLIFKDLKL-RGfwlSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQ 351
Cdd:cd05286   223 DSLRPRGTLVSF-GNASGPVPPfDLLRLSKGSLFLtRP---SLFHYIATREELLARAAELFDAVASGKLKVEIGKRYPLA 298
                         330
                  ....*....|.
gi 1167803563 352 DY---QSALEA 359
Cdd:cd05286   299 DAaqaHRDLES 309
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
75-358 2.50e-30

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 117.10  E-value: 2.50e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563   75 VKMLAAPINPSDINMIQGNYGFLPELpavgGNEGVAQVVAVGSNVTGLKPGDWVIpanaGL--GTWRTEAVFSEEALIQV 152
Cdd:smart00829   1 IEVRAAGLNFRDVLIALGLYPGEAVL----GGECAGVVTRVGPGVTGLAVGDRVM----GLapGAFATRVVTDARLVVPI 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  153 PSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQAVIQIAAALGLrTINVVRDRPDIQKLsdrLKSL 231
Cdd:smart00829  73 PDGWSFEEAATVPVVFLTAYYALVDLARLRPGESVlIHAAA-GGVGQAAIQLARHLGA-EVFATAGSPEKRDF---LRAL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  232 G--AEHVIT------EEELRRpemknffkdMPQPR---LALNCVGGksstELLRQ----LARGGTMVtygGMAKQPVVA- 295
Cdd:smart00829 148 GipDDHIFSsrdlsfADEILR---------ATGGRgvdVVLNSLSG----EFLDAslrcLAPGGRFV---EIGKRDIRDn 211
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167803563  296 -SVSLLIF-KDLKLRGFWLSQWKKDhsPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALE 358
Cdd:smart00829 212 sQLAMAPFrPNVSYHAVDLDALEEG--PDRIRELLAEVLELFAEGVLRPLPVTVFPISDAEDAFR 274
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
72-359 7.55e-29

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: 113.43  E-value: 7.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  72 DVRVKMLAAPINPSDINMIQGNYGFLPELPavgGNEGVAQVVAVGSNVTGLKPGDWVipanAGL--GTWRTEAVFSEEAL 149
Cdd:cd05195     2 EVEVEVKAAGLNFRDVLVALGLLPGDETPL---GLECSGIVTRVGSGVTGLKVGDRV----MGLapGAFATHVRVDARLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 150 IQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQAVIQIAAALGLRTINVVRDRPDIqklsDRL 228
Cdd:cd05195    75 VKIPDSLSFEEAATLPVAYLTAYYALVDLARLQKGESVlIHAAA-GGVGQAAIQLAQHLGAEVFATVGSEEKR----EFL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 229 KSLG--AEHVITEeelRRPEMKNFFKDMPQPR---LALNCVGGKSSTELLRQLARGGTMVtygGMAKQPVVA--SVSLLI 301
Cdd:cd05195   150 RELGgpVDHIFSS---RDLSFADGILRATGGRgvdVVLNSLSGELLRASWRCLAPFGRFV---EIGKRDILSnsKLGMRP 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1167803563 302 F-KDLKLRGFWLSQWKKdHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEA 359
Cdd:cd05195   224 FlRNVSFSSVDLDQLAR-ERPELLRELLREVLELLEAGVLKPLPPTVVPSASEIDAFRL 281
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
44-358 2.09e-28

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: 112.92  E-value: 2.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPaKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEgVA-QVVAVGSNVTGL 122
Cdd:cd05276     2 KAIVIKEPGGP-EVLELGEVPKPAPGPGEVLIRVAAAGVNRADLLQRQGLYPPPPGASDILGLE-VAgVVVAVGPGVTGW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 123 KPGDWVipanAGL---GTWRTEAVFSEEALIQVPSDIPLQSAATLgvnP---CTAYRMLMDFEQLQPGDSVIQNASNSGV 196
Cdd:cd05276    80 KVGDRV----CALlagGGYAEYVVVPAGQLLPVPEGLSLVEAAAL---PevfFTAWQNLFQLGGLKAGETVLIHGGASGV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 197 GQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSLGAEHVITeeelRRPEmkNF---FKDMPQPR---LALNCVGGKSST 270
Cdd:cd05276   153 GTAAIQLAKALGARVIATAGSE---EKL-EACRALGADVAIN----YRTE--DFaeeVKEATGGRgvdVILDMVGGDYLA 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 271 ELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWL-SQwkkdhsPDQFK-----ELILTLCDLIRRGQLTAPA 344
Cdd:cd05276   223 RNLRALAPDGRLVLIGLLGGAKAELDLAPLLRKRLTLTGSTLrSR------SLEEKaalaaAFREHVWPLFASGRIRPVI 296
                         330
                  ....*....|....
gi 1167803563 345 CSQVPLQDYQSALE 358
Cdd:cd05276   297 DKVFPLEEAAEAHR 310
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
47-362 2.80e-28

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: 112.31  E-value: 2.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  47 VYGHHGDPAkVVELKNLE--LAAVRGSDVRVKMLAAPINPSDINMIQGN-YGFLPE-LPAVGGNEGVAQVVAVGSNVTGL 122
Cdd:cd08267     2 VYTRYGSPE-VLLLLEVEvpIPTPKPGEVLVKVHAASVNPVDWKLRRGPpKLLLGRpFPPIPGMDFAGEVVAVGSGVTRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 123 KPGDWVIPANA--GLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAV 200
Cdd:cd08267    81 KVGDEVFGRLPpkGGGALAEYVVAPESGLAKKPEGVSFEEAAALPVAGLTALQALRDAGKVKPGQRVLINGASGGVGTFA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 201 IQIAAALGLRTINVVRDRpdiqKLsDRLKSLGAEHVI--TEEelrrpemkNFFKDMPQPR---LALNCVGGKSST--ELL 273
Cdd:cd08267   161 VQIAKALGAHVTGVCSTR----NA-ELVRSLGADEVIdyTTE--------DFVALTAGGEkydVIFDAVGNSPFSlyRAS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 274 RQLARGGTMVTYGGMAKQPVVASVSLLIFkdlklrGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDY 353
Cdd:cd08267   228 LALKPGGRYVSVGGGPSGLLLVLLLLPLT------LGGGGRRLKFFLAKPNAEDLEQLAELVEEGKLKPVIDSVYPLEDA 301

                  ....*....
gi 1167803563 354 QSALEASMK 362
Cdd:cd08267   302 PEAYRRLKS 310
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
44-341 9.27e-28

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: 111.11  E-value: 9.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAkVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08272     2 KALVLESFGGPE-VFELREVPRPQPGPGQVLVRVHASGVNPLDTKIRRGGAAARPPLPAILGCDVAGVVEAVGEGVTRFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIPANAGL----GTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQA 199
Cdd:cd08272    81 VGDEVYGCAGGLgglqGSLAEYAVVDARLLALKPANLSMREAAALPLVGITAWEGLVDRAAVQAGQTVLIHGGAGGVGHV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 200 VIQIAAALGLRTINVVRDRpdiqKLsDRLKSLGAEHVI------TEEELRRPEMKNFfkdmpqpRLALNCVGGKSSTELL 273
Cdd:cd08272   161 AVQLAKAAGARVYATASSE----KA-AFARSLGADPIIyyretvVEYVAEHTGGRGF-------DVVFDTVGGETLDASF 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167803563 274 RQLARGGTMVTYGGMAKQpvvaSVSLLIFKDLKLRG-FWLSQWKKDHSPDQFKELILTLCDLIRRGQLT 341
Cdd:cd08272   229 EAVALYGRVVSILGGATH----DLAPLSFRNATYSGvFTLLPLLTGEGRAHHGEILREAARLVERGQLR 293
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
44-287 1.17e-27

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: 111.14  E-value: 1.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPaKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08275     1 RAVVLTGFGGL-DKLKVEKEALPEPSSGEVRVRVEACGLNFADLMARQGLYDSAPKPPFVPGFECAGTVEAVGEGVKDFK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIpanaGL---GTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQNASnSGVGQA 199
Cdd:cd08275    80 VGDRVM----GLtrfGGYAEVVNVPADQVFPLPDGMSFEEAAAFPVNYLTAYYALFELGNLRPGQSVlVHSAA-GGVGLA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 200 VIQIAAAlgLRTINVVRDrPDIQKLsDRLKSLGAEHVITEEELR-RPEMKNFfkdMPQP-RLALNCVGGKSSTELLRQLA 277
Cdd:cd08275   155 AGQLCKT--VPNVTVVGT-ASASKH-EALKENGVTHVIDYRTQDyVEEVKKI---SPEGvDIVLDALGGEDTRKSYDLLK 227
                         250
                  ....*....|
gi 1167803563 278 RGGTMVTYGG 287
Cdd:cd08275   228 PMGRLVVYGA 237
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
62-309 2.71e-27

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: 109.93  E-value: 2.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  62 NLELAAV-----RGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP------ 130
Cdd:cd08276    14 NLKLVEEpvpepGPGEVLVRVHAVSLNYRDLLILNGRYPPPVKDPLIPLSDGAGEVVAVGEGVTRFKVGDRVVPtffpnw 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 131 ---------ANAGL-----GTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSV-IQnaSNSG 195
Cdd:cd08276    94 ldgpptaedEASALggpidGVLAEYVVLPEEGLVRAPDHLSFEEAATLPCAGLTAWNALFGLGPLKPGDTVlVQ--GTGG 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 196 VGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSLGAEHVIT-------EEELRRpemknffkdMPQPR---LALNCVG 265
Cdd:cd08276   172 VSLFALQFAKAAGARVIATSSSD---EKL-ERAKALGADHVINyrttpdwGEEVLK---------LTGGRgvdHVVEVGG 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1167803563 266 GKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRG 309
Cdd:cd08276   239 PGTLAQSIKAVAPGGVISLIGFLSGFEAPVLLLPLLTKGATLRG 282
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
44-373 4.26e-27

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 109.73  E-value: 4.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAkVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:PTZ00354    3 RAVTLKGFGGVD-VLKIGESPKPAPKRNDVLIKVSAAGVNRADTLQRQGKYPPPPGSSEILGLEVAGYVEDVGSDVKRFK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIPANAGlGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQI 203
Cdd:PTZ00354   82 EGDRVMALLPG-GGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQSVLIHAGASGVGTAAAQL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 204 AAALGLRTINVVRDRPDIQKlsdrLKSLGAEHVIteeelRRPEMKNF---FKDMPQPR---LALNCVGGKSSTELLRQLA 277
Cdd:PTZ00354  161 AEKYGAATIITTSSEEKVDF----CKKLAAIILI-----RYPDEEGFapkVKKLTGEKgvnLVLDCVGGSYLSETAEVLA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 278 RGGTMVTYGGM--AKQPVVASVSLL------IFKDLKLRGfwlSQWKKDHSpDQFKELILTlcdLIRRGQLTAPACSQVP 349
Cdd:PTZ00354  232 VDGKWIVYGFMggAKVEKFNLLPLLrkrasiIFSTLRSRS---DEYKADLV-ASFEREVLP---YMEEGEIKPIVDRTYP 304
                         330       340
                  ....*....|....*....|....*..
gi 1167803563 350 LQDYQSA---LEASMKpfiSSKQILTM 373
Cdd:PTZ00354  305 LEEVAEAhtfLEQNKN---IGKVVLTV 328
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
44-363 7.29e-26

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: 106.38  E-value: 7.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYghHGdpAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPElPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:COG1063     2 KALVL--HG--PGDLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRP-PLVLGHEFVGEVVEVGEGVTGLK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVI---------------------PANAGLGTWRTEAVFSE------EALIQVPSDIPLQSAATlgVNP-CTAYRML 175
Cdd:COG1063    77 VGDRVVvepnipcgecrycrrgrynlcENLQFLGIAGRDGGFAEyvrvpaANLVKVPDGLSDEAAAL--VEPlAVALHAV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 176 MDFeQLQPGDSV-IQNAsnsG-VGQAVIQIAAALGLRTINVVRDRPDiqKLsDRLKSLGAEHVITeeeLRRPEMKNFFKD 253
Cdd:COG1063   155 ERA-GVKPGDTVlVIGA---GpIGLLAALAARLAGAARVIVVDRNPE--RL-ELARELGADAVVN---PREEDLVEAVRE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 254 MPQPR---LALNCVGGKSS-TELLRQLARGGTMVTYGGMAKqPVVASVSLLIFKDLKLRGFWLsqwkkdHSPDQFKELIl 329
Cdd:COG1063   225 LTGGRgadVVIEAVGAPAAlEQALDLVRPGGTVVLVGVPGG-PVPIDLNALVRKELTLRGSRN------YTREDFPEAL- 296
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1167803563 330 tlcDLIRRGQL-TAPACS-QVPLQDYQSALEASMKP 363
Cdd:COG1063   297 ---ELLASGRIdLEPLIThRFPLDDAPEAFEAAADR 329
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
44-284 1.20e-25

