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Conserved domains on  [gi|6319257|ref|NP_009340|]
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putative dehydrogenase BDH2 [Saccharomyces cerevisiae S288C]

Protein Classification

2,3-butanediol dehydrogenase( domain architecture ID 10169507)

2,3-butanediol dehydrogenase is a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 1-375 0e+00

(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: 529.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFTNHLKEPhiVAPDELVIDIEWCGICGTDLHEYTDGPIFFPEDGHTHeISHNPLPQAMGHEMAGTVL 80
Cdd:cd08233   1 MKAARYHGRKDIRVEEVPEPP--VKPGEVKIKVAWCGICGSDLHEYLDGPIFIPTEGHPH-LTGETAPVTLGHEFSGVVV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVEPTGTCrdryrwplspnvdkEWCAACKKGYYNICSYLGLCGAGVQSGGFAERVVMNESHCYKV 160
Cdd:cd08233  78 EVGSGVTGFKVGDRVVVEPTIKC--------------GTCGACKRGLYNLCDSLGFIGLGGGGGGFAEYVVVPAYHVHKL 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  161 PDFVPLDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA-RVYD 239
Cdd:cd08233 144 PDNVPLEEAALVEPLAVAWHAVRRSGFKPGDTALVLGAGPIGLLTILALKAAGASKIIVSEPSEARRELAEELGAtIVLD 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  240 PTAHAAkesIDYLRSIADGGdGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGhHKIQFSPMDITLHERKYTGSMCY 319
Cdd:cd08233 224 PTEVDV---VAEVRKLTGGG-GVDVSFDCAGVQATLDTAIDALRPRGTAVNVAIWE-KPISFNPNDLVLKEKTLTGSICY 298

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6319257  320 THHDFEAVIEALEEGRIDidrARHMITGRVNIEDGLDGAIMKLINEKESTIKIILT 375
Cdd:cd08233 299 TREDFEEVIDLLASGKID---AEPLITSRIPLEDIVEKGFEELINDKEQHVKILVS 351
 
Name Accession Description Interval E-value
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 1-375 0e+00

(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: 529.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFTNHLKEPhiVAPDELVIDIEWCGICGTDLHEYTDGPIFFPEDGHTHeISHNPLPQAMGHEMAGTVL 80
Cdd:cd08233   1 MKAARYHGRKDIRVEEVPEPP--VKPGEVKIKVAWCGICGSDLHEYLDGPIFIPTEGHPH-LTGETAPVTLGHEFSGVVV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVEPTGTCrdryrwplspnvdkEWCAACKKGYYNICSYLGLCGAGVQSGGFAERVVMNESHCYKV 160
Cdd:cd08233  78 EVGSGVTGFKVGDRVVVEPTIKC--------------GTCGACKRGLYNLCDSLGFIGLGGGGGGFAEYVVVPAYHVHKL 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  161 PDFVPLDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA-RVYD 239
Cdd:cd08233 144 PDNVPLEEAALVEPLAVAWHAVRRSGFKPGDTALVLGAGPIGLLTILALKAAGASKIIVSEPSEARRELAEELGAtIVLD 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  240 PTAHAAkesIDYLRSIADGGdGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGhHKIQFSPMDITLHERKYTGSMCY 319
Cdd:cd08233 224 PTEVDV---VAEVRKLTGGG-GVDVSFDCAGVQATLDTAIDALRPRGTAVNVAIWE-KPISFNPNDLVLKEKTLTGSICY 298

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6319257  320 THHDFEAVIEALEEGRIDidrARHMITGRVNIEDGLDGAIMKLINEKESTIKIILT 375
Cdd:cd08233 299 TREDFEEVIDLLASGKID---AEPLITSRIPLEDIVEKGFEELINDKEQHVKILVS 351
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 1-377 3.52e-110

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: 327.48  E-value: 3.52e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFTNhLKEPHIvAPDELVIDIEWCGICGTDLHEYTDGPIFFPEdghtheishnplPQAMGHEMAGTVL 80
Cdd:COG1063   1 MKALVLHGPGDLRLEE-VPDPEP-GPGEVLVRVTAVGICGSDLHIYRGGYPFVRP------------PLVLGHEFVGEVV 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVEPTGTCRDryrwplspnvdkewCAACKKGYYNICSYLGLCGAGVQSGGFAERVVMNESHCYKV 160
Cdd:COG1063  67 EVGEGVTGLKVGDRVVVEPNIPCGE--------------CRYCRRGRYNLCENLQFLGIAGRDGGFAEYVRVPAANLVKV 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  161 PDFVPLDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA-RVYD 239
Cdd:COG1063 133 PDGLSDEAAALVEPLAVALHAVERAGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARELGAdAVVN 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  240 PTAHAAKESIDYLrsiaDGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGhHKIQFSPMDITLHERKYTGSMCY 319
Cdd:COG1063 213 PREEDLVEAVREL----TGGRGADVVIEAVGAPAALEQALDLVRPGGTVVLVGVPG-GPVPIDLNALVRKELTLRGSRNY 287

