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Conserved domains on  [gi|4545075|gb|AAD22381|]
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quinone oxidoreductase homolog-1 [Homo sapiens]

Protein Classification

quinone oxidoreductase-like protein 1( domain architecture ID 10142483)

quinone oxidoreductase-like protein 1 is a component of the FERRY complex (Five-subunit Endosomal Rab5 and RNA/ribosome intermediary) that directly interacts with mRNAs and RAB5A, and functions as a RAB5A effector involved in the localization and the distribution of specific mRNAs; belongs to the medium chain dehydrogenase/reductase (MDR) superfamily

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
31-347 2.32e-55

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: 182.77  E-value: 2.32e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   31 NFVKLQVKACALSQINTkLLAEMKMKKDLFPVGREIAGIVLDVGSKVSFFQPDDEVVGILPldsedPGLCEVVRVHEHYL 110
Cdd:cd05195   1 DEVEVEVKAAGLNFRDV-LVALGLLPGDETPLGLECSGIVTRVGSGVTGLKVGDRVMGLAP-----GAFATHVRVDARLV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  111 VHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSLEDKQCLERFRP 190
Cdd:cd05195  75 VKIPDSLSFEEAATLPVAYLTAYYALVDLARLQKGESVLIHAAAGGVGQAAIQLAQHLGAEVFATVGSEEKREFLRELGG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  191 PIARVIDVSNgkVHVAESCLEETGGLGVDIVLDAGVrlyskDDEPAVKLQLLPhkhDIITLLGVGGHWVTTEENLQLDPp 270
Cdd:cd05195 155 PVDHIFSSRD--LSFADGILRATGGRGVDVVLNSLS-----GELLRASWRCLA---PFGRFVEIGKRDILSNSKLGMRP- 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4545075  271 dshclLLKGATLAFLNdeVWNLSNVQQGKYLCILKDVMEKLSTGVFRPQLDEPIPLYEAKVSMEAVQKNQGRKKQVV 347
Cdd:cd05195 224 -----FLRNVSFSSVD--LDQLARERPELLRELLREVLELLEAGVLKPLPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
 
Name Accession Description Interval E-value
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
31-347 2.32e-55

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: 182.77  E-value: 2.32e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   31 NFVKLQVKACALSQINTkLLAEMKMKKDLFPVGREIAGIVLDVGSKVSFFQPDDEVVGILPldsedPGLCEVVRVHEHYL 110
Cdd:cd05195   1 DEVEVEVKAAGLNFRDV-LVALGLLPGDETPLGLECSGIVTRVGSGVTGLKVGDRVMGLAP-----GAFATHVRVDARLV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  111 VHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSLEDKQCLERFRP 190
Cdd:cd05195  75 VKIPDSLSFEEAATLPVAYLTAYYALVDLARLQKGESVLIHAAAGGVGQAAIQLAQHLGAEVFATVGSEEKREFLRELGG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  191 PIARVIDVSNgkVHVAESCLEETGGLGVDIVLDAGVrlyskDDEPAVKLQLLPhkhDIITLLGVGGHWVTTEENLQLDPp 270
Cdd:cd05195 155 PVDHIFSSRD--LSFADGILRATGGRGVDVVLNSLS-----GELLRASWRCLA---PFGRFVEIGKRDILSNSKLGMRP- 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4545075  271 dshclLLKGATLAFLNdeVWNLSNVQQGKYLCILKDVMEKLSTGVFRPQLDEPIPLYEAKVSMEAVQKNQGRKKQVV 347
Cdd:cd05195 224 -----FLRNVSFSSVD--LDQLARERPELLRELLREVLELLEAGVLKPLPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
1-347 6.74e-39

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: 140.28  E-value: 6.74e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    1 MKGLYFQQSSTDEeitfVFQEKE-DLPVTEDNFVKLQVKACALSQINTKLLA-EMKMKKDL-FPVGREIAGIVLDVGSKV 77
Cdd:COG0604   1 MKAIVITEFGGPE----VLELEEvPVPEPGPGEVLVRVKAAGVNPADLLIRRgLYPLPPGLpFIPGSDAAGVVVAVGEGV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   78 SFFQPDDEVVGILPldseDPGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAF 157
Cdd:COG0604  77 TGFKVGDRVAGLGR----GGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKPGETVLVHGAAGGV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  158 GTIAIQLAHHRGAKVISTAcSLEDKQ--CLERfrpPIARVIDvsNGKVHVAESCLEETGGLGVDIVLDA-GVRLYSkdde 234
Cdd:COG0604 153 GSAAVQLAKALGARVIATA-SSPEKAelLRAL---GADHVID--YREEDFAERVRALTGGRGVDVVLDTvGGDTLA---- 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  235 pavklqllphkhDIITLLGVGGHWVT----TEENLQLDPPDshcLLLKGATLAFLNdeVWNLSNVQQGKylcILKDVMEK 310
Cdd:COG0604 223 ------------RSLRALAPGGRLVSigaaSGAPPPLDLAP---LLLKGLTLTGFT--LFARDPAERRA---ALAELARL 282
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 4545075  311 LSTGVFRPQLDEPIPLYEAKVSMEAVQKNQGRKKQVV 347
Cdd:COG0604 283 LAAGKLRPVIDRVFPLEEAAEAHRLLESGKHRGKVVL 319
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
36-228 2.20e-32

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 122.11  E-value: 2.20e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075      36 QVKACALsqiNTK-LLAEMKMKKDLFPVGREIAGIVLDVGSKVSFFQPDDEVVGILPldsedPGLCEVVRVHEHYLVHKP 114
Cdd:smart00829   2 EVRAAGL---NFRdVLIALGLYPGEAVLGGECAGVVTRVGPGVTGLAVGDRVMGLAP-----GAFATRVVTDARLVVPIP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075     115 EKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSLEDKQCLERFRPPIAR 194
Cdd:smart00829  74 DGWSFEEAATVPVVFLTAYYALVDLARLRPGESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEKRDFLRALGIPDDH 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 4545075     195 VIDVSNGKvhVAESCLEETGGLGVDIVL--------DAGVRL 228
Cdd:smart00829 154 IFSSRDLS--FADEILRATGGRGVDVVLnslsgeflDASLRC 193
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
63-349 5.03e-27

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 108.96  E-value: 5.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    63 GREIAGIVLDVGSKVSFFQPDDEVVGILPldseDPGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHL 142
Cdd:PTZ00354  63 GLEVAGYVEDVGSDVKRFKEGDRVMALLP----GGGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDV 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   143 SPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSLEDKQCLERFRppiARVIDVSNGKVHVAESCLEETGGLGVDIVL 222
Cdd:PTZ00354 139 KKGQSVLIHAGASGVGTAAAQLAEKYGAATIITTSSEEKVDFCKKLA---AIILIRYPDEEGFAPKVKKLTGEKGVNLVL 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   223 DA-GVRLYSKDDEpavklqllphkhdiitLLGVGGHWV-------TTEENLQLDPpdshcLLLKGATLAF--LNDevwnl 292
Cdd:PTZ00354 216 DCvGGSYLSETAE----------------VLAVDGKWIvygfmggAKVEKFNLLP-----LLRKRASIIFstLRS----- 269
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4545075   293 snvQQGKYLCIL-----KDVMEKLSTGVFRPQLDEPIPLYEAKVSMEAVQKNQGRKKQVVQF 349
Cdd:PTZ00354 270 ---RSDEYKADLvasfeREVLPYMEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIGKVVLTV 328
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
158-224 9.90e-07

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 47.22  E-value: 9.90e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4545075    158 GTIAIQLAHHRGAKVIsTACSLEDKqcLErfrppIAR------VIDVSNgkVHVAESCLEETGGLGVDIVLDA 224
Cdd:pfam00107   3 GLAAIQLAKAAGAKVI-AVDGSEEK--LE-----LAKelgadhVINPKE--TDLVEEIKELTGGKGVDVVFDC 65
 
Name Accession Description Interval E-value
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
31-347 2.32e-55

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: 182.77  E-value: 2.32e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   31 NFVKLQVKACALSQINTkLLAEMKMKKDLFPVGREIAGIVLDVGSKVSFFQPDDEVVGILPldsedPGLCEVVRVHEHYL 110
Cdd:cd05195   1 DEVEVEVKAAGLNFRDV-LVALGLLPGDETPLGLECSGIVTRVGSGVTGLKVGDRVMGLAP-----GAFATHVRVDARLV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  111 VHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSLEDKQCLERFRP 190
Cdd:cd05195  75 VKIPDSLSFEEAATLPVAYLTAYYALVDLARLQKGESVLIHAAAGGVGQAAIQLAQHLGAEVFATVGSEEKREFLRELGG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  191 PIARVIDVSNgkVHVAESCLEETGGLGVDIVLDAGVrlyskDDEPAVKLQLLPhkhDIITLLGVGGHWVTTEENLQLDPp 270
Cdd:cd05195 155 PVDHIFSSRD--LSFADGILRATGGRGVDVVLNSLS-----GELLRASWRCLA---PFGRFVEIGKRDILSNSKLGMRP- 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4545075  271 dshclLLKGATLAFLNdeVWNLSNVQQGKYLCILKDVMEKLSTGVFRPQLDEPIPLYEAKVSMEAVQKNQGRKKQVV 347
Cdd:cd05195 224 -----FLRNVSFSSVD--LDQLARERPELLRELLREVLELLEAGVLKPLPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
1-347 6.74e-39