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: 105.74  E-value: 1.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVygHHGDPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQgnYGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08249     2 KAAV--LTGPGGGLLVVVDVPVPKPGPDEVLVKVKAVALNPVDWKHQD--YGFIPSYPAILGCDFAGTVVEVGSGVTRFK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVI-------PANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTA-----YRMLMDF-----EQLQPGDS 186
Cdd:cd08249    78 VGDRVAgfvhggnPNDPRNGAFQEYVVADADLTAKIPDNISFEEAATLPVGLVTAalalfQKLGLPLpppkpSPASKGKP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 187 VIQNASNSGVGQAVIQIAAALGLRTINVVrdrpdiqklS----DRLKSLGAEHVI------TEEELRRPEMKNFfkdmpq 256
Cdd:cd08249   158 VLIWGGSSSVGTLAIQLAKLAGYKVITTA---------SpknfDLVKSLGADAVFdyhdpdVVEDIRAATGGKL------ 222
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1167803563 257 pRLALNCVGGKSSTELLRQL---ARGGTMVT 284
Cdd:cd08249   223 -RYALDCISTPESAQLCAEAlgrSGGGKLVS 252
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
56-340 4.94e-25

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: 104.16  E-value: 4.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  56 KVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFlpELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI------ 129
Cdd:cd08279    11 KPLEIEEVELDDPGPGEVLVRIAAAGLCHSDLHVVTGDLPA--PLPAVLGHEGAGVVEEVGPGVTGVKPGDHVVlswipa 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 130 ----------------------------------------PANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLG---- 165
Cdd:cd08279    89 cgtcrycsrgqpnlcdlgagilggqlpdgtrrftadgepvGAMCGLGTFAEYTVVPEASVVKIDDDIPLDRAALLGcgvt 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 166 ------VNpcTAyrmlmdfeQLQPGDS--VIqnaSNSGVGQAVIQIAAALGLRTINVVrDrPDIQKLsDRLKSLGAEHVI 237
Cdd:cd08279   169 tgvgavVN--TA--------RVRPGDTvaVI---GCGGVGLNAIQGARIAGASRIIAV-D-PVPEKL-ELARRFGATHTV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 238 TEEElrrPEMKNFFKDMPQPRL---ALNCVGGKSSTEL-LRQLARGGTMVTYGGMAKQPVVA-SVSLLIFKDLKLRGFWL 312
Cdd:cd08279   233 NASE---DDAVEAVRDLTDGRGadyAFEAVGRAATIRQaLAMTRKGGTAVVVGMGPPGETVSlPALELFLSEKRLQGSLY 309
                         330       340       350
                  ....*....|....*....|....*....|
gi 1167803563 313 --SQWKKDhspdqfkelILTLCDLIRRGQL 340
Cdd:cd08279   310 gsANPRRD---------IPRLLDLYRAGRL 330
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
44-309 1.94e-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: 102.23  E-value: 1.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYghHGDPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08297     2 KAAVV--EEFGEKPYEVKDVPVPEPGPGEVLVKLEASGVCHTDLHAALGDWPVKPKLPLIGGHEGAGVVVAVGPGVSGLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGD-----WVIPA-------------------NAGL---GTWRTEAVFSEEALIQVPSDIPLQSAATL---GVnpcTAYR 173
Cdd:cd08297    80 VGDrvgvkWLYDAcgkceycrtgdetlcpnqkNSGYtvdGTFAEYAIADARYVTPIPDGLSFEQAAPLlcaGV---TVYK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 174 MLMDfEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINV-VRDRPdiQKLSdrlKSLGAEHVIteeelrrpemkNFFK 252
Cdd:cd08297   157 ALKK-AGLKPGDWVVISGAGGGLGHLGVQYAKAMGLRVIAIdVGDEK--LELA---KELGADAFV-----------DFKK 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167803563 253 DMPQPRL-----------ALNCVGGKSSTEL-LRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRG 309
Cdd:cd08297   220 SDDVEAVkeltggggahaVVVTAVSAAAYEQaLDYLRPGGTLVCVGLPPGGFIPLDPFDLVLRGITIVG 288
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
52-309 2.81e-24

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 102.08  E-value: 2.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  52 GDPAKVVELknlELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLpeLPAVGGNEGVAQVVAVGSNVTGLKPGDWVI-- 129
Cdd:COG1062     1 GGPLEIEEV---ELDEPRPGEVLVRIVAAGLCHSDLHVRDGDLPVP--LPAVLGHEGAGVVEEVGPGVTGVAPGDHVVls 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 130 -----------------------PANA-----------------------GLGTWRTEAVFSEEALIQVPSDIPLQSAAT 163
Cdd:COG1062    76 fipscghcrycasgrpalceagaALNGkgtlpdgtsrlssadgepvghffGQSSFAEYAVVPERSVVKVDKDVPLELAAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 164 LGvnpC---TAYRMLMDFEQLQPGDSVIqnasnsGVGQAVIQIAAALGLRTINVVrdrpDIqkLSDRL---KSLGAEHVI 237
Cdd:COG1062   156 LG---CgvqTGAGAVLNTAKVRPGDTVAvfg-lgGVGLSAVQGARIAGASRIIAV----DP--VPEKLelaRELGATHTV 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167803563 238 --TEEELRRpEMKNFFKDMPQprLALNCVGgksSTELLRQ----LARGGTMVTYG-GMAKQPVVASVSLLIFKDLKLRG 309
Cdd:COG1062   226 npADEDAVE-AVRELTGGGVD--YAFETTG---NPAVIRQaleaLRKGGTVVVVGlAPPGAEISLDPFQLLLTGRTIRG 298
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
44-309 2.88e-24

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: 101.66  E-value: 2.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHG-DPAKVVELKNLElaaVRGSDVRVKMLAAPINPSDINMIQGnYGFLPeLPAVGGNEGVAQVVAVGSNVTGL 122
Cdd:cd08264     2 KALVFEKSGiENLKVEDVKDPK---PGPGEVLIRVKMAGVNPVDYNVINA-VKVKP-MPHIPGAEFAGVVEEVGDHVKGV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 123 KPGDWVIPAN-----------------------AGLGT---WRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLM 176
Cdd:cd08264    77 KKGDRVVVYNrvfdgtcdmclsgnemlcrnggiIGVVSnggYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYHALK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 177 DFEqLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRdrpdiqklSDRLKSLGAEHVITEEELRrPEMKNFFKdmpQ 256
Cdd:cd08264   157 TAG-LGPGETVVVFGASGNTGIFAVQLAKMMGAEVIAVSR--------KDWLKEFGADEVVDYDEVE-EKVKEITK---M 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1167803563 257 PRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRG 309
Cdd:cd08264   224 ADVVINSLGSSFWDLSLSVLGRGGRLVTFGTLTGGEVKLDLSDLYSKQISIIG 276
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
54-359 4.08e-24

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: 101.24  E-value: 4.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  54 PAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGnygFLP--ELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP- 130
Cdd:cd08259     9 PNKPLQIEEVPDPEPGPGEVLIKVKAAGVCYRDLLFWKG---FFPrgKYPLILGHEIVGTVEEVGEGVERFKPGDRVILy 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 131 -------------------ANAGLGTWRTEAVFSEEA------LIQVPSDIPLQSAATLGVNPCTAYRMLmDFEQLQPGD 185
Cdd:cd08259    86 yyipcgkceyclsgeenlcRNRAEYGEEVDGGFAEYVkvpersLVKLPDNVSDESAALAACVVGTAVHAL-KRAGVKKGD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 186 SVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSLGAEHVIT----EEElrrpemknfFKDMPQPRLAL 261
Cdd:cd08259   165 TVLVTGAGGGVGIHAIQLAKALGARVIAVTRSP---EKL-KILKELGADYVIDgskfSED---------VKKLGGADVVI 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 262 NCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGfwlsqwkkdHSPDQFKELILTLcDLIRRGQLT 341
Cdd:cd08259   232 ELVGSPTIEESLRSLNKGGRLVLIGNVTPDPAPLRPGLLILKEIRIIG---------SISATKADVEEAL-KLVKEGKIK 301
                         330
                  ....*....|....*...
gi 1167803563 342 APACSQVPLQDYQSALEA 359
Cdd:cd08259   302 PVIDRVVSLEDINEALED 319
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
44-372 1.11e-23

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 100.04  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYgHHGDPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGfLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08271     2 KAWVL-PKPGAALQLTLEEIEIPGPGAGEVLVKVHAAGLNPVDWKVIAWGPP-AWSYPHVPGVDGAGVVVAVGAKVTGWK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVipanAGLGTWRTEAVFSE------EALIQVPSDIPLQSAATLgvnPC---TAYRMLMDFEQLQPGDSVIQNASNS 194
Cdd:cd08271    80 VGDRV----AYHASLARGGSFAEytvvdaRAVLPLPDSLSFEEAAAL---PCaglTAYQALFKKLRIEAGRTILITGGAG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 195 GVGQAVIQIAAALGLRTINVVRDRPdiqklSDRLKSLGAEHVITEeelRRPEMKNFFKDMPQPR---LALNCVGGKSSTE 271
Cdd:cd08271   153 GVGSFAVQLAKRAGLRVITTCSKRN-----FEYVKSLGADHVIDY---NDEDVCERIKEITGGRgvdAVLDTVGGETAAA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 272 LLRQLARGGTMVT-YGGMAKQPVVASVSLLIFKDLKLRGFWLSQwkkdhSPDQFKELILT---LCDLIRRGQLTAPACSQ 347
Cdd:cd08271   225 LAPTLAFNGHLVCiQGRPDASPDPPFTRALSVHEVALGAAHDHG-----DPAAWQDLRYAgeeLLELLAAGKLEPLVIEV 299
                         330       340
                  ....*....|....*....|....*
gi 1167803563 348 VPLQDYQSALEASMKPFISSKQILT 372
Cdd:cd08271   300 LPFEQLPEALRALKDRHTRGKIVVT 324
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
72-340 3.00e-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: 93.09  E-value: 3.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  72 DVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVipANAGLGTWRTEAVFSEEALIQ 151
Cdd:cd08250    32 EVLVKNRFVGINASDINFTAGRYDPGVKPPFDCGFEGVGEVVAVGEGVTDFKVGDAV--ATMSFGAFAEYQVVPARHAVP 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 152 VPSDIPlqSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVrDRPDIQKLsdrLKSL 231
Cdd:cd08250   110 VPELKP--EVLPLLVSGLTASIALEEVGEMKSGETVLVTAAAGGTGQFAVQLAKLAGCHVIGTC-SSDEKAEF---LKSL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 232 GAEHVI--TEEELRRPEMKNFfkdmpqPR---LALNCVGGKSSTELLRQLARGGTMVTYGGMA-----KQPVVASVSLLI 301
Cdd:cd08250   184 GCDRPInyKTEDLGEVLKKEY------PKgvdVVYESVGGEMFDTCVDNLALKGRLIVIGFISgyqsgTGPSPVKGATLP 257
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1167803563 302 FKDLK----LRGFWLSQWKKDhspdqFKELILTLCDLIRRGQL 340
Cdd:cd08250   258 PKLLAksasVRGFFLPHYAKL-----IPQHLDRLLQLYQRGKL 295
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
44-309 6.39e-20

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: 89.14  E-value: 6.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYgHHGDPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAvgSNVTGLK 123
Cdd:cd05280     2 KALVV-EEQDGGVSLFLRTLPLDDLPEGDVLIRVHYSSLNYKDALAATGNGGVTRNYPHTPGIDAAGTVVS--SDDPRFR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIPANAGLG--TWRTeavFSEeaLIQVPSD----IP----LQSAATLGVNPCTAYRMLMDFEQ--LQPGDSVIQ-N 190
Cdd:cd05280    79 EGDEVLVTGYDLGmnTDGG---FAE--YVRVPADwvvpLPeglsLREAMILGTAGFTAALSVHRLEDngQTPEDGPVLvT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 191 ASNSGVGQAVIQIAAALGLRTINVVRDrpdiQKLSDRLKSLGAEHVITEEEL----RRPEMKNFFKdmpqprLALNCVGG 266
Cdd:cd05280   154 GATGGVGSIAVAILAKLGYTVVALTGK----EEQADYLKSLGASEVLDREDLldesKKPLLKARWA------GAIDTVGG 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1167803563 267 KSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIfkdlkLRG 309
Cdd:cd05280   224 DVLANLLKQTKYGGVVASCGNAAGPELTTTVLPFI-----LRG 261
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
72-309 7.34e-19