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6319257  320 THHDFEAVIEALEEGRIDIDRarhMITGRVNIEDGLDgAIMKLINEKESTIKIILTPN 377
Cdd:COG1063 288 TREDFPEALELLASGRIDLEP---LITHRFPLDDAPE-AFEAAADRADGAIKVVLDPD 341
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 16-348 7.02e-38

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 140.68  E-value: 7.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    16 NHLK-EPHI---VAPDELVIDIEWCGICGTDLHEYtdgpiffpedgHTHEISHNPL--PQAMGHEMAGTVLEVGPGVKNL 89
Cdd:PLN02702  27 NTLKiQPFKlppLGPHDVRVRMKAVGICGSDVHYL-----------KTMRCADFVVkePMVIGHECAGIIEEVGSEVKHL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    90 KVGDKVVVEPTGTCRDryrwplspnvdkewCAACKKGYYNICSYLGLCGAGVQSGGFAERVVMNESHCYKVPDFVPLDVA 169
Cdd:PLN02702  96 VVGDRVALEPGISCWR--------------CNLCKEGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   170 ALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGArvyDPTAHAAKESI 249
Cdd:PLN02702 162 AMCEPLSVGVHACRRANIGPETNVLVMGAGPIGLVTMLAARAFGAPRIVIVDVDDERLSVAKQLGA---DEIVLVSTNIE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   250 DYLRSIAD----GGDGFDYTFDCSGLEVTLNAAIQClTFRGTAVNLAMWGHHKIQFSPMDITLHERKYTGSMCYtHHDFE 325
Cdd:PLN02702 239 DVESEVEEiqkaMGGGIDVSFDCVGFNKTMSTALEA-TRAGGKVCLVGMGHNEMTVPLTPAAAREVDVVGVFRY-RNTWP 316

                        330       340
                 ....*....|....*....|...
gi 6319257   326 AVIEALEEGRIDIdraRHMITGR 348
Cdd:PLN02702 317 LCLEFLRSGKIDV---KPLITHR 336
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 27-159 1.33e-35

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


Pssm-ID: 400513 [Multi-domain]  Cd Length: 106  Bit Score: 126.57  E-value: 1.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257     27 DELVIDIEWCGICGTDLHEYTDGPIffpedghtheisHNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTGTCRDr 106
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNP------------PVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGK- 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 6319257    107 yrwplspnvdkewCAACKKGYYNICSYLGLCGAGVQsGGFAERVVMNESHCYK 159
Cdd:pfam08240  68 -------------CEYCREGRYNLCPNGRFLGYDRD-GGFAEYVVVPERNLVP 106
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 66-348 4.27e-13

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 69.34  E-value: 4.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257      66 PLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVveptgtcrdryrwplspnvdkewcaackkgyynicsylglcgaGVQSGG 145
Cdd:smart00829  21 PGEAVLGGECAGVVTRVGPGVTGLAVGDRVM-------------------------------------------GLAPGA 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257     146 FAERVVMNESHCYKVPDFVPLDVAALIqPLAVC--WHAIR-VCEFKAGSTALI-IGAGPIGLGTI-LALnAAGCKDIV-V 219
Cdd:smart00829  58 FATRVVTDARLVVPIPDGWSFEEAATV-PVVFLtaYYALVdLARLRPGESVLIhAAAGGVGQAAIqLAR-HLGAEVFAtA 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257     220 SEPAKvrRELAEKMG---ARVYDPTahaakeSIDYLRSI--ADGGDGFDYTFDC-SGlEvTLNAAIQCLTFRGTAVNLA- 292
Cdd:smart00829 136 GSPEK--RDFLRALGipdDHIFSSR------DLSFADEIlrATGGRGVDVVLNSlSG-E-FLDASLRCLAPGGRFVEIGk 205

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319257     293 --MWGHHKIqfsPMDITLHERKYTG----SMCyTHHD-----FEAVIEALEEGRI--------DIDRA----RHMITGR 348
Cdd:smart00829 206 rdIRDNSQL---AMAPFRPNVSYHAvdldALE-EGPDrirelLAEVLELFAEGVLrplpvtvfPISDAedafRYMQQGK 280
 
Name Accession Description Interval E-value
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 1-375 0e+00