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: 140.28  E-value: 6.74e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    1 MKGLYFQQSSTDEeitfVFQEKE-DLPVTEDNFVKLQVKACALSQINTKLLA-EMKMKKDL-FPVGREIAGIVLDVGSKV 77
Cdd:COG0604   1 MKAIVITEFGGPE----VLELEEvPVPEPGPGEVLVRVKAAGVNPADLLIRRgLYPLPPGLpFIPGSDAAGVVVAVGEGV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   78 SFFQPDDEVVGILPldseDPGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAF 157
Cdd:COG0604  77 TGFKVGDRVAGLGR----GGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKPGETVLVHGAAGGV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  158 GTIAIQLAHHRGAKVISTAcSLEDKQ--CLERfrpPIARVIDvsNGKVHVAESCLEETGGLGVDIVLDA-GVRLYSkdde 234
Cdd:COG0604 153 GSAAVQLAKALGARVIATA-SSPEKAelLRAL---GADHVID--YREEDFAERVRALTGGRGVDVVLDTvGGDTLA---- 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  235 pavklqllphkhDIITLLGVGGHWVT----TEENLQLDPPDshcLLLKGATLAFLNdeVWNLSNVQQGKylcILKDVMEK 310
Cdd:COG0604 223 ------------RSLRALAPGGRLVSigaaSGAPPPLDLAP---LLLKGLTLTGFT--LFARDPAERRA---ALAELARL 282
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 4545075  311 LSTGVFRPQLDEPIPLYEAKVSMEAVQKNQGRKKQVV 347
Cdd:COG0604 283 LAAGKLRPVIDRVFPLEEAAEAHRLLESGKHRGKVVL 319
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
36-228 2.20e-32

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 122.11  E-value: 2.20e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075      36 QVKACALsqiNTK-LLAEMKMKKDLFPVGREIAGIVLDVGSKVSFFQPDDEVVGILPldsedPGLCEVVRVHEHYLVHKP 114
Cdd:smart00829   2 EVRAAGL---NFRdVLIALGLYPGEAVLGGECAGVVTRVGPGVTGLAVGDRVMGLAP-----GAFATRVVTDARLVVPIP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075     115 EKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSLEDKQCLERFRPPIAR 194
Cdd:smart00829  74 DGWSFEEAATVPVVFLTAYYALVDLARLRPGESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEKRDFLRALGIPDDH 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 4545075     195 VIDVSNGKvhVAESCLEETGGLGVDIVL--------DAGVRL 228
Cdd:smart00829 154 IFSSRDLS--FADEILRATGGRGVDVVLnslsgeflDASLRC 193
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
1-224 1.21e-31

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: 120.74  E-value: 1.21e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    1 MKGLYFQQSSTDEEItfvfqEKEDLPVTE--DNFVKLQVKACALSQINTKLLAEM--KMKKDLFPV--GREIAGIVLDVG 74
Cdd:cd05289   1 MKAVRIHEYGGPEVL-----ELADVPTPEpgPGEVLVKVHAAGVNPVDLKIREGLlkAAFPLTLPLipGHDVAGVVVAVG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   75 SKVSFFQPDDEVVGILPLDSeDPGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGA 154
Cdd:cd05289  76 PGVTGFKVGDEVFGMTPFTR-GGAYAEYVVVPADELALKPANLSFEEAAALPLAGLTAWQALFELGGLKAGQTVLIHGAA 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  155 SAFGTIAIQLAHHRGAKVISTACSlEDKQCLERFRPpiARVIDVSNGKVHVAEscleetGGLGVDIVLDA 224
Cdd:cd05289 155 GGVGSFAVQLAKARGARVIATASA-ANADFLRSLGA--DEVIDYTKGDFERAA------APGGVDAVLDT 215
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
63-340 5.27e-29

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: 114.08  E-value: 5.27e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   63 GREIAGIVLDVGSKVSFFQPDDEVVGILPldseDPGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHL 142
Cdd:cd05276  62 GLEVAGVVVAVGPGVTGWKVGDRVCALLA----GGGYAEYVVVPAGQLLPVPEGLSLVEAAALPEVFFTAWQNLFQLGGL 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  143 SPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSlEDKqcLERFRppiarvidvSNGKVHV--------AESCLEETG 214
Cdd:cd05276 138 KAGETVLIHGGASGVGTAAIQLAKALGARVIATAGS-EEK--LEACR---------ALGADVAinyrtedfAEEVKEATG 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  215 GLGVDIVLD--AGvrlyskddepavklqllPHKHDIITLLGVGGHWV--------TTEENLQLdppdshcLLLK-----G 279
Cdd:cd05276 206 GRGVDVILDmvGG-----------------DYLARNLRALAPDGRLVligllggaKAELDLAP-------LLRKrltltG 261
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4545075  280 ATLaflndevWNLSNVQQGKYL-CILKDVMEKLSTGVFRPQLDEPIPLYEAKVSMEAVQKNQ 340
Cdd:cd05276 262 STL-------RSRSLEEKAALAaAFREHVWPLFASGRIRPVIDKVFPLEEAAEAHRRMESNE 316
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
25-347 1.02e-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: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 110.38  E-value: 1.02e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   25 LPVTEDNFVKLQVKACALSQINTKLLaEMKMKKDL---FPV--GREIAGIVLDVGSKVSFFQPDDEVVGILPLDSEDpGL 99
Cdd:cd08267  21 IPTPKPGEVLVKVHAASVNPVDWKLR-RGPPKLLLgrpFPPipGMDFAGEVVAVGSGVTRFKVGDEVFGRLPPKGGG-AL 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  100 CEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLImDGAS-AFGTIAIQLAHHRGAKVISTaCS 178
Cdd:cd08267  99 AEYVVAPESGLAKKPEGVSFEEAAALPVAGLTALQALRDAGKVKPGQRVLI-NGASgGVGTFAVQIAKALGAHVTGV-CS 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  179 ledkqclerfrppiARVIDV--SNGKVHV----AESCLEETGGLGV-DIVLDA-GvrlYSKDDEPAVKLQLLPHKHDIIT 250
Cdd:cd08267 177 --------------TRNAELvrSLGADEVidytTEDFVALTAGGEKyDVIFDAvG---NSPFSLYRASLALKPGGRYVSV 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  251 LLGVGGHWVTteenlqldppdshcLLLKGATLAFLNDEVWNLSNVQQGKYLCILKDVMEKlstGVFRPQLDEPIPLYEAK 330
Cdd:cd08267 240 GGGPSGLLLV--------------LLLLPLTLGGGGRRLKFFLAKPNAEDLEQLAELVEE---GKLKPVIDSVYPLEDAP 302
                       330
                ....*....|....*..
gi 4545075  331 VSMEAVQKNQGRKKQVV 347
Cdd:cd08267 303 EAYRRLKSGRARGKVVI 319
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
63-349 5.03e-27

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 108.96  E-value: 5.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    63 GREIAGIVLDVGSKVSFFQPDDEVVGILPldseDPGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHL 142
Cdd:PTZ00354  63 GLEVAGYVEDVGSDVKRFKEGDRVMALLP----GGGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDV 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   143 SPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSLEDKQCLERFRppiARVIDVSNGKVHVAESCLEETGGLGVDIVL 222
Cdd:PTZ00354 139 KKGQSVLIHAGASGVGTAAAQLAEKYGAATIITTSSEEKVDFCKKLA---AIILIRYPDEEGFAPKVKKLTGEKGVNLVL 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   223 DA-GVRLYSKDDEpavklqllphkhdiitLLGVGGHWV-------TTEENLQLDPpdshcLLLKGATLAF--LNDevwnl 292
Cdd:PTZ00354 216 DCvGGSYLSETAE----------------VLAVDGKWIvygfmggAKVEKFNLLP-----LLRKRASIIFstLRS----- 269
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4545075   293 snvQQGKYLCIL-----KDVMEKLSTGVFRPQLDEPIPLYEAKVSMEAVQKNQGRKKQVVQF 349
Cdd:PTZ00354 270 ---RSDEYKADLvasfeREVLPYMEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIGKVVLTV 328
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
18-223 2.53e-26