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: 86.22  E-value: 7.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  72 DVRVKMLAAPINPSDINMIQGNYGFlPELPAVGGNEGVAQVVAVGSNVTGLKPGD-----WVIPA--------------- 131
Cdd:cd08245    26 EVLIKIEACGVCHTDLHAAEGDWGG-SKYPLVPGHEIVGEVVEVGAGVEGRKVGDrvgvgWLVGScgrceycrrglenlc 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 132 ----NAGL---GTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEqLQPGDSV-IQNAsnSGVGQAVIQI 203
Cdd:cd08245   105 qkavNTGYttqGGYAEYMVADAEYTVLLPDGLPLAQAAPLLCAGITVYSALRDAG-PRPGERVaVLGI--GGLGHLAVQY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 204 AAALGLRTINVVRDrPDIQKLSdrlKSLGAEHVI-TEEELRRPEMKNFFkdmpqpRLALNCV-GGKSSTELLRQLARGGT 281
Cdd:cd08245   182 ARAMGFETVAITRS-PDKRELA---RKLGADEVVdSGAELDEQAAAGGA------DVILVTVvSGAAAEAALGGLRRGGR 251
                         250       260
                  ....*....|....*....|....*...
gi 1167803563 282 MVTYGGMAKQPVVASVSLLIFKDLKLRG 309
Cdd:cd08245   252 IVLVGLPESPPFSPDIFPLIMKRQSIAG 279
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
48-359 8.05e-19

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: 86.15  E-value: 8.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  48 YGHHGDPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDW 127
Cdd:cd08254     4 WRFHKGSKGLLVLEEVPVPEPGPGEVLVKVKAAGVCHSDLHILDGGVPTLTKLPLTLGHEIAGTVVEVGAGVTNFKVGDR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 128 VI--------------------------PANAGLGTWRTEAVFSEEALIQVPSDIPLQ--SAATLGVNpcTAYRMLMDFE 179
Cdd:cd08254    84 VAvpavipcgacalcrrgrgnlclnqgmPGLGIDGGFAEYIVVPARALVPVPDGVPFAqaAVATDAVL--TPYHAVVRAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 180 QLQPGDSV-IQNAsnSGVGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSLGA-EHVITEEELRRPEMKNffkdmPQP 257
Cdd:cd08254   162 EVKPGETVlVIGL--GGLGLNAVQIAKAMGAAVIAVDIKE---EKL-ELAKELGAdEVLNSLDDSPKDKKAA-----GLG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 258 R---LALNCVGGKSSTEL-LRQLARGGTMVTYG-GMAKQPVvaSVSLLIFKDLKLRGFWlsqwkkDHSPDQFKELIltlc 332
Cdd:cd08254   231 GgfdVIFDFVGTQPTFEDaQKAVKPGGRIVVVGlGRDKLTV--DLSDLIARELRIIGSF------GGTPEDLPEVL---- 298
                         330       340
                  ....*....|....*....|....*..
gi 1167803563 333 DLIRRGQLTaPACSQVPLQDYQSALEA 359
Cdd:cd08254   299 DLIAKGKLD-PQVETRPLDEIPEVLER 324
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
44-328 6.52e-18

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: 84.03  E-value: 6.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPakvVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLpeLPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd05279     2 KAAVLWEKGKP---LSIEEIEVAPPKAGEVRIKVVATGVCHTDLHVIDGKLPTP--LPVILGHEGAGIVESIGPGVTTLK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIPANA-----------------------------------------------GLGTWRTEAVFSEEALIQVPSDI 156
Cdd:cd05279    77 PGDKVIPLFGpqcgkckqclnprpnlcsksrgtngrglmsdgtsrftckgkpihhflGTSTFAEYTVVSEISLAKIDPDA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 157 PLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASnSGVGQAVIQIAAALGLRTINVVrdrpDIQKlsDRL---KSLGA 233
Cdd:cd05279   157 PLEKVCLIGCGFSTGYGAAVNTAKVTPGSTCAVFGL-GGVGLSVIMGCKAAGASRIIAV----DINK--DKFekaKQLGA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 234 EHVITEEELRRP------EMKNFFKDmpqprLALNCVGgksSTELLRQL-----ARGGTMVTYGGMAKQPVVASVSLLIF 302
Cdd:cd05279   230 TECINPRDQDKPivevltEMTDGGVD-----YAFEVIG---SADTLKQAldatrLGGGTSVVVGVPPSGTEATLDPNDLL 301
                         330       340
                  ....*....|....*....|....*.
gi 1167803563 303 KDLKLRGFWLSQWKkdhSPDQFKELI 328
Cdd:cd05279   302 TGRTIKGTVFGGWK---SKDSVPKLV 324
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
44-362 1.01e-17

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: 83.12  E-value: 1.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEG--------------- 108
Cdd:cd08274     2 RAVLLTGHGGLDKLVYRDDVPVPTPAPGEVLIRVGACGVNNTDINTREGWYSTEVDGATDSTGAGeagwwggtlsfpriq 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 109 ----VAQVVAVGSNVTGLKPGDWVIpanagLGTWRTEAVFSEEALIQ---------------VPSD-----IPLQSAATL 164
Cdd:cd08274    82 gadiVGRVVAVGEGVDTARIGERVL-----VDPSIRDPPEDDPADIDyigserdggfaeytvVPAEnaypvNSPLSDVEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 165 GVNPC---TAYRMLmDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDiqklsDRLKSLGAEHVITEEE 241
Cdd:cd08274   157 ATFPCsysTAENML-ERAGVGAGETVLVTGASGGVGSALVQLAKRRGAIVIAVAGAAKE-----EAVRALGADTVILRDA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 242 LRRPEMKNFFKdmPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGfwLSQWkkdhSP 321
Cdd:cd08274   231 PLLADAKALGG--EPVDVVADVVGGPLFPDLLRLLRPGGRYVTAGAIAGPVVELDLRTLYLKDLTLFG--STLG----TR 302
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1167803563 322 DQFKELIltlcDLIRRGQLTaPACSQV-PLQDYQSALEASMK 362
Cdd:cd08274   303 EVFRRLV----RYIEEGEIR-PVVAKTfPLSEIREAQAEFLE 339
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
195-328 1.31e-17

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 78.03  E-value: 1.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 195 GVGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKSLGAEHVITEEELRRPE-MKNFFKDMpQPRLALNCVG-GKSSTEL 272
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSE---EKL-ELAKELGADHVINPKETDLVEeIKELTGGK-GVDVVFDCVGsPATLEQA 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1167803563 273 LRQLARGGTMVTYgGMAKQPVVASVSLLIFKDLKLRGFWLSqwkkdhSPDQFKELI 328
Cdd:pfam00107  76 LKLLRPGGRVVVV-GLPGGPLPLPLAPLLLKELTILGSFLG------SPEEFPEAL 124
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
44-318 1.43e-17

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 82.78  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAKVVELKNLELAAvrgSDVRVKMLAAPINPSDINMIQGnygFLP--ELPAVGGNEGVAQVVAVGSNVTG 121
Cdd:PRK13771    2 KAVILPGFKQGYRIEEVPDPKPGK---DEVVIKVNYAGLCYRDLLQLQG---FYPrmKYPVILGHEVVGTVEEVGENVKG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 122 LKPGDWVIP--------------ANAGLgtWRTEAVFSEE--------------ALIQVPSDIPLQSAAtlgVNPC---T 170
Cdd:PRK13771   76 FKPGDRVASllyapdgtceycrsGEEAY--CKNRLGYGEEldgffaeyakvkvtSLVKVPPNVSDEGAV---IVPCvtgM 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 171 AYRMLMDFEqLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDrpdiqklSDRLKSLG--AEHVITEEELRRpEMK 248
Cdd:PRK13771  151 VYRGLRRAG-VKKGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSS-------ESKAKIVSkyADYVIVGSKFSE-EVK 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167803563 249 NFfkdmPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVA-SVSLLIFKDLKLRGFwLSQWKKD 318
Cdd:PRK13771  222 KI----GGADIVIETVGTPTLEESLRSLNMGGKIIQIGNVDPSPTYSlRLGYIILKDIEIIGH-ISATKRD 287
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
44-284 2.86e-17

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: 81.89  E-value: 2.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAKVVELKNLELAAVRGS-DVRVKMLAAPINPSDINMIQGnYG--FL-------------PELPAVGGNE 107
Cdd:cd08248     2 KAWQIHSYGGIDSLLLLENARIPVIRKPnQVLIKVHAASVNPIDVLMRSG-YGrtLLnkkrkpqsckysgIEFPLTLGRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 108 GVAQVVAVGSNVTGLKPGD--WVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQP-- 183
Cdd:cd08248    81 CSGVVVDIGSGVKSFEIGDevWGAVPPWSQGTHAEYVVVPENEVSKKPKNLSHEEAASLPYAGLTAWSALVNVGGLNPkn 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 184 --GDSVIQNASNSGVGQAVIQIAAALGlrtINVV-----RDRPDIqklsdrlKSLGAEHVIT------EEELRRPEMKNF 250
Cdd:cd08248   161 aaGKRVLILGGSGGVGTFAIQLLKAWG---AHVTttcstDAIPLV-------KSLGADDVIDynnedfEEELTERGKFDV 230
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1167803563 251 FkdmpqprlaLNCVGGKSSTELLRQLARGGTMVT 284
Cdd:cd08248   231 I---------LDTVGGDTEKWALKLLKKGGTYVT 255
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
50-358 4.11e-17

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: 81.51  E-value: 4.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  50 HHGDPAKVVELknlELAAVRGSDVRVKMLAAPINPSDINMIQGNY----GFL-------PELPAVGGNEGVAQVVAVGSN 118
Cdd:cd08240     8 EPGKPLEEVEI---DTPKPPGTEVLVKVTACGVCHSDLHIWDGGYdlggGKTmslddrgVKLPLVLGHEIVGEVVAVGPD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 119 VTGLKPGDWVI-----------------------PANAGL---GTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAY 172
Cdd:cd08240    85 AADVKVGDKVLvypwigcgecpvclagdenlcakGRALGIfqdGGYAEYVIVPHSRYLVDPGGLDPALAATLACSGLTAY 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 173 ---RMLMDFEQLQPgdSVIQNAsnSGVGQAVIQIAAALGLRTInVVRDrPDIQKLsDRLKSLGAEHVITEEELRrpEMKN 249
Cdd:cd08240   165 savKKLMPLVADEP--VVIIGA--GGLGLMALALLKALGPANI-IVVD-IDEAKL-EAAKAAGADVVVNGSDPD--AAKR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 250 FFKDMP-QPRLALNCVGGKSSTEL-LRQLARGGTMVT---YGGMAKQPVVasvsLLIFKDLKLRGFWLSqwkkdhSPDQF 324
Cdd:cd08240   236 IIKAAGgGVDAVIDFVNNSATASLaFDILAKGGKLVLvglFGGEATLPLP----LLPLRALTIQGSYVG------SLEEL 305
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1167803563 325 KELIltlcDLIRRGQLTAPACSQVPLQDYQSALE 358
Cdd:cd08240   306 RELV----ALAKAGKLKPIPLTERPLSDVNDALD 335
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
72-357 4.24e-17