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 106.87  E-value: 2.53e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   18 VFQEKE-DLPVTEDNFVKLQVKACALSQINTKLLAEMKMKKDLFPV--GREIAGIVLDVGSKVSFFQPDDEVVGILPLDS 94
Cdd:cd08272  14 VFELREvPRPQPGPGQVLVRVHASGVNPLDTKIRRGGAAARPPLPAilGCDVAGVVEAVGEGVTRFRVGDEVYGCAGGLG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   95 EDPG-LCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVI 173
Cdd:cd08272  94 GLQGsLAEYAVVDARLLALKPANLSMREAAALPLVGITAWEGLVDRAAVQAGQTVLIHGGAGGVGHVAVQLAKAAGARVY 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 4545075  174 STAcSLEDKQCLERFRppiARVIDvsNGKVHVAESCLEETGGLGVDIVLD 223
Cdd:cd08272 174 ATA-SSEKAAFARSLG---ADPII--YYRETVVEYVAEHTGGRGFDVVFD 217
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
1-224 2.31e-25

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: 104.12  E-value: 2.31e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    1 MKGLYFQQSSTDEEItfVFQEKEDLPVTEDNfVKLQVKACALSQINTkLLAEMK--MKKDL-FPVGREIAGIVLDVGSKV 77
Cdd:cd08241   1 MKAVVCKELGGPEDL--VLEEVPPEPGAPGE-VRIRVEAAGVNFPDL-LMIQGKyqVKPPLpFVPGSEVAGVVEAVGEGV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   78 SFFQPDDEVVGILPLDsedpGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAF 157
Cdd:cd08241  77 TGFKVGDRVVALTGQG----GFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALVRRARLQPGETVLVLGAAGGV 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4545075  158 GTIAIQLAHHRGAKVISTACSlEDKqcLErfrppIAR------VIDVSNGkvHVAESCLEETGGLGVDIVLDA 224
Cdd:cd08241 153 GLAAVQLAKALGARVIAAASS-EEK--LA-----LARalgadhVIDYRDP--DLRERVKALTGGRGVDVVYDP 215
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
1-223 1.26e-24

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: 102.33  E-value: 1.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    1 MKGLYFQQSSTDEEItfvfqEKEDLPVTE--DNFVKLQVKACALSQINTKLLAEMKMKKDLFP--VGREIAGIVLDVGSK 76
Cdd:cd08266   1 MKAVVIRGHGGPEVL-----EYGDLPEPEpgPDEVLVRVKAAALNHLDLWVRRGMPGIKLPLPhiLGSDGAGVVEAVGPG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   77 VSFFQPDDEVVgILPLDS------------------------EDPGLCEVVRVHEHYLVHKPEKVTWTEAAGSirdGVRA 132
Cdd:cd08266  76 VTNVKPGQRVV-IYPGIScgrceyclagrenlcaqygilgehVDGGYAEYVAVPARNLLPIPDNLSFEEAAAA---PLTF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  133 YTALHYL---SHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTAcSLEDKqcLERFRPPIA-RVIDVSNGKvhVAES 208
Cdd:cd08266 152 LTAWHMLvtrARLRPGETVLVHGAGSGVGSAAIQIAKLFGATVIATA-GSEDK--LERAKELGAdYVIDYRKED--FVRE 226
                       250
                ....*....|....*
gi 4545075  209 CLEETGGLGVDIVLD 223
Cdd:cd08266 227 VRELTGKRGVDVVVE 241
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
23-224 2.30e-24

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


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 101.52  E-value: 2.30e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   23 EDLPVTE--DNFVKLQVKACALSQintkllAEMKMKKDLFP--------VGREIAGIVLDVGSKVSFFQPDDEVVGILPL 92
Cdd:cd08268  18 EELPVPApgAGEVLIRVEAIGLNR------ADAMFRRGAYIeppplparLGYEAAGVVEAVGAGVTGFAVGDRVSVIPAA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   93 DSEDPGLC-EVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAK 171
Cdd:cd08268  92 DLGQYGTYaEYALVPAAAVVKLPDGLSFVEAAALWMQYLTAYGALVELAGLRPGDSVLITAASSSVGLAAIQIANAAGAT 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 4545075  172 VISTACSLEDKQCLERFrpPIARVIDVSNgkVHVAESCLEETGGLGVDIVLDA 224
Cdd:cd08268 172 VIATTRTSEKRDALLAL--GAAHVIVTDE--EDLVAEVLRITGGKGVDVVFDP 220
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
18-178 4.18e-23

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: 98.45  E-value: 4.18e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   18 VFQEKEDLPV-TEDNFVKLQVKACAL-------------SQINTKLLAE-MKMKKDLFPV--GREIAGIVLDVGSKVSFF 80
Cdd:cd08248  16 LLLENARIPViRKPNQVLIKVHAASVnpidvlmrsgygrTLLNKKRKPQsCKYSGIEFPLtlGRDCSGVVVDIGSGVKSF 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   81 QPDDEVVGILPLdsEDPG-LCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSP----GKSVLIMDGAS 155
Cdd:cd08248  96 EIGDEVWGAVPP--WSQGtHAEYVVVPENEVSKKPKNLSHEEAASLPYAGLTAWSALVNVGGLNPknaaGKRVLILGGSG 173
                       170       180
                ....*....|....*....|...
gi 4545075  156 AFGTIAIQLAHHRGAKVISTaCS 178
Cdd:cd08248 174 GVGTFAIQLLKAWGAHVTTT-CS 195
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
33-224 2.32e-22

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: 94.70  E-value: 2.32e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   33 VKLQVKACALSQINTKLLAEMKMKKDLFPV--GREIAGIVLDVGSKVSFFQPDDEVV-------GILPLDSEDP------ 97
Cdd:cd05188   2 VLVRVEAAGLCGTDLHIRRGGYPPPPKLPLilGHEGAGVVVEVGPGVTGVKVGDRVVvlpnlgcGTCELCRELCpgggil 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   98 ------GLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMdGASAFGTIAIQLAHHRGAK 171
Cdd:cd05188  82 gegldgGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVLKPGDTVLVL-GAGGVGLLAAQLAKAAGAR 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4545075  172 VISTACSledKQCLERfrppiAR---VIDVSNGKVHVAESCLEETGGLGVDIVLDA 224
Cdd:cd05188 161 VIVTDRS---DEKLEL-----AKelgADHVIDYKEEDLEEELRLTGGGGADVVIDA 208
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
24-223 8.48e-21

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: 90.95  E-value: 8.48e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   24 DLPVTEDNFVKLQVKACALSqintklLAEMKMKKDLFPV--------GREIAGIVLDVGSKVSFFQPDDEVvgILPLDSE 95
Cdd:cd08251   1 EVAPPGPGEVRIQVRAFSLN------FGDLLCVRGLYPTmppypftpGFEASGVVRAVGPHVTRLAVGDEV--IAGTGES 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   96 DPGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLShLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVIST 175
Cdd:cd08251  73 MGGHATLVTVPEDQVVRKPASLSFEEACALPVVFLTVIDAFARAG-LAKGEHILIQTATGGTGLMAVQLARLKGAEIYAT 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 4545075  176 ACSLEDKQCLERFRPPiaRVIDVSNGKVHvaESCLEETGGLGVDIVLD 223
Cdd:cd08251 152 ASSDDKLEYLKQLGVP--HVINYVEEDFE--EEIMRLTGGRGVDVVIN 195
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-223 7.65e-20

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: 88.87  E-value: 7.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    1 MKGLYFQQSStdEEITFVFQEKEdLPVTEDNFVKLQVKACALSQINTKLLAEMKMKKDL-FPVGREIAGIVLDVGSKVSF 79
Cdd:cd08271   1 MKAWVLPKPG--AALQLTLEEIE-IPGPGAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYpHVPGVDGAGVVVAVGAKVTG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   80 FQPDDEVVGILPLdSEDPGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAFGT 159
Cdd:cd08271  78 WKVGDRVAYHASL-ARGGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYQALFKKLRIEAGRTILITGGAGGVGS 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4545075  160 IAIQLAHHRGAKVISTaCSledKQCLERFRPPIAR-VIDVSNGKvhVAESCLEETGGLGVDIVLD 223
Cdd:cd08271 157 FAVQLAKRAGLRVITT-CS---KRNFEYVKSLGADhVIDYNDED--VCERIKEITGGRGVDAVLD 215
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
23-348 2.18e-19

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


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 87.32  E-value: 2.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   23 EDLPVTEDNFVKLQVKACALSQINTKLLAEMKMKKDLFPV--GREIAGIVLDVGSKVSFFQPDDEVVGILPLDSEdpglC 100
Cdd:cd08273  20 ADLPEPAAGEVVVKVEASGVSFADVQMRRGLYPDQPPLPFtpGYDLVGRVDALGSGVTGFEVGDRVAALTRVGGN----A 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  101 EVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACsle 180
Cdd:cd08273  96 EYINLDAKYLVPVPEGVDAAEAVCLVLNYVTAYQMLHRAAKVLTGQRVLIHGASGGVGQALLELALLAGAEVYGTAS--- 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  181 dkqclERFRPPIARV----IDVSNGKVHVAesclEETGGlGVDIVLDaGVRLYSKDDEpavkLQLLPHKHdiiTLLGVGG 256
Cdd:cd08273 173 -----ERNHAALRELgatpIDYRTKDWLPA----MLTPG-GVDVVFD-GVGGESYEES----YAALAPGG---TLVCYGG 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  257 HWVTTEENLQLDP--PDSHCLLLKGAT-----LAFLNdeVWNLSNVQQGKYLCILKDVMEKLSTGVFRPQLDEPIPLYEA 329
Cdd:cd08273 235 NSSLLQGRRSLAAlgSLLARLAKLKLLptgrrATFYY--VWRDRAEDPKLFRQDLTELLDLLAKGKIRPKIAKRLPLSEV 312
                       330
                ....*....|....*....
gi 4545075  330 KVSMEAVQKNQGRKKQVVQ 348
Cdd:cd08273 313 AEAHRLLESGKVVGKIVLL 331
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
26-176 8.45e-19

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: 86.10  E-value: 8.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   26 PVTEDNFVKLQVKACALSQINTKLLAEMKMKKDLFPVGREIAGIVLDVGSKVSFFQPDDEVVGI----LPLDSEDPGLCE 101
Cdd:cd08249  22 PKPGPDEVLVKVKAVALNPVDWKHQDYGFIPSYPAILGCDFAGTVVEVGSGVTRFKVGDRVAGFvhggNPNDPRNGAFQE 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  102 VVRVHEHYLVHKPEKVTWTEAAgSIrdGVRAYTA---LHYLSHL----------SPGKSVLIMDGASAFGTIAIQLAHHR 168
Cdd:cd08249 102 YVVADADLTAKIPDNISFEEAA-TL--PVGLVTAalaLFQKLGLplpppkpspaSKGKPVLIWGGSSSVGTLAIQLAKLA 178

                ....*...
gi 4545075  169 GAKVISTA 176
Cdd:cd08249 179 GYKVITTA 186
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
1-348 1.23e-17

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: 82.25  E-value: 1.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    1 MKGLYFQQSSTDEeitfVFQEkEDLPVTE--DNFVKLQVKACALSQINTKLLAEM--KMKKDLFPVGREIAGIVLDVGSK 76
Cdd:cd08253   1 MRAIRYHEFGAPD----VLRL-GDLPVPTpgPGEVLVRVHASGVNPVDTYIRAGAypGLPPLPYVPGSDGAGVVEAVGEG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   77 VSFFQPDDEV-VGILPLDSEDPGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGAS 155
Cdd:cd08253  76 VDGLKVGDRVwLTNLGWGRRQGTAAEYVVVPADQLVPLPDGVSFEQGAALGIPALTAYRALFHRAGAKAGETVLVHGGSG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  156 AFGTIAIQLAHHRGAKVISTACSLEDKQclerfrppIARvidvSNGKVHV--------AESCLEETGGLGVDIVLD--AG 225
Cdd:cd08253 156 AVGHAAVQLARWAGARVIATASSAEGAE--------LVR----QAGADAVfnyraedlADRILAATAGQGVDVIIEvlAN 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  226 VRLyskddepAVKLQLLPHkHDIITLLGVGGHWVTTEenlqLDPpdshcLLLKGATLAFLNdeVWNLSNVQQGKylcILK 305
Cdd:cd08253 224 VNL-------AKDLDVLAP-GGRIVVYGSGGLRGTIP----INP-----LMAKEASIRGVL--LYTATPEERAA---AAE 281
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 4545075  306 DVMEKLSTGVFRPQLDEPIPLYEAKVSMEAVQKNQGRKKQVVQ 348
Cdd:cd08253 282 AIAAGLADGALRPVIAREYPLEEAAAAHEAVESGGAIGKVVLD 324
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
60-226 1.58e-17

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: 82.10  E-value: 1.58e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   60 FPVGREIAGIVLDVGSKVSFFQPDDEVVGILPLDSedpgLCEVVRVHEHYLVHKPEKVTWTEAAGSIrdgVRAYTAlHYL 139
Cdd:cd05286  56 FVLGVEGAGVVEAVGPGVTGFKVGDRVAYAGPPGA----YAEYRVVPASRLVKLPDGISDETAAALL---LQGLTA-HYL 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  140 SH----LSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTAcSLEDKqcLErfrppIAR------VIDVSNGKvhVAESC 209
Cdd:cd05286 128 LRetypVKPGDTVLVHAAAGGVGLLLTQWAKALGATVIGTV-SSEEK--AE-----LARaagadhVINYRDED--FVERV 197
                       170
                ....*....|....*..
gi 4545075  210 LEETGGLGVDIVLDaGV 226
Cdd:cd05286 198 REITGGRGVDVVYD-GV 213
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
67-225 1.02e-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: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 79.89  E-value: 1.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   67 AGIVLDVGSKVSFFQPDDEVVGIL-------PLDSED---------PG-LCEVVRVHEHYLVHKPEKVTWTEAAGSIRDG 129
Cdd:cd08276  66 AGEVVAVGEGVTRFKVGDRVVPTFfpnwldgPPTAEDeasalggpiDGvLAEYVVLPEEGLVRAPDHLSFEEAATLPCAG 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  130 VRAYTALHYLSHLSPGKSVLIM--DGASAFgtiAIQLAHHRGAKVISTAcSLEDKqcLERfrppiAR---VIDVSNGKVH 204
Cdd:cd08276 146 LTAWNALFGLGPLKPGDTVLVQgtGGVSLF---ALQFAKAAGARVIATS-SSDEK--LER-----AKalgADHVINYRTT 214
                       170       180
                ....*....|....*....|...
gi 4545075  205 --VAESCLEETGGLGVDIVLDAG 225
Cdd:cd08276 215 pdWGEEVLKLTGGRGVDHVVEVG 237
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
1-283 3.05e-16

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 78.23  E-value: 3.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    1 MKGLYFQQSSTDeeitFVFQEKEDlPVTEDNFVKLQVKACAL--SQINTkllAEMKMKKDLFPV--GREIAGIVLDVGSK 76
Cdd:COG1064   1 MKAAVLTEPGGP----LELEEVPR-PEPGPGEVLVKVEACGVchSDLHV---AEGEWPVPKLPLvpGHEIVGRVVAVGPG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   77 VSFFQPDDEvVGILPLDS---------------EDP---------GLCEVVRVHEHYLVHKPEKVTWTEAA-----GSIr 127
Cdd:COG1064  73 VTGFKVGDR-VGVGWVDScgtceycrsgrenlcENGrftgyttdgGYAEYVVVPARFLVKLPDGLDPAEAApllcaGIT- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  128 dgvrAYTALHyLSHLSPGKSVLIMdGASAFGTIAIQLAHHRGAKVIstacsledkqclerfrppiarVIDVSNGKVHVAE 207
Cdd:COG1064 151 ----AYRALR-RAGVGPGDRVAVI-GAGGLGHLAVQIAKALGAEVI---------------------AVDRSPEKLELAR 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  208 ScleetggLGVDIVLDagvrlySKDDEPAVKLQLL----------PHKHDI---ITLLGVGGHWVT---TEENLQLDPPD 271
Cdd:COG1064 204 E-------LGADHVVN------SSDEDPVEAVRELtgadvvidtvGAPATVnaaLALLRRGGRLVLvglPGGPIPLPPFD 270
                       330
                ....*....|..
gi 4545075  272 shcLLLKGATLA 283
Cdd:COG1064 271 ---LILKERSIR 279
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
20-231 7.49e-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: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 77.24  E-value: 7.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   20 QEKEDLPVTEDNFVKLQVKACALSqintklLAEMKMKKDLFP--------VGREIAGIVLDVGSKVSFFQPDDEVVGILP 91
Cdd:cd08275  16 VEKEALPEPSSGEVRVRVEACGLN------FADLMARQGLYDsapkppfvPGFECAGTVEAVGEGVKDFKVGDRVMGLTR 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   92 LDsedpGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAFGTIAIQLA-HHRGA 170
Cdd:cd08275  90 FG----GYAEVVNVPADQVFPLPDGMSFEEAAAFPVNYLTAYYALFELGNLRPGQSVLVHSAAGGVGLAAGQLCkTVPNV 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4545075  171 KVISTACSLEDKQCLERFrppIARVID--VSNGKVHVAESCLEetgglGVDIVLDA-GVRLYSK 231
Cdd:cd08275 166 TVVGTASASKHEALKENG---VTHVIDyrTQDYVEEVKKISPE-----GVDIVLDAlGGEDTRK 221
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
24-224 3.89e-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: 71.96  E-value: 3.89e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   24 DLPVTEDNFVKLQVKACAL--SQINTkllAEMKMKKDLFPV--GREIAGIVLDVGSKVSFFQPDDEVV--------GILP 91
Cdd:cd08258  20 PEPEPGPGEVLIKVAAAGIcgSDLHI---YKGDYDPVETPVvlGHEFSGTIVEVGPDVEGWKVGDRVVsettfstcGRCP 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   92 L-DSEDPGLC---------------EVVRVHEHYLVHKPEKVTWTEAAGSIRDGVrAYTALHYLSHLSPGKSVLIMdGAS 155
Cdd:cd08258  97 YcRRGDYNLCphrkgigtqadggfaEYVLVPEESLHELPENLSLEAAALTEPLAV-AVHAVAERSGIRPGDTVVVF-GPG 174
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4545075  156 AFGTIAIQLAHHRGAKVISTACSlEDKqclERFrpPIAR---VIDVSNGKVHVAESCLEETGGLGVDIVLDA 224
Cdd:cd08258 175 PIGLLAAQVAKLQGATVVVVGTE-KDE---VRL--DVAKelgADAVNGGEEDLAELVNEITDGDGADVVIEC 240
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
19-223 5.98e-14