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: 80.93  E-value: 4.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  72 DVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpANAG--LGTWRTEAVFSEEAL 149
Cdd:cd08251     9 EVRIQVRAFSLNFGDLLCVRGLYPTMPPYPFTPGFEASGVVRAVGPHVTRLAVGDEVI-AGTGesMGGHATLVTVPEDQV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 150 IQVPSDIPLQSAATLgvnPCTAYRMLMDFEQ--LQPGDSV-IQNASnSGVGQAVIQIAAALGLrTINVVRDRPDiqKLsD 226
Cdd:cd08251    88 VRKPASLSFEEACAL---PVVFLTVIDAFARagLAKGEHIlIQTAT-GGTGLMAVQLARLKGA-EIYATASSDD--KL-E 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 227 RLKSLGAEHVIT------EEELRRpemknffkdMPQPR---LALNCVGGKSSTELLRQLARGGTMVTYGGMA-KQPVVAS 296
Cdd:cd08251   160 YLKQLGVPHVINyveedfEEEIMR---------LTGGRgvdVVINTLSGEAIQKGLNCLAPGGRYVEIAMTAlKSAPSVD 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167803563 297 VSLLI----FKDLKLRGFWLSqwkkdhSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSAL 357
Cdd:cd08251   231 LSVLSnnqsFHSVDLRKLLLL------DPEFIADYQAEMVSLVEEGELRPTVSRIFPFDDIGEAY 289
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
114-373 1.07e-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: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 79.72  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 114 AVGSNVTGLKPGdwvipanaglGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQpGDSVIQNASN 193
Cdd:cd08270    74 AVGARVVGLGAM----------GAWAELVAVPTGWLAVLPDGVSFAQAATLPVAGVTALRALRRGGPLL-GRRVLVTGAS 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 194 SGVGQAVIQIAAALGLRTINVVRDRPDiqklSDRLKSLGAEH-VITEEELRRPEMKnffkdmpqprLALNCVGGKSSTEL 272
Cdd:cd08270   143 GGVGRFAVQLAALAGAHVVAVVGSPAR----AEGLRELGAAEvVVGGSELSGAPVD----------LVVDSVGGPQLARA 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 273 LRQLARGGTMVTYGGMAKQPVVASVSLLIFK--DLKLRGFWLSQwKKDHSPDqfkelILTLCDLIRRGQLTAPACSQVPL 350
Cdd:cd08270   209 LELLAPGGTVVSVGSSSGEPAVFNPAAFVGGggGRRLYTFFLYD-GEPLAAD-----LARLLGLVAAGRLDPRIGWRGSW 282
                         250       260
                  ....*....|....*....|...
gi 1167803563 351 QDYQSALEASMKPFISSKQILTM 373
Cdd:cd08270   283 TEIDEAAEALLARRFRGKAVLDV 305
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
108-340 1.58e-16

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: 79.45  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 108 GVAQVVAvgSNVTGLKPGDWVIpanaGLGTWRTEAVFSEEALIQV---PSDIPLQSAA-TLGVNPCTAYRMLMDFEQLQP 183
Cdd:cd05288    72 GVGEVVE--SRSPDFKVGDLVS----GFLGWQEYAVVDGASGLRKldpSLGLPLSAYLgVLGMTGLTAYFGLTEIGKPKP 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 184 GDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiQKLsDRLKS-LGAEHVITeeelRRPEmkNFFKDmpqprLALN 262
Cdd:cd05288   146 GETVVVSAAAGAVGSVVGQIAKLLGARVVGIAGSD---EKC-RWLVEeLGFDAAIN----YKTP--DLAEA-----LKEA 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 263 C----------VGGKSSTELLRQLARGGTMVTYGGMA-----KQPVVASVSLLIFKDLKLRGFWLSQWKkdhspDQFKEL 327
Cdd:cd05288   211 ApdgidvyfdnVGGEILDAALTLLNKGGRIALCGAISqynatEPPGPKNLGNIITKRLTMQGFIVSDYA-----DRFPEA 285
                         250
                  ....*....|...
gi 1167803563 328 ILTLCDLIRRGQL 340
Cdd:cd05288   286 LAELAKWLAEGKL 298
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
44-281 3.05e-16

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: 78.42  E-value: 3.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAkVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLpELPAVGGNEGVAQVVAVGSNvtGLK 123
Cdd:cd08243     2 KAIVIEQPGGPE-VLKLREIPIPEPKPGWVLIRVKAFGLNRSEIFTRQGHSPSV-KFPRVLGIEAVGEVEEAPGG--TFT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIPANAGLGtwRT-------EAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGV 196
Cdd:cd08243    78 PGQRVATAMGGMG--RTfdgsyaeYTLVPNEQVYAIDSDLSWAELAALPETYYTAWGSLFRSLGLQPGDTLLIRGGTSSV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 197 GQAVIQIAAALGLRTINVVRDrpdiQKLSDRLKSLGAEHVITE-----EELRRpEMKNFFKdmpqprlALNCVGGKSSTE 271
Cdd:cd08243   156 GLAALKLAKALGATVTATTRS----PERAALLKELGADEVVIDdgaiaEQLRA-APGGFDK-------VLELVGTATLKD 223
                         250
                  ....*....|
gi 1167803563 272 LLRQLARGGT 281
Cdd:cd08243   224 SLRHLRPGGI 233
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
44-286 1.28e-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: 77.41  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPakvVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPelPAVGGNEGVAQVVAVGSNVT--- 120
Cdd:cd08263     2 KAAVLKGPNPP---LTIEEIPVPRPKEGEILIRVAACGVCHSDLHVLKGELPFPP--PFVLGHEISGEVVEVGPNVEnpy 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 121 GLKPGD-----WVIP--------------------ANAGLGT-----------------------WRTEAVFSEEALIQV 152
Cdd:cd08263    77 GLSVGDrvvgsFIMPcgkcrycargkenlcedffaYNRLKGTlydgttrlfrldggpvymysmggLAEYAVVPATALAPL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 153 PSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASnSGVGQAVIQIAAALGLRTINVVrdrpDIQKlsDRLKS-- 230
Cdd:cd08263   157 PESLDYTESAVLGCAGFTAYGALKHAADVRPGETVAVIGV-GGVGSSAIQLAKAFGASPIIAV----DVRD--EKLAKak 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167803563 231 -LGAEHVITEEELRRPEMknfFKDMPQPRLALNCVGGKSSTELLRQ----LARGGTMVTYG 286
Cdd:cd08263   230 eLGATHTVNAAKEDAVAA---IREITGGRGVDVVVEALGKPETFKLaldvVRDGGRAVVVG 287
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
42-360 1.41e-15

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: 77.15  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  42 RVRALVYGHHGDPakvVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGflPELPAVGGNEGVAQVVAVGSNVTG 121
Cdd:cd08278     2 KTTAAVVREPGGP---FVLEDVELDDPRPDEVLVRIVATGICHTDLVVRDGGLP--TPLPAVLGHEGAGVVEAVGSAVTG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 122 LKPGDWVI----------------PA---------NAGL---GTWR--------------------TEAVFSEEALIQVP 153
Cdd:cd08278    77 LKPGDHVVlsfascgecanclsghPAycenffplnFSGRrpdGSTPlslddgtpvhghffgqssfaTYAVVHERNVVKVD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 154 SDIPLQSAATLGvnpC-------TAYRMLmdfeQLQPGDSV-IQNAsnSGVGQAVIQIAAALGLRTINVVrdrpDIQklS 225
Cdd:cd08278   157 KDVPLELLAPLG---CgiqtgagAVLNVL----KPRPGSSIaVFGA--GAVGLAAVMAAKIAGCTTIIAV----DIV--D 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 226 DRL---KSLGAEHVI------TEEELRR--PEMKNFfkdmpqprlALNCVGgksSTELLRQ----LARGGTMVTYgGMAK 290
Cdd:cd08278   222 SRLelaKELGATHVInpkeedLVAAIREitGGGVDY---------ALDTTG---VPAVIEQavdaLAPRGTLALV-GAPP 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 291 QPVVASVSLLifkDLKLRGfwlsqwKK-------DHSPDQFkelILTLCDLIRRGQLtaPA---CSQVPLQDYQSALEAS 360
Cdd:cd08278   289 PGAEVTLDVN---DLLVSG------KTirgviegDSVPQEF---IPRLIELYRQGKF--PFdklVTFYPFEDINQAIADS 354
PRK10754 PRK10754
NADPH:quinone reductase;
51-293 1.55e-15

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 76.70  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  51 HGDPaKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGfLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP 130
Cdd:PRK10754   10 HGGP-EVLQAVEFTPADPAENEVQVENKAIGINYIDTYIRSGLYP-PPSLPSGLGTEAAGVVSKVGSGVKHIKVGDRVVY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 131 ANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLR 210
Cdd:PRK10754   88 AQSALGAYSSVHNVPADKAAILPDAISFEQAAASFLKGLTVYYLLRKTYEIKPDEQFLFHAAAGGVGLIACQWAKALGAK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 211 TINVVRDRPDIQklsdRLKSLGAEHVITEEELRRPEMKNFFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGmAK 290
Cdd:PRK10754  168 LIGTVGSAQKAQ----RAKKAGAWQVINYREENIVERVKEITGGKKVRVVYDSVGKDTWEASLDCLQRRGLMVSFGN-AS 242

                  ...
gi 1167803563 291 QPV 293
Cdd:PRK10754  243 GPV 245
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
53-309 1.80e-15

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: 76.38  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  53 DPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFlPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVipan 132
Cdd:cd05283     7 DASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGP-TKYPLVPGHEIVGIVVAVGSKVTKFKVGDRV---- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 133 aGLGTWR---------------------------------------TEAVFSEEALIQVPSDIPLQSAATL---GVnpcT 170
Cdd:cd05283    82 -GVGCQVdscgtceqcksgeeqycpkgvvtyngkypdgtitqggyaDHIVVDERFVFKIPEGLDSAAAAPLlcaGI---T 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 171 AYRMLMDFeQLQPGDSViqnasnsGV------GQAVIQIAAALGLRTinVVRDRPDIQKlsDRLKSLGAEHVI-TEEElr 243
Cdd:cd05283   158 VYSPLKRN-GVGPGKRV-------GVvgigglGHLAVKFAKALGAEV--TAFSRSPSKK--EDALKLGADEFIaTKDP-- 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167803563 244 rPEMKNFFKDMpqpRLALNCVGGKSS-TELLRQLARGGTMVTYgGMAKQPVVASVSLLIFKDLKLRG 309
Cdd:cd05283   224 -EAMKKAAGSL---DLIIDTVSASHDlDPYLSLLKPGGTLVLV-GAPEEPLPVPPFPLIFGRKSVAG 285
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
73-292 3.37e-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: 75.48  E-value: 3.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  73 VRVKMLAAPINPSDINMIQGNYG--FLPELPAVGGNEGVAQVVAVGSNV-TGLKPGDWVIPANAGLGTWRTEAVFSEEAL 149
Cdd:cd08244    30 VRIAVAAAGVHFVDTQLRSGWGPgpFPPELPYVPGGEVAGVVDAVGPGVdPAWLGRRVVAHTGRAGGGYAELAVADVDSL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 150 IQVPSDIPLQSAATLGVNPCTAYRMLmDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVR-DRpdiqKLsDRL 228
Cdd:cd08244   110 HPVPDGLDLEAAVAVVHDGRTALGLL-DLATLTPGDVVLVTAAAGGLGSLLVQLAKAAGATVVGAAGgPA----KT-ALV 183
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167803563 229 KSLGAEHVITEEELRRPEMKNFFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQP 292
Cdd:cd08244   184 RALGADVAVDYTRPDWPDQVREALGGGGVTVVLDGVGGAIGRAALALLAPGGRFLTYGWASGEW 247
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
44-237 7.90e-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. 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: 74.56  E-value: 7.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAKVVELknlELAAVRGSDVRVKMLAAPINPSDINMIQGNyGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08260     2 RAAVYEEFGEPLEIREV---PDPEPPPDGVVVEVEACGVCRSDWHGWQGH-DPDVTLPHVPGHEFAGVVVEVGEDVSRWR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVI-PANAGLGTWR-------------------TEAVFSEEA--------LIQVPSDIPLQSAATLGVNPCTAYRML 175
Cdd:cd08260    78 VGDRVTvPFVLGCGTCPycragdsnvcehqvqpgftHPGSFAEYVavpradvnLVRLPDDVDFVTAAGLGCRFATAFRAL 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167803563 176 MDFEQLQPGDSVIQNASnSGVGQAVIQIAAALGLRTINVvrdrpDI--QKLsDRLKSLGAEHVI 237
Cdd:cd08260   158 VHQARVKPGEWVAVHGC-GGVGLSAVMIASALGARVIAV-----DIddDKL-ELARELGAVATV 214
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
44-359 1.63e-14

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: 73.75  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAKVVELknlELAAVRGSDVRVKMLAAPINPSDINMIQGNYG--FLPELPAVGGNEGVAQVVAVGSNVTG 121
Cdd:cd05284     2 KAARLYEYGKPLRLEDV---PVPEPGPGQVLVRVGGAGVCHSDLHVIDGVWGgiLPYKLPFTLGHENAGWVEEVGSGVDG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 122 LKPGDWVI-----------------------PANAGLGTWRTEA---VFSEEALIQVPSDIPLQSAATLGVNPCTAYRML 175
Cdd:cd05284    79 LKEGDPVVvhppwgcgtcrycrrgeenycenARFPGIGTDGGFAeylLVPSRRLVKLPRGLDPVEAAPLADAGLTAYHAV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 176 ---MDFeqLQPGDSVIQNASnSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRlksLGAEHVI-----TEEELRRpem 247
Cdd:cd05284   159 kkaLPY--LDPGSTVVVIGV-GGLGHIAVQILRALTPATVIAVDRSEEALKLAER---LGADHVLnasddVVEEVRE--- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 248 knfFKDMPQPRLALNCVGGKSSTEL-LRQLARGG--TMVTYGGMAKQPVVAsvslLIFKDLKLRG-FWLSQwkkdhspDQ 323
Cdd:cd05284   230 ---LTGGRGADAVIDFVGSDETLALaAKLLAKGGryVIVGYGGHGRLPTSD----LVPTEISVIGsLWGTR-------AE 295
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1167803563 324 FKELIltlcDLIRRGQLTaPACSQVPLQDYQSALEA 359
Cdd:cd05284   296 LVEVV----ALAESGKVK-VEITKFPLEDANEALDR 326
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
72-358 2.50e-14