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: 71.89  E-value: 5.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   19 FQEKEDLPVTEDNF--VKLQVKACALSQINTKLL--AEMKMKKDLFPVGREIAGIVLDVGSKVSFFQPDDEVVGILPLDS 94
Cdd:cd08254  13 LLVLEEVPVPEPGPgeVLVKVKAAGVCHSDLHILdgGVPTLTKLPLTLGHEIAGTVVEVGAGVTNFKVGDRVAVPAVIPC 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   95 EDPGLC-----------------------EVVRVHEHYLVHKPEKVTWTEAAgSIRDGV-RAYTALHYLSHLSPGKSVLI 150
Cdd:cd08254  93 GACALCrrgrgnlclnqgmpglgidggfaEYIVVPARALVPVPDGVPFAQAA-VATDAVlTPYHAVVRAGEVKPGETVLV 171
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4545075  151 MdGASAFGTIAIQLAHHRGAKVIstACSLeDKQCLERfrppiAR---VIDVSNGKVHVAESCLEETGGLGVDIVLD 223
Cdd:cd08254 172 I-GLGGLGLNAVQIAKAMGAAVI--AVDI-KEEKLEL-----AKelgADEVLNSLDDSPKDKKAAGLGGGFDVIFD 238
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
24-224 6.65e-14

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: 71.86  E-value: 6.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   24 DLPVTEDNFVKLQVKACALSQINTKLLAEMKMKKDLFPV-GREIAGIVLDVGSKVSFFQPDDEV---------------- 86
Cdd:cd08235  18 PVPEPGPGEVLVKVRACGICGTDVKKIRGGHTDLKPPRIlGHEIAGEIVEVGDGVTGFKVGDRVfvaphvpcgechyclr 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   87 -----------VGILpldsEDPGLCEVVRVHEHYLVHK-----PEKVTWTEA------AGSIRdGVRaytalhyLSHLSP 144
Cdd:cd08235  98 gnenmcpnykkFGNL----YDGGFAEYVRVPAWAVKRGgvlklPDNVSFEEAalveplACCIN-AQR-------KAGIKP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  145 GKSVLIMdGASAFGTIAIQLAHHRGAKVISTACSLED--KQCLERfrpPIARVIDVSngKVHVAESCLEETGGLGVDIVL 222
Cdd:cd08235 166 GDTVLVI-GAGPIGLLHAMLAKASGARKVIVSDLNEFrlEFAKKL---GADYTIDAA--EEDLVEKVRELTDGRGADVVI 239

                ..
gi 4545075  223 DA 224
Cdd:cd08235 240 VA 241
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
1-322 8.02e-14

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: 71.40  E-value: 8.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    1 MKGLYFQQSSTDEEiTFVFQEKE-DLPVTEDNFVKLQVKACALSQINTKLLAEMKMKKDLFPV-GREIAGIVLDVGSKVS 78
Cdd:cd08252   1 MKAIGFTQPLPITD-PDSLIDIElPKPVPGGRDLLVRVEAVSVNPVDTKVRAGGAPVPGQPKIlGWDASGVVEAVGSEVT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   79 FFQPDDEV--VGilplDSEDPGL-CEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSP-----GKSVLI 150
Cdd:cd08252  80 LFKVGDEVyyAG----DITRPGSnAEYQLVDERIVGHKPKSLSFAEAAALPLTSLTAWEALFDRLGISEdaeneGKTLLI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  151 MDGASAFGTIAIQLA-HHRGAKVISTACsledkqclerfRPpiarvidvsngkvhvaES---CLEetggLGVDIVLDagv 226
Cdd:cd08252 156 IGGAGGVGSIAIQLAkQLTGLTVIATAS-----------RP----------------ESiawVKE----LGADHVIN--- 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  227 rlYSKDDEPAVKLQLLPHKHDIITLLGVGGHW----------------VTTEENLQLDPpdshcLLLKGATLaflndeVW 290
Cdd:cd08252 202 --HHQDLAEQLEALGIEPVDYIFCLTDTDQHWdamaeliapqghicliVDPQEPLDLGP-----LKSKSASF------HW 268
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 4545075  291 NL----------SNVQQGKylcILKDVMEKLSTGVFRPQLDE 322
Cdd:cd08252 269 EFmftrsmfqtpDMIEQHE---ILNEVADLLDAGKLKTTLTE 307
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
2-261 8.08e-14

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: 71.53  E-value: 8.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    2 KGLYFQQSSTDEEITFvfqEKEDLPVT-EDNFVKLQVKACALSQINTKLLAE----MKMKKDLFpvGREIAGIVLDVGSK 76
Cdd:cd08247   2 KALTFKNNTSPLTITT---IKLPLPNCyKDNEIVVKVHAAALNPVDLKLYNSytfhFKVKEKGL--GRDYSGVIVKVGSN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   77 V-SFFQPDDEVVGILPLDSEDPGLCEvvrvheHYL-----------VHKPEKVTWTEAAGSIRDGVRAYTAL-HYLSHLS 143
Cdd:cd08247  77 VaSEWKVGDEVCGIYPHPYGGQGTLS------QYLlvdpkkdkksiTRKPENISLEEAAAWPLVLGTAYQILeDLGQKLG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  144 PGKSVLIMDGASAFGTIAIQLA--HHRGAKVISTaCSledKQCLERFRPP-IARVID-VSNGKVHVAESCLEETGGLG-V 218
Cdd:cd08247 151 PDSKVLVLGGSTSVGRFAIQLAknHYNIGTVVGT-CS---SRSAELNKKLgADHFIDyDAHSGVKLLKPVLENVKGQGkF 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 4545075  219 DIVLDAgvrlYSKDDepavklqLLPHKHDIITLLGVGGHWVTT 261
Cdd:cd08247 227 DLILDC----VGGYD-------LFPHINSILKPKSKNGHYVTI 258
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
1-224 1.16e-13

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: 70.94  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    1 MKGLYFQqsstdEEITFVFQEKEDlPVTEDNFVKLQVKACAL--SQINtklLAEMKMKKDLFPV--GREIAGIVLDVGSK 76
Cdd:COG1063   1 MKALVLH-----GPGDLRLEEVPD-PEPGPGEVLVRVTAVGIcgSDLH---IYRGGYPFVRPPLvlGHEFVGEVVEVGEG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   77 VSFFQPDDEVV---------------------------GILPLDSedpGLCEVVRVHEHYLVHKPEKVTWTEAA-----G 124
Cdd:COG1063  72 VTGLKVGDRVVvepnipcgecrycrrgrynlcenlqflGIAGRDG---GFAEYVRVPAANLVKVPDGLSDEAAAlveplA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  125 sirdgvrayTALH--YLSHLSPGKSVLIMdGASAFGTIAIQLAHHRGAKVIsTACSLEDkqclerFRPPIAR------VI 196
Cdd:COG1063 149 ---------VALHavERAGVKPGDTVLVI-GAGPIGLLAALAARLAGAARV-IVVDRNP------ERLELARelgadaVV 211
                       250       260
                ....*....|....*....|....*...
gi 4545075  197 DVSngKVHVAESCLEETGGLGVDIVLDA 224
Cdd:COG1063 212 NPR--EEDLVEAVRELTGGRGADVVIEA 237
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
63-182 3.23e-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: 70.14  E-value: 3.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   63 GREIAGIVLDVGSKVSFFQPDDEVV---GILPLDSE-----DPGLC----------------EVVRVHEHYLVHKPEKVT 118
Cdd:cd08246  86 GSDASGIVWAVGEGVKNWKVGDEVVvhcSVWDGNDPeraggDPMFDpsqriwgyetnygsfaQFALVQATQLMPKPKHLS 165
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4545075  119 WTEAAGSIRDGVRAYTALHylSH----LSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSlEDK 182
Cdd:cd08246 166 WEEAAAYMLVGATAYRMLF--GWnpntVKPGDNVLIWGASGGLGSMAIQLARAAGANPVAVVSS-EEK 230
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
24-224 1.42e-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: 67.64  E-value: 1.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   24 DLPVTEDNFVKLQVKACAL--SQIntklLAEMKMKKDLFPV--GREIAGIVLDVGSKVSFFQPDDEVVGIlPL------- 92
Cdd:cd08236  18 PKPEPGPGEVLVKVKACGIcgSDI----PRYLGTGAYHPPLvlGHEFSGTVEEVGSGVDDLAVGDRVAVN-PLlpcgkce 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   93 --DSEDPGLC---------------EVVRVHEHYLVHKPEKVTWTEAAGSirdgVRAYTALH--YLSHLSPGKSVLIMdG 153
Cdd:cd08236  93 ycKKGEYSLCsnydyigsrrdgafaEYVSVPARNLIKIPDHVDYEEAAMI----EPAAVALHavRLAGITLGDTVVVI-G 167
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4545075  154 ASAFGTIAIQLAHHRGAKVISTACSLEDKqcLErfrppIARVI---DVSNGKVHVAESCLEETGGLGVDIVLDA 224
Cdd:cd08236 168 AGTIGLLAIQWLKILGAKRVIAVDIDDEK--LA-----VARELgadDTINPKEEDVEKVRELTEGRGADLVIEA 234
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
60-224 3.20e-12