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: 72.99  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  72 DVRVKMLAAPINPSDINMIQGNYGFLpELPAVGGNEGVAQVVAVGSNVTGLKPGDWV--IP------------------- 130
Cdd:cd08261    26 EVLVRVKRVGICGSDLHIYHGRNPFA-SYPRILGHELSGEVVEVGEGVAGLKVGDRVvvDPyiscgecyacrkgrpncce 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 131 ANAGLGTWRTEAvFSE-----EALIQVPSDIPLQSAA-----TLGVNpcTAYRMlmdfeQLQPGDSV-IQNAsnSGVGQA 199
Cdd:cd08261   105 NLQVLGVHRDGG-FAEyivvpADALLVPEGLSLDQAAlveplAIGAH--AVRRA-----GVTAGDTVlVVGA--GPIGLG 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 200 VIQIAAALGLRTInvVRDRPDiqklsDRL---KSLGAEHVI------TEEELRrpEMKNffKDMPQprLALNCVGGKSS- 269
Cdd:cd08261   175 VIQVAKARGARVI--VVDIDD-----ERLefaRELGADDTInvgdedVAARLR--ELTD--GEGAD--VVIDATGNPASm 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 270 TELLRQLARGGTMVtYGGMAKQPVVASVSLLIFKDLKLRGFWLSQwkkdhsPDQFKELIltlcDLIRRGQLTAPA-CSQ- 347
Cdd:cd08261   242 EEAVELVAHGGRVV-LVGLSKGPVTFPDPEFHKKELTILGSRNAT------REDFPDVI----DLLESGKVDPEAlITHr 310
                         330
                  ....*....|.
gi 1167803563 348 VPLQDYQSALE 358
Cdd:cd08261   311 FPFEDVPEAFD 321
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
44-245 3.47e-14

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: 73.14  E-value: 3.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAKVVELknlELAAVRGSDVRVKMLAAPINPSDINMIQGnyGFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08277     4 KAAVAWEAGKPLVIEEI---EVAPPKANEVRIKMLATSVCHTDILAIEG--FKATLFPVILGHEGAGIVESVGEGVTNLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIPANA----------------------------------------------GLGTWRTEAVFSEEALIQVPSDIP 157
Cdd:cd08277    79 PGDKVIPLFIgqcgecsncrsgktnlcqkyranesglmpdgtsrftckgkkiyhflGTSTFSQYTVVDENYVAKIDPAAP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 158 LQSAATLGVNPCTAYRMLMDFEQLQPGDSViqnA--SNSGVGQAVIQIAAALGLRTINVVrdrpDIQKLSD-RLKSLGAE 234
Cdd:cd08277   159 LEHVCLLGCGFSTGYGAAWNTAKVEPGSTV---AvfGLGAVGLSAIMGAKIAGASRIIGV----DINEDKFeKAKEFGAT 231
                         250
                  ....*....|.
gi 1167803563 235 HVITEEELRRP 245
Cdd:cd08277   232 DFINPKDSDKP 242
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
58-309 7.01e-14

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: 71.58  E-value: 7.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  58 VELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFlPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI-------- 129
Cdd:cd08258    14 VELREVPEPEPGPGEVLIKVAAAGICGSDLHIYKGDYDP-VETPVVLGHEFSGTIVEVGPDVEGWKVGDRVVsettfstc 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 130 --------------PANAGLGTWR----TEAVFS-EEALIQVPSDIPLQSAATLgvNP-CTAYRMLMDFEQLQPGDSVIq 189
Cdd:cd08258    93 grcpycrrgdynlcPHRKGIGTQAdggfAEYVLVpEESLHELPENLSLEAAALT--EPlAVAVHAVAERSGIRPGDTVV- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 190 nASNSG-VGQAVIQIAAALGLRTINVvrdrpDIQKLSDRL---KSLGAEHVITEEELRRpEMKNFFKDMPQPRLALNCVG 265
Cdd:cd08258   170 -VFGPGpIGLLAAQVAKLQGATVVVV-----GTEKDEVRLdvaKELGADAVNGGEEDLA-ELVNEITDGDGADVVIECSG 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1167803563 266 G----KSSTELLRqlaRGGTMVTYGGMAKQPVVASVSLLIFKDLKLRG 309
Cdd:cd08258   243 AvpalEQALELLR---KGGRIVQVGIFGPLAASIDVERIIQKELSVIG 287
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
43-286 7.37e-14

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: 72.02  E-value: 7.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  43 VRALVYGHHGDPA-----KVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYgflPE-LPAVGGNEGVAQVVAVG 116
Cdd:cd08281     1 MRAAVLRETGAPTpyadsRPLVIEEVELDPPGPGEVLVKIAAAGLCHSDLSVINGDR---PRpLPMALGHEAAGVVVEVG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 117 SNVTGLKPGDWVI-------------------------PANA----------------------GLGTWRTEAVFSEEAL 149
Cdd:cd08281    78 EGVTDLEVGDHVVlvfvpscghcrpcaegrpalcepgaAANGagtllsggrrlrlrggeinhhlGVSAFAEYAVVSRRSV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 150 IQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQnASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSdrlK 229
Cdd:cd08281   158 VKIDKDVPLEIAALFGCAVLTGVGAVVNTAGVRPGQSVAV-VGLGGVGLSALLGAVAAGASQVVAVDLNEDKLALA---R 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 230 SLGAEHVITEEElrrPEMKNFFKDMPQ--PRLALNCVGGKSSTEL-LRQLARGGTMVTYG 286
Cdd:cd08281   234 ELGATATVNAGD---PNAVEQVRELTGggVDYAFEMAGSVPALETaYEITRRGGTTVTAG 290
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
103-341 9.65e-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: 71.24  E-value: 9.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 103 VGGneGVAQVVAvgSNVTGLKPGDWVIpanaGLGTWRTEAVFSEEALIQV-PSDIPLQSA-ATLGVNPCTAYRMLMDFEQ 180
Cdd:COG2130    72 RGG--AVGEVVE--SRHPDFAVGDLVL----GMLGWQDYAVSDGAGLRKVdPSLAPLSAYlGVLGMPGLTAYFGLLDIGK 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 181 LQPGDSVIQNASNSGVGQAVIQIAAALGLRTINV---------VRDRpdiqklsdrlksLGAEHVI---TEeelrrpemk 248
Cdd:COG2130   144 PKAGETVVVSAAAGAVGSVVGQIAKLKGCRVVGIaggaekcryLVEE------------LGFDAAIdykAG--------- 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 249 nffkDMPQpRLALNC----------VGGKSSTELLRQLARGGTMV------TYGGMAKQPVVASVSLLIFKDLKLRGFWL 312
Cdd:COG2130   203 ----DLAA-ALAAACpdgidvyfdnVGGEILDAVLPLLNTFARIAvcgaisQYNATEPPPGPRNLGQLLVKRLRMQGFIV 277
                         250       260
                  ....*....|....*....|....*....
gi 1167803563 313 SqwkkDHsPDQFKELILTLCDLIRRGQLT 341
Cdd:COG2130   278 F----DH-ADRFPEFLAELAGWVAEGKLK 301
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
51-237 1.02e-13

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: 71.68  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  51 HGDPAKVVELKNLELAAVRGSDVRVKMLAAPIN----------PSDINMIQGNYGfLPELPAVGGNEGVAQVVAVGSNVT 120
Cdd:cd08246    23 YGDPAQAIQLEDVPVPELGPGEVLVAVMAAGVNynnvwaalgePVSTFAARQRRG-RDEPYHIGGSDASGIVWAVGEGVK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 121 GLKPGDWVI----------PANAGLGT--------WRTE---AVFSEEALIQV------PSDIPLQSAATLGVNPCTAYR 173
Cdd:cd08246   102 NWKVGDEVVvhcsvwdgndPERAGGDPmfdpsqriWGYEtnyGSFAQFALVQAtqlmpkPKHLSWEEAAAYMLVGATAYR 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167803563 174 MLMDFE--QLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRpdiQKlSDRLKSLGAEHVI 237
Cdd:cd08246   182 MLFGWNpnTVKPGDNVLIWGASGGLGSMAIQLARAAGANPVAVVSSE---EK-AEYCRALGAEGVI 243
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
54-359 1.86e-13

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: 70.75  E-value: 1.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  54 PAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPeLPAVGGNEGVAQVVAVGSNVT------GLKPGDW 127
Cdd:cd08231     9 PGKPLEIREVPLPDLEPGAVLVRVRLAGVCGSDVHTVAGRRPRVP-LPIILGHEGVGRVVALGGGVTtdvagePLKVGDR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 128 VI-----------------PA----------NAGLGTWRTEAVFSEEALIQ-------VPSDIPLQSAATLGVNPCTAYR 173
Cdd:cd08231    88 VTwsvgapcgrcyrclvgdPTkcenrkkyghEASCDDPHLSGGYAEHIYLPpgtaivrVPDNVPDEVAAPANCALATVLA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 174 MLMDFEQLQPGDSV-IQNAsnSGVGQAVIQIAAALGLRTInVVRDRPDiqklsDRLK---SLGAEHVITEEELRRPEMKN 249
Cdd:cd08231   168 ALDRAGPVGAGDTVvVQGA--GPLGLYAVAAAKLAGARRV-IVIDGSP-----ERLElarEFGADATIDIDELPDPQRRA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 250 FFKDMPQPR---LALNCVGGKSS-TELLRQLARGGTMVTYGGMAKQPVVA-SVSLLIFKDLKLRGFWLSqwkkdhSPDQF 324
Cdd:cd08231   240 IVRDITGGRgadVVIEASGHPAAvPEGLELLRRGGTYVLVGSVAPAGTVPlDPERIVRKNLTIIGVHNY------DPSHL 313
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1167803563 325 KELILTLCDLIRR----GQLTAPacsqVPLQDYQSALEA 359
Cdd:cd08231   314 YRAVRFLERTQDRfpfaELVTHR----YPLEDINEALEL 348
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
100-240 3.47e-13

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


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 69.22  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 100 LPAVGGNEGVAQVVAVGSNVTGLKPGDWVipanAGLGTWRTEAVFSEEALIQVPSDIPLQSAAtLGVNPCTAYRMLMDFE 179
Cdd:cd08255    20 LPLPPGYSSVGRVVEVGSGVTGFKPGDRV----FCFGPHAERVVVPANLLVPLPDGLPPERAA-LTALAATALNGVRDAE 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167803563 180 qLQPGDSVI---QNAsnsgVGQAVIQIAAALGLRTInVVRDRpdiqkLSDRL---KSLGAEHVITEE 240
Cdd:cd08255    95 -PRLGERVAvvgLGL----VGLLAAQLAKAAGAREV-VGVDP-----DAARRelaEALGPADPVAAD 150
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
43-358 4.06e-13

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: 69.60  E-value: 4.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  43 VRALVYGHHGDPAKVVELKnLELAAVRGSD-VRVKMLAAPINPSDInMIQGNYGFLPELPAVG-GNE--GVaqVVAVGSN 118
Cdd:cd08247     1 YKALTFKNNTSPLTITTIK-LPLPNCYKDNeIVVKVHAAALNPVDL-KLYNSYTFHFKVKEKGlGRDysGV--IVKVGSN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 119 V-TGLKPGDWV----IPANAGLGTWRTEAVF----SEEALIQVPSDIPLQSAA----TLGvnpcTAYRMLMDFEQ-LQPG 184
Cdd:cd08247    77 VaSEWKVGDEVcgiyPHPYGGQGTLSQYLLVdpkkDKKSITRKPENISLEEAAawplVLG----TAYQILEDLGQkLGPD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 185 DSVIQNASNSGVGQAVIQIaAALGLRTINVV---RDRPdiqklSDRLKSLGAEHVI-----TEEELRRPEMKNfFKDMPQ 256
Cdd:cd08247   153 SKVLVLGGSTSVGRFAIQL-AKNHYNIGTVVgtcSSRS-----AELNKKLGADHFIdydahSGVKLLKPVLEN-VKGQGK 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 257 PRLALNCVGG----KSSTELLRQLARGGTMVT----YGGMAKQPVVASVSLLIFKDLKLRG---FWLSQWKKDHsPDQFK 325
Cdd:cd08247   226 FDLILDCVGGydlfPHINSILKPKSKNGHYVTivgdYKANYKKDTFNSWDNPSANARKLFGslgLWSYNYQFFL-LDPNA 304
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1167803563 326 ELILTLCDLIRRGQLTAPACSQVPLQDYQSALE 358
Cdd:cd08247   305 DWIEKCAELIADGKVKPPIDSVYPFEDYKEAFE 337
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
44-248 4.82e-13

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


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 69.48  E-value: 4.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHG---DPAKVVELkNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPElPAVGGNEGVAQVVAVGSNVT 120
Cdd:cd08252     2 KAIGFTQPLpitDPDSLIDI-ELPKPVPGGRDLLVRVEAVSVNPVDTKVRAGGAPVPGQ-PKILGWDASGVVEAVGSEVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 121 GLKPGDWVIPA--------NAGLgtwrtEAVfsEEALI-QVPSDIPLQSAATLGVNPCTAYRMLmdFEQLQpGDSVIQNA 191
Cdd:cd08252    80 LFKVGDEVYYAgditrpgsNAEY-----QLV--DERIVgHKPKSLSFAEAAALPLTSLTAWEAL--FDRLG-ISEDAENE 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167803563 192 SNS--------GVGQAVIQIAAALGLRTINVVRDRPDIQklsDRLKSLGAEHVITEEELRRPEMK 248
Cdd:cd08252   150 GKTlliiggagGVGSIAIQLAKQLTGLTVIATASRPESI---AWVKELGADHVINHHQDLAEQLE 211
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
44-358 1.19e-12

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 68.02  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDpakvVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPelPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08236     2 KALVLTGPGD----LRYEDIPKPEPGPGEVLVKVKACGICGSDIPRYLGTGAYHP--PLVLGHEFSGTVEEVGSGVDDLA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWV-----IPANA------G----------LGTWRTEAvFSE------EALIQVPSDIPLQSAATlgVNPCT----AY 172
Cdd:cd08236    76 VGDRVavnplLPCGKceyckkGeyslcsnydyIGSRRDGA-FAEyvsvpaRNLIKIPDHVDYEEAAM--IEPAAvalhAV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 173 RMLMdfeqLQPGDSVIqnASNSG-VGQAVIQIAAALGLRTINVVrDrPDIQKLsDRLKSLGAEHVIteeelrRPEMKNFF 251
Cdd:cd08236   153 RLAG----ITLGDTVV--VIGAGtIGLLAIQWLKILGAKRVIAV-D-IDDEKL-AVARELGADDTI------NPKEEDVE 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 252 KDMPQ-----PRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVV---ASVSLLIFKDLKLRGFWLSQWKKDhSPDQ 323
Cdd:cd08236   218 KVRELtegrgADLVIEAAGSPATIEQALALARPGGKVVLVGIPYGDVTlseEAFEKILRKELTIQGSWNSYSAPF-PGDE 296
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1167803563 324 FKELIltlcDLIRRGQLTA-PACS-QVPLQDYQSALE 358
Cdd:cd08236   297 WRTAL----DLLASGKIKVePLIThRLPLEDGPAAFE 329
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
58-241 1.69e-12

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: 67.38  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  58 VELKNLELAAVRGSDVRVKMLAAPINPSDINMI-QGNYGFL-PELPAVGGNEGVAQVVAVGSNVTGLKPGDWVipANAGL 135
Cdd:cd08269     7 FEVEEHPRPTPGPGQVLVRVEGCGVCGSDLPAFnQGRPWFVyPAEPGGPGHEGWGRVVALGPGVRGLAVGDRV--AGLSG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 136 GTWRTEAVFSEEALIQVPSD-----IPLQSAATlGVNpctayrmLMDFEQLQPGDSVIQNASNSgVGQAVIQIAAALGLR 210
Cdd:cd08269    85 GAFAEYDLADADHAVPLPSLldgqaFPGEPLGC-ALN-------VFRRGWIRAGKTVAVIGAGF-IGLLFLQLAAAAGAR 155
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1167803563 211 TINVVRDRPDIQKLSdrlKSLGAEHVITEEE 241
Cdd:cd08269   156 RVIAIDRRPARLALA---RELGATEVVTDDS 183
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
107-340 2.82e-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: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 107 EGVAQVVAvgSNVTGLKPGDWVIpANAGlgtWRTEAVFSEEA---LIQVPSDIPLQ---SAA--TLGVNPCTAYRMLMDF 178
Cdd:cd08294    65 TQVAKVIE--SKNSKFPVGTIVV-ASFG---WRTHTVSDGKDqpdLYKLPADLPDDlppSLAlgVLGMPGLTAYFGLLEI 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 179 EQLQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRdrpdiqklSD----RLKSLGAEHVIT------EEELRR--PE 246
Cdd:cd08294   139 CKPKAGETVVVNGAAGAVGSLVGQIAKIKGCKVIGCAG--------SDdkvaWLKELGFDAVFNyktvslEEALKEaaPD 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 247 MKNFFKDmpqprlalNcVGGKSSTELLRQLARGGTMV------TYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWkKDHS 320
Cdd:cd08294   211 GIDCYFD--------N-VGGEFSSTVLSHMNDFGRVAvcgsisTYNDKEPKKGPYVQETIIFKQLKMEGFIVYRW-QDRW 280
                         250       260
                  ....*....|....*....|
gi 1167803563 321 PDQFKELIltlcDLIRRGQL 340
Cdd:cd08294   281 PEALKQLL----KWIKEGKL 296
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
44-363 4.03e-12

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: 66.40  E-value: 4.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYghhgDPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGflPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08234     2 KALVY----EGPGELEVEEVPVPEPGPDEVLIKVAACGICGTDLHIYEGEFG--AAPPLVPGHEFAGVVVAVGSKVTGFK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWV-----IPAN----------------AGLGTWRT----E-AVFSEEALIQVPSDIPLQSAATL--------GVNPC 169
Cdd:cd08234    76 VGDRVavdpnIYCGecfycrrgrpnlcenlTAVGVTRNggfaEyVVVPAKQVYKIPDNLSFEEAALAeplscavhGLDLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 170 tayrmlmdfeQLQPGDSV-IQNAsnsGV-GQAVIQIAAALGLRTINVVrDRPDIqKLsDRLKSLGAEHVITEEELRRPEM 247
Cdd:cd08234   156 ----------GIKPGDSVlVFGA---GPiGLLLAQLLKLNGASRVTVA-EPNEE-KL-ELAKKLGATETVDPSREDPEAQ 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 248 KNffkdmPQPR---LALNCVGGKSSTEL-LRQLARGGTMVTYG-GMAKQPVVASVSLLIFKDLKLRGFWLsqwkkdhSPD 322
Cdd:cd08234   220 KE-----DNPYgfdVVIEATGVPKTLEQaIEYARRGGTVLVFGvYAPDARVSISPFEIFQKELTIIGSFI-------NPY 287
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1167803563 323 QFKELIltlcDLIRRGQL-TAPACS-QVPLQDYQSALEASMKP 363
Cdd:cd08234   288 TFPRAI----ALLESGKIdVKGLVShRLPLEEVPEALEGMRSG 326
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
72-129 1.17e-11

Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure.


Pssm-ID: 400513 [Multi-domain]  Cd Length: 106  Bit Score: 60.70  E-value: 1.17e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1167803563  72 DVRVKMLAAPINPSDINMIQGNYgFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI 129
Cdd:pfam08240   2 EVLVKVKAAGICGSDLHIYKGGN-PPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVV 58
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
51-328 3.41e-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: 63.86  E-value: 3.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  51 HGDPAKV-VELKNLELAAVRGSDVRVKMLAAPINPsdinmiqgnYGFLPELPAVGGNEGVAQVVA--VGSNVTGLKPGDW 127
Cdd:TIGR02825  11 VGYPTDSdFELKTVELPPLNNGEVLLEALFLSVDP---------YMRVAAKRLKEGDTMMGQQVArvVESKNVALPKGTI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 128 VIpanAGLGtWRTEAVFS----EEALIQVPSDIPLQSA-ATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQ 202
Cdd:TIGR02825  82 VL---ASPG-WTSHSISDgkdlEKLLTEWPDTLPLSLAlGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 203 IAAALGLRTINVVRDRPDIqklsDRLKSLGAEHVIT-------EEELRR--PEMKNFFKDMpqprlalncVGGKSSTELL 273
Cdd:TIGR02825 158 IAKLKGCKVVGAAGSDEKV----AYLKKLGFDVAFNyktvkslEETLKKasPDGYDCYFDN---------VGGEFSNTVI 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167803563 274 RQL------ARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRGFWLSQWKKDHSPDQFKELI 328
Cdd:TIGR02825 225 GQMkkfgriAICGAISTYNRTGPLPPGPPPEIVIYQELRMEGFIVNRWQGEVRQKALKELL 285
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
44-309 3.44e-11

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


Pssm-ID: 176249 [Multi-domain]  Cd Length: 326  Bit Score: 63.50  E-value: 3.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAKVvELKNLELAAVRGSDVRVKMLAAPINPSD------INMIQGNYGFLPELPAVGgnegvaqvVAVGS 117
Cdd:cd08289     2 QALVVEKDEDDVSV-SVKNLTLDDLPEGDVLIRVAYSSVNYKDglasipGGKIVKRYPFIPGIDLAG--------TVVES 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 118 NVTGLKPGDWVIPANAGLGTWRtEAVFSEEA------LIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQ--LQP-GDSVI 188
Cdd:cd08289    73 NDPRFKPGDEVIVTSYDLGVSH-HGGYSEYArvpaewVVPLPKGLTLKEAMILGTAGFTAALSIHRLEEngLTPeQGPVL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 189 QNASNSGVGQAVIQIAAALGLRTINVVRDRPDiqklSDRLKSLGAEHVITEEELRRPEMKNFFKDMPQPrlALNCVGGKS 268
Cdd:cd08289   152 VTGATGGVGSLAVSILAKLGYEVVASTGKADA----ADYLKKLGAKEVIPREELQEESIKPLEKQRWAG--AVDPVGGKT 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1167803563 269 STELLRQLARGGTMVTYGGMAKQPVVASVSLLIFKDLKLRG 309
Cdd:cd08289   226 LAYLLSTLQYGGSVAVSGLTGGGEVETTVFPFILRGVNLLG 266
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
72-234 6.42e-11

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; Glutathione-dependent formaldehyde dehydrogenases (FDHs) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. These tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176244 [Multi-domain]  Cd Length: 344  Bit Score: 63.04  E-value: 6.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  72 DVRVKMLAAPINPSDINMIQGNYGFLPelPAVGGNEGVAQVVAVGSNVTGLKPGDWVI-PANAGLG---------TWR-- 139
Cdd:cd08284    27 DAIVKVTAAAICGSDLHIYRGHIPSTP--GFVLGHEFVGEVVEVGPEVRTLKVGDRVVsPFTIACGecfycrrgqSGRca 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 140 -----------------TEAV---FSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFeQLQPGDSVIQNASNSgVGQA 199
Cdd:cd08284   105 kgglfgyagspnldgaqAEYVrvpFADGTLLKLPDGLSDEAALLLGDILPTGYFGAKRA-QVRPGDTVAVIGCGP-VGLC 182
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1167803563 200 VIQIAAALGLRTINVVrDRpdiqkLSDRL---KSLGAE 234
Cdd:cd08284   183 AVLSAQVLGAARVFAV-DP-----VPERLeraAALGAE 214
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
54-130 2.78e-10

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


Pssm-ID: 176259 [Multi-domain]  Cd Length: 373  Bit Score: 61.18  E-value: 2.78e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167803563  54 PAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNygFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP 130
Cdd:cd08299    16 PKKPFSIEEIEVAPPKAHEVRIKIVATGICRSDDHVVSGK--LVTPFPVILGHEAAGIVESVGEGVTTVKPGDKVIP 90
MDR_yhdh cd08288
Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR ...
44-289 5.79e-10