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: 66.53  E-value: 3.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   60 FPVGREIAGIVLDVGSKVSFFQPDDEVvgiLPLDSEdpGL-CEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHY 138
Cdd:cd05282  58 AVPGNEGVGVVVEVGSGVSGLLVGQRV---LPLGGE--GTwQEYVVAPADDLIPVPDSISDEQAAMLYINPLTAWLMLTE 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  139 LSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSLEDKQCLERFRppIARVIDVSNGKvhVAESCLEETGGLGV 218
Cdd:cd05282 133 YLKLPPGDWVIQNAANSAVGRMLIQLAKLLGFKTINVVRRDEQVEELKALG--ADEVIDSSPED--LAQRVKEATGGAGA 208

                ....*.
gi 4545075  219 DIVLDA 224
Cdd:cd05282 209 RLALDA 214
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
1-268 2.81e-11

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: 63.52  E-value: 2.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    1 MKGLYFQQSSTD----EEItfvfqekeDLPVTEDNFVKLQVKACALSQINTKLLAEMKMKKDLFPVGREIAGIVLDVGSK 76
Cdd:cd08264   1 MKALVFEKSGIEnlkvEDV--------KDPKPGPGEVLIRVKMAGVNPVDYNVINAVKVKPMPHIPGAEFAGVVEEVGDH 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   77 VSFFQPDDEVV------------------------GILPLDSeDPGLCEVVRVHEHYLVHKPEKVTWTEAAgSIrdGVRA 132
Cdd:cd08264  73 VKGVKKGDRVVvynrvfdgtcdmclsgnemlcrngGIIGVVS-NGGYAEYIVVPEKNLFKIPDSISDELAA-SL--PVAA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  133 YTALH--YLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVIstACSleDKQCLERFRPpiARVIDVSNgkvhVAESCL 210
Cdd:cd08264 149 LTAYHalKTAGLGPGETVVVFGASGNTGIFAVQLAKMMGAEVI--AVS--RKDWLKEFGA--DEVVDYDE----VEEKVK 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4545075  211 EETGglGVDIVLDA-GVRLYSKDdepavklqllphkhdiITLLGVGGHWVT----TEENLQLD 268
Cdd:cd08264 219 EITK--MADVVINSlGSSFWDLS----------------LSVLGRGGRLVTfgtlTGGEVKLD 263
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
60-257 1.60e-10

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: 61.42  E-value: 1.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   60 FPVGREIAGIVLDVGSKVSFFQPDDEVV-----------------------GILPLDSEDPGLCEVVRVHEHYLVHKPEK 116
Cdd:cd05284  59 FTLGHENAGWVEEVGSGVDGLKEGDPVVvhppwgcgtcrycrrgeenycenARFPGIGTDGGFAEYLLVPSRRLVKLPRG 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  117 VTWTEAAGSIRDGVRAYTAL-HYLSHLSPGKSVLIMdGASAFGTIAIQLAhhR---GAKVISTACSLEDKQCLERFRppi 192
Cdd:cd05284 139 LDPVEAAPLADAGLTAYHAVkKALPYLDPGSTVVVI-GVGGLGHIAVQIL--RaltPATVIAVDRSEEALKLAERLG--- 212
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4545075  193 ARVidVSNGKVHVAESCLEETGGLGVDIVLDagvrLYSKDDEPAVKLQLLPHKHDIItLLGVGGH 257
Cdd:cd05284 213 ADH--VLNASDDVVEEVRELTGGRGADAVID----FVGSDETLALAAKLLAKGGRYV-IVGYGGH 270
PRK10754 PRK10754
NADPH:quinone reductase;
30-224 1.62e-10

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 61.29  E-value: 1.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    30 DNFVKLQVKACALSQINTKllaemkMKKDLFPV-------GREIAGIVLDVGSKVSFFQPDDEVVGIlplDSEDPGLCEV 102
Cdd:PRK10754  28 ENEVQVENKAIGINYIDTY------IRSGLYPPpslpsglGTEAAGVVSKVGSGVKHIKVGDRVVYA---QSALGAYSSV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   103 VRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSLEDK 182
Cdd:PRK10754  99 HNVPADKAAILPDAISFEQAAASFLKGLTVYYLLRKTYEIKPDEQFLFHAAAGGVGLIACQWAKALGAKLIGTVGSAQKA 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 4545075   183 QclerfRPPIARVIDVSN-GKVHVAESCLEETGGLGVDIVLDA 224
Cdd:PRK10754 179 Q-----RAKKAGAWQVINyREENIVERVKEITGGKKVRVVYDS 216
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
63-224 3.41e-10

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: 60.46  E-value: 3.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   63 GREIAGIVLDVGSKVsffqpDDE-----VVGILPLDSEdpGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAyTALH 137
Cdd:cd08244  64 GGEVAGVVDAVGPGV-----DPAwlgrrVVAHTGRAGG--GYAELAVADVDSLHPVPDGLDLEAAVAVVHDGRTA-LGLL 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  138 YLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSlEDKQCLERfRPPIARVIDVSN----GKVHvaesclEET 213
Cdd:cd08244 136 DLATLTPGDVVLVTAAAGGLGSLLVQLAKAAGATVVGAAGG-PAKTALVR-ALGADVAVDYTRpdwpDQVR------EAL 207
                       170
                ....*....|.
gi 4545075  214 GGLGVDIVLDA 224
Cdd:cd08244 208 GGGGVTVVLDG 218
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
63-223 3.63e-09

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: 57.33  E-value: 3.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   63 GREIAGIVLDVGSKVSFFQPDDEVVG-----------------------ILPLDSEDPGLCEVVRVHEHYLVHKPEKVTw 119
Cdd:cd08259  59 GHEIVGTVEEVGEGVERFKPGDRVILyyyipcgkceyclsgeenlcrnrAEYGEEVDGGFAEYVKVPERSLVKLPDNVS- 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  120 TEAAGSIRDGV-RAYTALHyLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSlEDKqcLERFRPPIARVIDV 198
Cdd:cd08259 138 DESAALAACVVgTAVHALK-RAGVKKGDTVLVTGAGGGVGIHAIQLAKALGARVIAVTRS-PEK--LKILKELGADYVID 213
                       170       180
                ....*....|....*....|....*
gi 4545075  199 SNGKVHVAESCleetggLGVDIVLD 223
Cdd:cd08259 214 GSKFSEDVKKL------GGADVVIE 232
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
63-224 4.77e-09

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: 56.81  E-value: 4.77e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   63 GREIAGIVLDVGSKVSFFQPDDEVVgILPLDS------------------------EDPGLCEVVRVHEHYLvHKPEKVT 118
Cdd:cd08261  58 GHELSGEVVEVGEGVAGLKVGDRVV-VDPYIScgecyacrkgrpnccenlqvlgvhRDGGFAEYIVVPADAL-LVPEGLS 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  119 WTEAAGsirdgVRAYT-ALHYLSH--LSPGKSVLIMdGASAFGTIAIQLAHHRGAKVISTacsleDKQClERFRppIAR- 194
Cdd:cd08261 136 LDQAAL-----VEPLAiGAHAVRRagVTAGDTVLVV-GAGPIGLGVIQVAKARGARVIVV-----DIDD-ERLE--FARe 201
                       170       180       190
                ....*....|....*....|....*....|....*
gi 4545075  195 -----VIDVSNGKVHvaESCLEETGGLGVDIVLDA 224
Cdd:cd08261 202 lgaddTINVGDEDVA--ARLRELTDGEGADVVIDA 234
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
26-347 5.22e-09