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: 59.86  E-value: 5.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYgHHGDPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNvtGLK 123
Cdd:cd08288     2 KALVL-EKDDGGTSAELRELDESDLPEGDVTVEVHYSTLNYKDGLAITGKGGIVRTFPLVPGIDLAGTVVESSSP--RFK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIPANAGLGTWR-----TEAVFSEEALIQVPSDIPLQSAATLGVNPCTAyrML--MDFEQ--LQPGDS-VIQNASN 193
Cdd:cd08288    79 PGDRVVLTGWGVGERHwggyaQRARVKADWLVPLPEGLSARQAMAIGTAGFTA--MLcvMALEDhgVTPGDGpVLVTGAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 194 SGVGQAVIQIAAALGLRTInVVRDRPDiqkLSDRLKSLGAEHVITEEELRRPEmknffKDMPQPRLA--LNCVGGKSSTE 271
Cdd:cd08288   157 GGVGSVAVALLARLGYEVV-ASTGRPE---EADYLRSLGASEIIDRAELSEPG-----RPLQKERWAgaVDTVGGHTLAN 227
                         250
                  ....*....|....*...
gi 1167803563 272 LLRQLARGGTmVTYGGMA 289
Cdd:cd08288   228 VLAQTRYGGA-VAACGLA 244
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
43-237 1.80e-09

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


Pssm-ID: 176246 [Multi-domain]  Cd Length: 345  Bit Score: 58.42  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  43 VRALVYghHGDpaKVVELKNLELAAVR-GSDVRVKMLAAPINPSDINMIQGNygfLPELPA--VGGNEGVAQVVAVGSNV 119
Cdd:cd08286     1 MKALVY--HGP--GKISWEDRPKPTIQePTDAIVKMLKTTICGTDLHILKGD---VPTVTPgrILGHEGVGVVEEVGSAV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 120 TGLKPGDWVIPA-----------NAGL------GTWR-------TEAVF-----SEEALIQVPSDIPLQSAATLG-VNPc 169
Cdd:cd08286    74 TNFKVGDRVLIScisscgtcgycRKGLyshcesGGWIlgnlidgTQAEYvriphADNSLYKLPEGVDEEAAVMLSdILP- 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167803563 170 TAYRMLMDFEQLQPGDSV-IQNAsnsG-VGQAVIQIAAALGLRTINVVrDRPDiqklsDRL---KSLGAEHVI 237
Cdd:cd08286   153 TGYECGVLNGKVKPGDTVaIVGA---GpVGLAALLTAQLYSPSKIIMV-DLDD-----NRLevaKKLGATHTV 216
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
44-342 6.08e-09

(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin. BDH functions as a homodimer. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit.


Pssm-ID: 176195 [Multi-domain]  Cd Length: 351  Bit Score: 56.78  E-value: 6.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYghHGdpAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLP----------ELPAVGGNEGVAQVV 113
Cdd:cd08233     2 KAARY--HG--RKDIRVEEVPEPPVKPGEVKIKVAWCGICGSDLHEYLDGPIFIPteghphltgeTAPVTLGHEFSGVVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 114 AVGSNVTGLKPGDWVI--PA--------------NA-------GLGTW----RTEAVFSEEALIQVPSDIPLQSAATlgV 166
Cdd:cd08233    78 EVGSGVTGFKVGDRVVvePTikcgtcgackrglyNLcdslgfiGLGGGgggfAEYVVVPAYHVHKLPDNVPLEEAAL--V 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 167 NPCT----AYRMlmdfEQLQPGDSV-IQNAsnsG-VGQAVIQIAAALGLRTINVVRDRPDIQKLSdrlKSLGAEHVI--- 237
Cdd:cd08233   156 EPLAvawhAVRR----SGFKPGDTAlVLGA---GpIGLLTILALKAAGASKIIVSEPSEARRELA---EELGATIVLdpt 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 238 ---TEEELRRPEMKNFFKdmpqprLALNCVGGKSSTEL-LRQLARGGTMVTYGGMAKqPVVASVSLLIFKDLKLRGFWLs 313
Cdd:cd08233   226 evdVVAEVRKLTGGGGVD------VSFDCAGVQATLDTaIDALRPRGTAVNVAIWEK-PISFNPNDLVLKEKTLTGSIC- 297
                         330       340
                  ....*....|....*....|....*....
gi 1167803563 314 qwkkdHSPDQFKELIltlcDLIRRGQLTA 342
Cdd:cd08233   298 -----YTREDFEEVI----DLLASGKIDA 317
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
44-365 9.83e-09

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: 56.06  E-value: 9.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYghHGdpAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYgFLPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08235     2 KAAVL--HG--PNDVRLEEVPVPEPGPGEVLVKVRACGICGTDVKKIRGGH-TDLKPPRILGHEIAGEIVEVGDGVTGFK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 124 PGDWVIPA-NAGLGTWR-----TEAVFSEEALIQVPSD--------IPLQSAATLGVNPCTAYrmlMDFEQL---QPGDS 186
Cdd:cd08235    77 VGDRVFVApHVPCGECHyclrgNENMCPNYKKFGNLYDggfaeyvrVPAWAVKRGGVLKLPDN---VSFEEAalvEPLAC 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 187 VIQNASNSGV--GQAV------------IQIAAALGLRTI---NVVRDRPDIqklsdrLKSLGAEHVI-TEEELRRPEMK 248
Cdd:cd08235   154 CINAQRKAGIkpGDTVlvigagpigllhAMLAKASGARKVivsDLNEFRLEF------AKKLGADYTIdAAEEDLVEKVR 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 249 NFFK----DmpqprLALNCVGGKSSTEL-LRQLARGGTMVTYGGMAK-QPVVASVSLLIFKDLKLRGFWLSqwkkdhSPD 322
Cdd:cd08235   228 ELTDgrgaD-----VVIVATGSPEAQAQaLELVRKGGRILFFGGLPKgSTVNIDPNLIHYREITITGSYAA------SPE 296
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1167803563 323 QFKELIltlcDLIRRGQLTAPA--CSQVPLQDYQSALE-----ASMKPFI 365
Cdd:cd08235   297 DYKEAL----ELIASGKIDVKDliTHRFPLEDIEEAFElaadgKSLKIVI 342
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
44-358 4.10e-08

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: 54.20  E-value: 4.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDpakvVELKNLELAAVRGS-DVRVKMLAAPINPSDINMIQGNyGFLPELPAVGGNEGVAQVVAVGSNVTGL 122
Cdd:cd05278     2 KALVYLGPGK----IGLEEVPDPKIQGPhDAIVRVTATSICGSDLHIYRGG-VPGAKHGMILGHEFVGEVVEVGSDVKRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 123 KPGDWV-IPANA------------------GLGTW----RTEAVFSE--------EALIQVPSDIPLQSAATLGVNPCTA 171
Cdd:cd05278    77 KPGDRVsVPCITfcgrcrfcrrgyhahcenGLWGWklgnRIDGGQAEyvrvpyadMNLAKIPDGLPDEDALMLSDILPTG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 172 Y---RMlmdfEQLQPGDSVIqnASNSG-VGQAVIQIAAALGLRTINVVRDRPDIQKLsdrLKSLGAEHVITeeeLRRPEM 247
Cdd:cd05278   157 FhgaEL----AGIKPGSTVA--VIGAGpVGLCAVAGARLLGAARIIAVDSNPERLDL---AKEAGATDIIN---PKNGDI 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 248 KNFFKDMPQPRLA---LNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVvasvsllifkDLKLRGFWlsqWKKDHS---- 320
Cdd:cd05278   225 VEQILELTGGRGVdcvIEAVGFEETFEQAVKVVRPGGTIANVGVYGKPD----------PLPLLGEW---FGKNLTfktg 291
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1167803563 321 ----PDQFKELIltlcDLIRRGQL-TAPACSQV-PLQDYQSALE 358
Cdd:cd05278   292 lvpvRARMPELL----DLIEEGKIdPSKLITHRfPLDDILKAYR 331
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
44-137 1.81e-07

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


Pssm-ID: 176242 [Multi-domain]  Cd Length: 375  Bit Score: 52.59  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYGHHGDPAkVVELKNLELaaVRGSDVRVKMLAAPINPSDINMIQGNYGflPELPAVGGNEGVAQVVAVGSNVTGLK 123
Cdd:cd08282     2 KAVVYGGPGNVA-VEDVPDPKI--EHPTDAIVRITTTAICGSDLHMYRGRTG--AEPGLVLGHEAMGEVEEVGSAVESLK 76
                          90
                  ....*....|....*
gi 1167803563 124 PGDWV-IPANAGLGT 137
Cdd:cd08282    77 VGDRVvVPFNVACGR 91
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
72-362 2.66e-07

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


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 51.85  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  72 DVRVKMLAAPINPSDINMIQ-GNYG-FLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVI--PA---------NAGL--- 135
Cdd:cd08232    23 EVRVRVAAGGICGSDLHYYQhGGFGtVRLREPMVLGHEVSGVVEAVGPGVTGLAPGQRVAvnPSrpcgtcdycRAGRpnl 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 136 -----------------GTWRTEAVFSEEALIQVPSDIPLQSAA---TLGVnpCT-AYRMLMDFEqlqpGDSVIqnASNS 194
Cdd:cd08232   103 clnmrflgsamrfphvqGGFREYLVVDASQCVPLPDGLSLRRAAlaePLAV--ALhAVNRAGDLA----GKRVL--VTGA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 195 G-VGQAVIQIAAALGLRTINVVrdrpDIQKLS-DRLKSLGAEHVIteeELRRPEMKNFFKDMPQPRLALNCVGGKSSTE- 271
Cdd:cd08232   175 GpIGALVVAAARRAGAAEIVAT----DLADAPlAVARAMGADETV---NLARDPLAAYAADKGDFDVVFEASGAPAALAs 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 272 LLRQLARGGTMVTYgGMAKQPVVASVSLLIFKDLKLRGfwlSQwkkdhspdQFKELILTLCDLIRRGQL-TAPACSQV-P 349
Cdd:cd08232   248 ALRVVRPGGTVVQV-GMLGGPVPLPLNALVAKELDLRG---SF--------RFDDEFAEAVRLLAAGRIdVRPLITAVfP 315
                         330
                  ....*....|....*....
gi 1167803563 350 LQDYQSALE------ASMK 362
Cdd:cd08232   316 LEEAAEAFAlaadrtRSVK 334
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
53-130 3.16e-07

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: 51.85  E-value: 3.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  53 DPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYgflPE--LPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP 130
Cdd:cd08300    10 EAGKPLSIEEVEVAPPKAGEVRIKILATGVCHTDAYTLSGAD---PEglFPVILGHEGAGIVESVGEGVTSVKPGDHVIP 86
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
72-142 3.73e-07

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


Pssm-ID: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 51.47  E-value: 3.73e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167803563  72 DVRVKMLAAPINPSDINMIQGNYGFLPElPAVGGNEGVAQVVAVGSNVTGLKPGDWVIpANAGLGTWRTEA 142
Cdd:cd08285    26 DAIVRPTAVAPCTSDVHTVWGGAPGERH-GMILGHEAVGVVEEVGSEVKDFKPGDRVI-VPAITPDWRSVA 94
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
43-311 4.25e-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: 51.17  E-value: 4.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  43 VRALVYghHGDpaKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGL 122
Cdd:cd08239     1 MRGAVF--PGD--RTVELREFPVPVPGPGEVLLRVKASGLCGSDLHYYYHGHRAPAYQGVIPGHEPAGVVVAVGPGVTHF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 123 KPGDWVIPAN-AGLGTWRT-----------------------EAVF---SEEALIQVPSDIPLQSAATLGVNPCTAYRML 175
Cdd:cd08239    77 RVGDRVMVYHyVGCGACRNcrrgwmqlctskraaygwnrdggHAEYmlvPEKTLIPLPDDLSFADGALLLCGIGTAYHAL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 176 mDFEQLQPGDSVIqnASNSG-VGQAVIQIAAALGLRTINVVRDRPDIQKLSdrlKSLGAEHVITEEELRRPEMKNFFKDM 254
Cdd:cd08239   157 -RRVGVSGRDTVL--VVGAGpVGLGALMLARALGAEDVIGVDPSPERLELA---KALGADFVINSGQDDVQEIRELTSGA 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1167803563 255 PQpRLALNCVGGKSSTEL-LRQLARGGTMVtYGGMAKQPVVASVSLLIFKDLKLRGFW 311
Cdd:cd08239   231 GA-DVAIECSGNTAARRLaLEAVRPWGRLV-LVGEGGELTIEVSNDLIRKQRTLIGSW 286
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
167-241 2.98e-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: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 167 NPC------TAYRMLMDFEQ---LQPGDSVIQNAS-NSGVGQAVIqiAAALGLRTINVVRDRPDIQKLsDRLKSLGAEHV 236
Cdd:cd01561    27 NPGgsvkdrIALYMIEDAEKrglLKPGTTIIEPTSgNTGIGLAMV--AAAKGYRFIIVMPETMSEEKR-KLLRALGAEVI 103

                  ....*
gi 1167803563 237 ITEEE 241
Cdd:cd01561   104 LTPEA 108
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
58-309 5.06e-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: 47.87  E-value: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  58 VELKNLELAAVRGSDVRVKMLAAPINPSDINMIQ--GNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV-----IP 130
Cdd:cd05285    10 LRLEERPIPEPGPGEVLVRVRAVGICGSDVHYYKhgRIGDFVVKEPMVLGHESAGTVVAVGSGVTHLKVGDRVaiepgVP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 131 AN------AGL----------------GTWRTEAVFSEEALIQVPSDIPLQSAA---TLGVNPCTAYRMlmdfeQLQPGD 185
Cdd:cd05285    90 CRtcefckSGRynlcpdmrfaatppvdGTLCRYVNHPADFCHKLPDNVSLEEGAlvePLSVGVHACRRA-----GVRPGD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 186 SV-IQNAsnsG-VGQAVIQIAAALGLRTINVVrdrpDIQKlsDRL---KSLGAEHVI----TEEELRRPEMKNFFKDMpQ 256
Cdd:cd05285   165 TVlVFGA---GpIGLLTAAVAKAFGATKVVVT----DIDP--SRLefaKELGATHTVnvrtEDTPESAEKIAELLGGK-G 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1167803563 257 PRLALNCVGGKSSTEL-LRQLARGGTMVTyGGMAKQPVVASVSLLIFKDLKLRG 309
Cdd:cd05285   235 PDVVIECTGAESCIQTaIYATRPGGTVVL-VGMGKPEVTLPLSAASLREIDIRG 287
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
72-234 5.11e-06

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 47.95  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  72 DVRVKMLAAPINPSDINMIQGNYGFlPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV----------------------- 128
Cdd:PLN02586   39 DVTVKILYCGVCHSDLHTIKNEWGF-TRYPIVPGHEIVGIVTKLGKNVKKFKEGDRVgvgvivgsckscescdqdlenyc 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 129 ----IPANA-------GLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSvIQNASNSGVG 197
Cdd:PLN02586  118 pkmiFTYNSighdgtkNYGGYSDMIVVDQHFVLRFPDNLPLDAGAPLLCAGITVYSPMKYYGMTEPGKH-LGVAGLGGLG 196
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1167803563 198 QAVIQIAAALGLRtINVVRDRPdiQKLSDRLKSLGAE 234
Cdd:PLN02586  197 HVAVKIGKAFGLK-VTVISSSS--NKEDEAINRLGAD 230
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
44-309 6.68e-06

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: 47.55  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  44 RALVYghHGDPAKVV-ELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVA-------V 115
Cdd:TIGR02823   1 KALVV--EKEDGKVSaQVETLDLSDLPEGDVLIKVAYSSLNYKDALAITGKGGVVRSYPMIPGIDAAGTVVSsedprfrE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 116 GSNV--TGLK---------------PGDWVIPanaglgtwrteavfseealiqVPSDIPLQSAATLGVNPCTAYRMLMDF 178
Cdd:TIGR02823  79 GDEVivTGYGlgvshdggysqyarvPADWLVP---------------------LPEGLSLREAMALGTAGFTAALSVMAL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 179 EQ--LQPGD-SVIQNASNSGVGQAVIQIAAALGLRTInVVRDRPDiqkLSDRLKSLGAEHVITEEELR---RPEMKNFFK 252
Cdd:TIGR02823 138 ERngLTPEDgPVLVTGATGGVGSLAVAILSKLGYEVV-ASTGKAE---EEDYLKELGASEVIDREDLSppgKPLEKERWA 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1167803563 253 DmpqprlALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLLIfkdlkLRG 309
Cdd:TIGR02823 214 G------AVDTVGGHTLANVLAQLKYGGAVAACGLAGGPDLPTTVLPFI-----LRG 259
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
231-361 1.52e-05

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 44.24  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 231 LGAEHVI--TEEELRRPEMKNFFKdmpqprLALNCVGGKSSTELLRQLARGGTMVTYGGmakqPVVASVSLLIFKDLKLR 308
Cdd:pfam13602   1 LGADEVIdyRTTDFVQATGGEGVD------VVLDTVGGEAFEASLRVLPGGGRLVTIGG----PPLSAGLLLPARKRGGR 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1167803563 309 GFWLSQWKkdHSPDQFKELILTLCDLIRRGQLTaPACSQV-PLQDYQSALEASM 361
Cdd:pfam13602  71 GVKYLFLF--VRPNLGADILQELADLIEEGKLR-PVIDRVfPLEEAAEAHRYLE 121
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
54-132 1.62e-05

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


Pssm-ID: 176192 [Multi-domain]  Cd Length: 355  Bit Score: 46.44  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  54 PAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGFLPE----LpaVGGNEGVAQVVAVGSNvTGLKPGDWVI 129
Cdd:cd08230     9 GKPGVRVVDIPEPEPTPGEVLVRTLEVGVCGTDREIVAGEYGTAPPgedfL--VLGHEALGVVEEVGDG-SGLSPGDLVV 85

                  ...
gi 1167803563 130 PAN 132
Cdd:cd08230    86 PTV 88
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
59-128 2.16e-05

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


Pssm-ID: 176258 [Multi-domain]  Cd Length: 329  Bit Score: 46.02  E-value: 2.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  59 ELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGfLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV 128
Cdd:cd08298    18 RLTEVPVPEPGPGEVLIKVEACGVCRTDLHIVEGDLP-PPKLPLIPGHEIVGRVEAVGPGVTRFSVGDRV 86
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
72-130 2.64e-05

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


Pssm-ID: 176261 [Multi-domain]  Cd Length: 369  Bit Score: 45.75  E-value: 2.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1167803563  72 DVRVKMLAAPINPSDINMIQGNyGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP 130
Cdd:cd08301    29 EVRIKILHTSLCHTDVYFWEAK-GQTPLFPRILGHEAAGIVESVGEGVTDLKPGDHVLP 86
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
108-315 3.39e-05

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 45.22  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 108 GVAQVVAvgSNVTGLKPGDWVipanAGLGTWRTEAVF--SEEAL--IQVPSDIPLQ-SAATLGVNPCTAYRMLMDFEQLQ 182
Cdd:PLN03154   84 GVSKVVD--SDDPNFKPGDLI----SGITGWEEYSLIrsSDNQLrkIQLQDDIPLSyHLGLLGMAGFTAYAGFYEVCSPK 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 183 PGDSVIQNASNSGVGQAVIQIAAalgLRTINVVRDRPDIQKLsDRLKS-LGAEHVITEEE-------LRR--PEMKNFFK 252
Cdd:PLN03154  158 KGDSVFVSAASGAVGQLVGQLAK---LHGCYVVGSAGSSQKV-DLLKNkLGFDEAFNYKEepdldaaLKRyfPEGIDIYF 233
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167803563 253 DMpqprlalncVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSL-----LIFKDLKLRGFWLSQW 315
Cdd:PLN03154  234 DN---------VGGDMLDAALLNMKIHGRIAVCGMVSLNSLSASQGIhnlynLISKRIRMQGFLQSDY 292
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
71-228 1.48e-04

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 43.47  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  71 SDVRVKMLAAPINPSDINMIQGNYGFlPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV------------IPANAGLGTW 138
Cdd:PLN02178   32 NDVTVKILFCGVCHSDLHTIKNHWGF-SRYPIIPGHEIVGIATKVGKNVTKFKEGDRVgvgviigscqscESCNQDLENY 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 139 RTEAVFSEEA----------------------LIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGV 196
Cdd:PLN02178  111 CPKVVFTYNSrssdgtrnqggysdvivvdhrfVLSIPDGLPSDSGAPLLCAGITVYSPMKYYGMTKESGKRLGVNGLGGL 190
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1167803563 197 GQAVIQIAAALGLRTINVVRDRPDIQKLSDRL 228
Cdd:PLN02178  191 GHIAVKIGKAFGLRVTVISRSSEKEREAIDRL 222
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
72-245 2.45e-04

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176243 [Multi-domain]  Cd Length: 386  Bit Score: 42.91  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  72 DVRVKMLAAPINPSDINMIQGnygFLPELPA--VGGNEGVAQVVAVGSNVTGLKPGDWV-IPANAGLGT----------- 137
Cdd:cd08283    27 DAIVRVTATAICGSDLHLYHG---YIPGMKKgdILGHEFMGVVEEVGPEVRNLKVGDRVvVPFTIACGEcfyckrglysq 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 138 ---------------WRTEAVF---------------------SEEALIQVPSDIPLQSAATLGVNPCTAYrMLMDFEQL 181
Cdd:cd08283   104 cdntnpsaemaklygHAGAGIFgyshltggyaggqaeyvrvpfADVGPFKIPDDLSDEKALFLSDILPTGY-HAAELAEV 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167803563 182 QPGDSV-IQNAsnSGVGQAVIQIAAALGLRTINVVrDRPDiqklsDRL----KSLGAEhVITEEELRRP 245
Cdd:cd08283   183 KPGDTVaVWGC--GPVGLFAARSAKLLGAERVIAI-DRVP-----ERLemarSHLGAE-TINFEEVDDV 242
PLN02740 PLN02740
Alcohol dehydrogenase-like
72-130 3.80e-04

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 42.09  E-value: 3.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1167803563  72 DVRVKMLAAPINPSDINMIQGNYGFLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWVIP 130
Cdd:PLN02740   37 EVRIKILYTSICHTDLSAWKGENEAQRAYPRILGHEAAGIVESVGEGVEDLKAGDHVIP 95
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
62-212 4.01e-04

Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This group includes proteins identified as the Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase. The Arabidopsis enzyme, a member of the medium chain dehydrogenase/reductase family, catalyzes the reduction of 7-8-double bond of phenylpropanal substrates as a plant defense mechanism. Prostaglandins and related eicosanoids (lipid mediators involved in host defense and inflamation) are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. Leukotriene B4 (LTB4) can be metabolized by LTB4 20-hydroxylase in inflamatory cells, and in other cells by bifunctional LTB4 12-HD/PGR. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176255 [Multi-domain]  Cd Length: 338  Bit Score: 41.92  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  62 NLELAAVRGS--DVRVKMLAAPINP------SDINMIQGNYGFLPELPAVGGneGVAQVVAvgSNVTGLKPGDWVipanA 133
Cdd:cd08295    27 KLTLKVPPGGsgDVLVKNLYLSCDPymrgrmKGHDDSLYLPPFKPGEVITGY--GVAKVVD--SGNPDFKVGDLV----W 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563 134 GLGTWRTEAVFS-EEALIQV-PSDIPLQS-AATLGVNPCTAYRMLMDFEQLQPGDSVIQNASNSGVGQAVIQIAAALGLR 210
Cdd:cd08295    99 GFTGWEEYSLIPrGQDLRKIdHTDVPLSYyLGLLGMPGLTAYAGFYEVCKPKKGETVFVSAASGAVGQLVGQLAKLKGCY 178

                  ..
gi 1167803563 211 TI 212
Cdd:cd08295   179 VV 180
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
171-241 5.51e-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: 5.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167803563 171 AYRMLMDFEQLQPGDSVIQnASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLsDRLKSLGAEHVITEEE 241
Cdd:pfam00291  42 ALNLLLRLKEGEGGKTVVE-ASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKL-LLMRALGAEVVLVGGD 110
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
53-128 1.02e-03

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 40.94  E-value: 1.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167803563  53 DPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGfLPELPAVGGNEGVAQVVAVGSNVTGLKPGDWV 128
Cdd:PLN02514   17 DPSGHLSPYTYTLRKTGPEDVVIKVIYCGICHTDLHQIKNDLG-MSNYPMVPGHEVVGEVVEVGSDVSKFTVGDIV 91
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
101-128 4.89e-03

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 38.65  E-value: 4.89e-03
                          10        20
                  ....*....|....*....|....*...
gi 1167803563 101 PAVGGNEGVAQVVAVGSNVTGLKPGDWV 128
Cdd:PRK05396   58 PMVVGHEFVGEVVEVGSEVTGFKVGDRV 85
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
53-128 5.84e-03

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


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 38.37  E-value: 5.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167803563  53 DPAKVVELKNLELAAVRGSDVRVKMLAAPINPSDINMIQGNY----GFLPelPAVGGNEGVAQVVAVGSNVTGLKPGDWV 128
Cdd:cd05281     8 KAGPGAELVEVPVPKPGPGEVLIKVLAASICGTDVHIYEWDEwaqsRIKP--PLIFGHEFAGEVVEVGEGVTRVKVGDYV 85
 
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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