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: 56.85  E-value: 5.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   26 PVTEDNFVKLQVKACALSQintkllAEMKMKKDLFP-------VGREIAGIVlDVGSKvSFFQPDDEVVGILP--LDSED 96
Cdd:cd08243  23 PEPKPGWVLIRVKAFGLNR------SEIFTRQGHSPsvkfprvLGIEAVGEV-EEAPG-GTFTPGQRVATAMGgmGRTFD 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   97 PGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTA 176
Cdd:cd08243  95 GSYAEYTLVPNEQVYAIDSDLSWAELAALPETYYTAWGSLFRSLGLQPGDTLLIRGGTSSVGLAALKLAKALGATVTATT 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  177 CSLEDKQCLERFrpPIARVIdVSNGKvhVAESCLEEtgGLGVDIVLD-AGVrlyskddePAVK--LQLLpHKHDIITLLG 253
Cdd:cd08243 175 RSPERAALLKEL--GADEVV-IDDGA--IAEQLRAA--PGGFDKVLElVGT--------ATLKdsLRHL-RPGGIVCMTG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  254 V-GGHWVTTEENLQLDPPDSHCLLLKGATLAFLNDEVwnlsnvqqgkylciLKDVMEKLSTGVFRPQLDEPIPL---YEA 329
Cdd:cd08243 239 LlGGQWTLEDFNPMDDIPSGVNLTLTGSSSGDVPQTP--------------LQELFDFVAAGHLDIPPSKVFTFdeiVEA 304
                       330
                ....*....|....*...
gi 4545075  330 KVSMEAvqkNQGRKKQVV 347
Cdd:cd08243 305 HAYMES---NRAFGKVVV 319
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
63-226 6.01e-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: 6.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   63 GREIAGIVLDVGSKVSFFQPDDEVV------------------------GILPLDSEDPGLCEVVRVHEHYLVHKPEKVT 118
Cdd:cd08233  69 GHEFSGVVVEVGSGVTGFKVGDRVVveptikcgtcgackrglynlcdslGFIGLGGGGGGFAEYVVVPAYHVHKLPDNVP 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  119 WTEAA----GSIrdGVRAYTalhyLSHLSPGKSVLIMdGASAFGTIAIQLAHHRGA-KVISTACSLEDKQCLERFrpPIA 193
Cdd:cd08233 149 LEEAAlvepLAV--AWHAVR----RSGFKPGDTALVL-GAGPIGLLTILALKAAGAsKIIVSEPSEARRELAEEL--GAT 219
                       170       180       190
                ....*....|....*....|....*....|....
gi 4545075  194 RVIDVSngKVHVAESCLEETGGLGVDIVLD-AGV 226
Cdd:cd08233 220 IVLDPT--EVDVVAEVRKLTGGGGVDVSFDcAGV 251
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
60-224 7.87e-09

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: 55.74  E-value: 7.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   60 FPVGREIAGIVLDVGSKVSFFQPDDEVVGILPLDsedpglcEVVRVHEHYLVHKPEKVTWTEAA----GSIrdgvrAYTA 135
Cdd:cd08255  22 LPPGYSSVGRVVEVGSGVTGFKPGDRVFCFGPHA-------ERVVVPANLLVPLPDGLPPERAAltalAAT-----ALNG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  136 LHyLSHLSPGKSVLIMdGASAFGTIAIQLAHHRGAKVIsTACSLEDkqclerFRPPIARVIDVSNGKVHVAEsclEETGG 215
Cdd:cd08255  90 VR-DAEPRLGERVAVV-GLGLVGLLAAQLAKAAGAREV-VGVDPDA------ARRELAEALGPADPVAADTA---DEIGG 157

                ....*....
gi 4545075  216 LGVDIVLDA 224
Cdd:cd08255 158 RGADVVIEA 166
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
63-260 1.16e-08

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: 55.96  E-value: 1.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   63 GREIAGIVLDVGSKVSFFQPDDEV---VGIlPLDSEDP---G---LCEVVR---------------VHEHYLVHK-PEKV 117
Cdd:cd05285  59 GHESAGTVVAVGSGVTHLKVGDRVaiePGV-PCRTCEFcksGrynLCPDMRfaatppvdgtlcryvNHPADFCHKlPDNV 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  118 TWTEAA----GSIrdGVRAYTalhyLSHLSPGKSVLIMdGASAFGTIAIQLAHHRGAKVIsTACSLEDKQcLERFR-PPI 192
Cdd:cd05285 138 SLEEGAlvepLSV--GVHACR----RAGVRPGDTVLVF-GAGPIGLLTAAVAKAFGATKV-VVTDIDPSR-LEFAKeLGA 208
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4545075  193 ARVIDVSNGKVH-VAESCLEETGGLGVDIVLDA-GVrlyskddEPAVKLQLLPHK-HDIITLLGVGGHWVT 260
Cdd:cd05285 209 THTVNVRTEDTPeSAEKIAELLGGKGPDVVIECtGA-------ESCIQTAIYATRpGGTVVLVGMGKPEVT 272
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
63-224 2.15e-08

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: 54.92  E-value: 2.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   63 GREIAGIVLDVGSKVSFFQPDDEVVGILPLD--------SEDPGLC---------------EVVRVH--EHYLVHKPEKV 117
Cdd:cd08260  59 GHEFAGVVVEVGEDVSRWRVGDRVTVPFVLGcgtcpycrAGDSNVCehqvqpgfthpgsfaEYVAVPraDVNLVRLPDDV 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  118 TWTEAAGSirdGVRAYTALHYLSH---LSPGKSVLIMdGASAFGTIAIQLAHHRGAKVISTACSlEDKqcLERFRPPIA- 193
Cdd:cd08260 139 DFVTAAGL---GCRFATAFRALVHqarVKPGEWVAVH-GCGGVGLSAVMIASALGARVIAVDID-DDK--LELARELGAv 211
                       170       180       190
                ....*....|....*....|....*....|.
gi 4545075  194 RVIDvSNGKVHVAESCLEETGGlGVDIVLDA 224
Cdd:cd08260 212 ATVN-ASEVEDVAAAVRDLTGG-GAHVSVDA 240
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
62-225 7.09e-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: 53.43  E-value: 7.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   62 VGREIAGIVLDVGSKVSFFQPDDEVV--------------------------GILPLDSEDPGLCEVVRVHE--HYLVHK 113
Cdd:cd05278  58 LGHEFVGEVVEVGSDVKRLKPGDRVSvpcitfcgrcrfcrrgyhahcenglwGWKLGNRIDGGQAEYVRVPYadMNLAKI 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  114 PEKVTwTEAAGSIRDGVRayTALH--YLSHLSPGKSVLIMdGASAFGTIAIQLAHHRGAKVIsTACSLeDKQCLE--RFR 189
Cdd:cd05278 138 PDGLP-DEDALMLSDILP--TGFHgaELAGIKPGSTVAVI-GAGPVGLCAVAGARLLGAARI-IAVDS-NPERLDlaKEA 211
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4545075  190 PPiARVIDVSNGkvHVAESCLEETGGLGVDIVLDAG 225
Cdd:cd05278 212 GA-TDIINPKNG--DIVEQILELTGGRGVDCVIEAV 244
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
54-188 7.46e-08

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 53.50  E-value: 7.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    54 KMKKDLFPvGREIAGIVLDVGSKVSFFQPDDEVVGILpldSEDPGLCEVVRVHEHY------------------------ 109
Cdd:PRK13771  51 RMKYPVIL-GHEVVGTVEEVGENVKGFKPGDRVASLL---YAPDGTCEYCRSGEEAycknrlgygeeldgffaeyakvkv 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   110 --LVHKPEKVTwTEAA-------GSIRDGVRaytalhyLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSLE 180
Cdd:PRK13771 127 tsLVKVPPNVS-DEGAvivpcvtGMVYRGLR-------RAGVKKGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSSES 198

                 ....*...
gi 4545075   181 DKQCLERF 188
Cdd:PRK13771 199 KAKIVSKY 206
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
60-182 9.75e-08

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: 53.03  E-value: 9.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   60 FPVGREIAGIVLDVGSKVSFFQPDDEVVGILPldsedPGLCEVVRVHEHYLVHKPEKVTwtEAAGSIRDGVRAYTALHYL 139
Cdd:cd08250  62 FDCGFEGVGEVVAVGEGVTDFKVGDAVATMSF-----GAFAEYQVVPARHAVPVPELKP--EVLPLLVSGLTASIALEEV 134
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 4545075  140 SHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTaCSLEDK 182
Cdd:cd08250 135 GEMKSGETVLVTAAAGGTGQFAVQLAKLAGCHVIGT-CSSDEK 176
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
23-224 1.68e-07

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: 52.37  E-value: 1.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   23 EDLPVTE--DNFVKLQVKACAL--SQINTkllaemkMKKDL-FP----VGREIAGIVLDVGSKV---SFFQPDDEVVG-- 88
Cdd:cd08263  16 EEIPVPRpkEGEILIRVAACGVchSDLHV-------LKGELpFPppfvLGHEISGEVVEVGPNVenpYGLSVGDRVVGsf 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   89 ILP----------------------------LDSE--------DP-------GLCEVVRVHEHYLVHKPEKVTWTEAAGS 125
Cdd:cd08263  89 IMPcgkcrycargkenlcedffaynrlkgtlYDGTtrlfrldgGPvymysmgGLAEYAVVPATALAPLPESLDYTESAVL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  126 IRDGVRAYTALHYLSHLSPGKSVLIMdGASAFGTIAIQLAHHRGAKVISTACSLEDKqcLERFRPPIARVIdVSNGKVHV 205
Cdd:cd08263 169 GCAGFTAYGALKHAADVRPGETVAVI-GVGGVGSSAIQLAKAFGASPIIAVDVRDEK--LAKAKELGATHT-VNAAKEDA 244
                       250
                ....*....|....*....
gi 4545075  206 AESCLEETGGLGVDIVLDA 224
Cdd:cd08263 245 VAAIREITGGRGVDVVVEA 263
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
17-223 3.34e-07

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: 51.22  E-value: 3.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   17 FVFQEKEDlPVTEDNFVKLQVKACALSQINTKLLAemkMKKDLFPVGREIAGIVLDVGSKVSFFQPDDEVVGILPLDsed 96
Cdd:cd08270  14 LRLGEVPD-PQPAPHEALVRVAAISLNRGELKFAA---ERPDGAVPGWDAAGVVERAAADGSGPAVGARVVGLGAMG--- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   97 pGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSpGKSVLIMDGASAFGTIAIQLAHHRGAKVISTA 176
Cdd:cd08270  87 -AWAELVAVPTGWLAVLPDGVSFAQAATLPVAGVTALRALRRGGPLL-GRRVLVTGASGGVGRFAVQLAALAGAHVVAVV 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 4545075  177 CSLEDKQCLERFrppiarvidvsnGKVHVAESCLEETGGlGVDIVLD 223
Cdd:cd08270 165 GSPARAEGLREL------------GAAEVVVGGSELSGA-PVDLVVD 198
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
62-175 4.49e-07

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: 50.96  E-value: 4.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   62 VGREIAGIVLDVGSKVSFFQPDDEV-VG-----------------------ILPLDSEDP-------GLCEVVRVHEHYL 110
Cdd:cd05283  57 PGHEIVGIVVAVGSKVTKFKVGDRVgVGcqvdscgtceqcksgeeqycpkgVVTYNGKYPdgtitqgGYADHIVVDERFV 136
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4545075  111 VHKPEKVTWTEAA----GsirdGVRAYTALHYLsHLSPGKSVLIMdGASAFGTIAIQLAHHRGAKV--IST 175
Cdd:cd05283 137 FKIPEGLDSAAAApllcA----GITVYSPLKRN-GVGPGKRVGVV-GIGGLGHLAVKFAKALGAEVtaFSR 201
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
158-224 9.90e-07

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 47.22  E-value: 9.90e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4545075    158 GTIAIQLAHHRGAKVIsTACSLEDKqcLErfrppIAR------VIDVSNgkVHVAESCLEETGGLGVDIVLDA 224
Cdd:pfam00107   3 GLAAIQLAKAAGAKVI-AVDGSEEK--LE-----LAKelgadhVINPKE--TDLVEEIKELTGGKGVDVVFDC 65
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
63-222 1.13e-06

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


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 49.53  E-value: 1.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   63 GREIAGIVLDVGSKVSFFQPDDEVVgilPLDsedPGL---CEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYL 139
Cdd:cd08290  68 GNEGVGEVVKVGSGVKSLKPGDWVI---PLR---PGLgtwRTHAVVPADDLIKVPNDVDPEQAATLSVNPCTAYRLLEDF 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  140 SHLSPGKSVlIMDGA-SAFGTIAIQLAHHRGAKVISTAcsledkqcleRFRPPIARVIdvsngkvhvaesclEETGGLGV 218
Cdd:cd08290 142 VKLQPGDWV-IQNGAnSAVGQAVIQLAKLLGIKTINVV----------RDRPDLEELK--------------ERLKALGA 196

                ....
gi 4545075  219 DIVL 222
Cdd:cd08290 197 DHVL 200
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
1-224 2.98e-06

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: 48.29  E-value: 2.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    1 MKGLYFQQSStDEEITFVfqekeDLPVTEDNFVKLQVKACALSQINTKLLAEMKMKKdlFPV--GREIAGIVLDVGSKVS 78
Cdd:cd08234   1 MKALVYEGPG-ELEVEEV-----PVPEPGPDEVLIKVAACGICGTDLHIYEGEFGAA--PPLvpGHEFAGVVVAVGSKVT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   79 FFQPDDEVVGilpldseDPG---------------LC---------------EVVRVHEHYLVHKPEKVTWTEAA----G 124
Cdd:cd08234  73 GFKVGDRVAV-------DPNiycgecfycrrgrpnLCenltavgvtrnggfaEYVVVPAKQVYKIPDNLSFEEAAlaepL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  125 SirdgvrayTALHYLSHLS--PGKSVLIMdGASAFGTIAIQLAHHRGAKVISTACSLEDKqcLErfrppIAR------VI 196
Cdd:cd08234 146 S--------CAVHGLDLLGikPGDSVLVF-GAGPIGLLLAQLLKLNGASRVTVAEPNEEK--LE-----LAKklgateTV 209
                       250       260
                ....*....|....*....|....*...
gi 4545075  197 DVSNGKVHVAesclEETGGLGVDIVLDA 224
Cdd:cd08234 210 DPSREDPEAQ----KEDNPYGFDVVIEA 233
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
132-223 4.66e-06

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: 47.68  E-value: 4.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  132 AY-TALHYL--SHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVIstACSLEDKQclERFRPPIA-RVIDVSNGKVHVAe 207
Cdd:cd08274 162 SYsTAENMLerAGVGAGETVLVTGASGGVGSALVQLAKRRGAIVI--AVAGAAKE--EAVRALGAdTVILRDAPLLADA- 236
                        90
                ....*....|....*.
gi 4545075  208 sclEETGGLGVDIVLD 223
Cdd:cd08274 237 ---KALGGEPVDVVAD 249
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
21-224 8.25e-06

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: 46.97  E-value: 8.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   21 EKEDLPVTEDNFVKLQVKACA-----LSQINTKLLAEMKMKKDLFPvGREIAGIVLDVGSKVSFFQPDDEVVGIlpldsE 95
Cdd:cd08269  10 EEHPRPTPGPGQVLVRVEGCGvcgsdLPAFNQGRPWFVYPAEPGGP-GHEGWGRVVALGPGVRGLAVGDRVAGL-----S 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   96 DPGLCEVVRVHEHYLVHKPEKVT----WTEAAGSIRDGVRaytalhyLSHLSPGKSVLIMdGASAFGTIAIQLAHHRGAK 171
Cdd:cd08269  84 GGAFAEYDLADADHAVPLPSLLDgqafPGEPLGCALNVFR-------RGWIRAGKTVAVI-GAGFIGLLFLQLAAAAGAR 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4545075  172 VIsTACSLEDkqclerFRPPIARVID----VSNGKVHVAESCLEETGGLGVDIVLDA 224
Cdd:cd08269 156 RV-IAIDRRP------ARLALARELGatevVTDDSEAIVERVRELTGGAGADVVIEA 205
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
63-222 2.68e-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: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 45.60  E-value: 2.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075   63 GREIAGIVLDVGSKVSFFQPDDEVvGILPLDS----------EDPGLC---------------EVVRVHEHYLVHKPEKV 117
Cdd:cd08297  61 GHEGAGVVVAVGPGVSGLKVGDRV-GVKWLYDacgkceycrtGDETLCpnqknsgytvdgtfaEYAIADARYVTPIPDGL 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075  118 TWTEAAGSIRDGVRAYTALHyLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKV--ISTAcslEDKQ--CLERfrpPIA 193
Cdd:cd08297 140 SFEQAAPLLCAGVTVYKALK-KAGLKPGDWVVISGAGGGLGHLGVQYAKAMGLRViaIDVG---DEKLelAKEL---GAD 212
                       170       180
                ....*....|....*....|....*....
gi 4545075  194 RVIDVSngKVHVAESCLEETGGLGVDIVL 222
Cdd:cd08297 213 AFVDFK--KSDDVEAVKELTGGGGAHAVV 239
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
129-173 1.28e-04

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: 43.24  E-value: 1.28e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 4545075  129 GVRAYTALHYLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVI 173
Cdd:cd05288 130 GLTAYFGLTEIGKPKPGETVVVSAAAGAVGSVVGQIAKLLGARVV 174
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
96-239 1.41e-04

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 43.10  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4545075    96 DPGLCEVVRVHEHYLVHKPEKVTwTEAAGSIR-DGVRAYTALHyLSHLSPGKSVLIMdGASAFGTIAIQLAHHR-GAKVI 173
Cdd:PRK09422 115 DGGMAEQCIVTADYAVKVPEGLD-PAQASSITcAGVTTYKAIK-VSGIKPGQWIAIY-GAGGLGNLALQYAKNVfNAKVI 191
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4545075   174 stacsledkqclerfrppiarVIDVSNGKVHVAEScleetggLGVDIVLDagvrlySKDDEPAVKL 239
Cdd:PRK09422 192 ---------------------AVDINDDKLALAKE-------VGADLTIN------SKRVEDVAKI 223
 
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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