(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: 529.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFTNHLKEPhiVAPDELVIDIEWCGICGTDLHEYTDGPIFFPEDGHTHeISHNPLPQAMGHEMAGTVL 80
Cdd:cd08233   1 MKAARYHGRKDIRVEEVPEPP--VKPGEVKIKVAWCGICGSDLHEYLDGPIFIPTEGHPH-LTGETAPVTLGHEFSGVVV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVEPTGTCrdryrwplspnvdkEWCAACKKGYYNICSYLGLCGAGVQSGGFAERVVMNESHCYKV 160
Cdd:cd08233  78 EVGSGVTGFKVGDRVVVEPTIKC--------------GTCGACKRGLYNLCDSLGFIGLGGGGGGFAEYVVVPAYHVHKL 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  161 PDFVPLDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA-RVYD 239
Cdd:cd08233 144 PDNVPLEEAALVEPLAVAWHAVRRSGFKPGDTALVLGAGPIGLLTILALKAAGASKIIVSEPSEARRELAEELGAtIVLD 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  240 PTAHAAkesIDYLRSIADGGdGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGhHKIQFSPMDITLHERKYTGSMCY 319
Cdd:cd08233 224 PTEVDV---VAEVRKLTGGG-GVDVSFDCAGVQATLDTAIDALRPRGTAVNVAIWE-KPISFNPNDLVLKEKTLTGSICY 298

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6319257  320 THHDFEAVIEALEEGRIDidrARHMITGRVNIEDGLDGAIMKLINEKESTIKIILT 375
Cdd:cd08233 299 TREDFEEVIDLLASGKID---AEPLITSRIPLEDIVEKGFEELINDKEQHVKILVS 351
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 1-377 3.52e-110

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: 327.48  E-value: 3.52e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFTNhLKEPHIvAPDELVIDIEWCGICGTDLHEYTDGPIFFPEdghtheishnplPQAMGHEMAGTVL 80
Cdd:COG1063   1 MKALVLHGPGDLRLEE-VPDPEP-GPGEVLVRVTAVGICGSDLHIYRGGYPFVRP------------PLVLGHEFVGEVV 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVEPTGTCRDryrwplspnvdkewCAACKKGYYNICSYLGLCGAGVQSGGFAERVVMNESHCYKV 160
Cdd:COG1063  67 EVGEGVTGLKVGDRVVVEPNIPCGE--------------CRYCRRGRYNLCENLQFLGIAGRDGGFAEYVRVPAANLVKV 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  161 PDFVPLDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA-RVYD 239
Cdd:COG1063 133 PDGLSDEAAALVEPLAVALHAVERAGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARELGAdAVVN 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  240 PTAHAAKESIDYLrsiaDGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGhHKIQFSPMDITLHERKYTGSMCY 319
Cdd:COG1063 213 PREEDLVEAVREL----TGGRGADVVIEAVGAPAALEQALDLVRPGGTVVLVGVPG-GPVPIDLNALVRKELTLRGSRNY 287

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6319257  320 THHDFEAVIEALEEGRIDIDRarhMITGRVNIEDGLDgAIMKLINEKESTIKIILTPN 377
Cdd:COG1063 288 TREDFPEALELLASGRIDLEP---LITHRFPLDDAPE-AFEAAADRADGAIKVVLDPD 341
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 1-374 5.22e-81

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: 252.92  E-value: 5.22e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFTNhLKEPhIVAPDELVIDIEWCGICGTDLHEYtdgpiffpeDGHTheiSHNPlPQAMGHEMAGTVL 80
Cdd:cd08236   1 MKALVLTGPGDLRYED-IPKP-EPGPGEVLVKVKACGICGSDIPRY---------LGTG---AYHP-PLVLGHEFSGTVE 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVEPTGTCRDryrwplspnvdkewCAACKKGYYNICSYLGLCGAgVQSGGFAERVVMNESHCYKV 160
Cdd:cd08236  66 EVGSGVDDLAVGDRVAVNPLLPCGK--------------CEYCKKGEYSLCSNYDYIGS-RRDGAFAEYVSVPARNLIKI 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  161 PDFVPLDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA-RVYD 239
Cdd:cd08236 131 PDHVDYEEAAMIEPAAVALHAVRLAGITLGDTVVVIGAGTIGLLAIQWLKILGAKRVIAVDIDDEKLAVARELGAdDTIN 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  240 PTAHAAKESIDYlrsiaDGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAV--NLAMWGHHKIQFSPMDITLHERKYTGSM 317
Cdd:cd08236 211 PKEEDVEKVREL-----TEGRGADLVIEAAGSPATIEQALALARPGGKVVlvGIPYGDVTLSEEAFEKILRKELTIQGSW 285

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319257  318 CYT-----HHDFEAVIEALEEGRIDIDRarhMITGRVNIEDGlDGAIMKLINEKESTIKIIL 374
Cdd:cd08236 286 NSYsapfpGDEWRTALDLLASGKIKVEP---LITHRLPLEDG-PAAFERLADREEFSGKVLL 343
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 3-373 4.56e-76

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: 240.09  E-value: 4.56e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    3 ALAYFGKGNIRFTNhlKEPHIVAPDELVIDIEWCGICGTDLHEYTDGPI--FFPEDghtheishnplPQAMGHEMAGTVL 80
Cdd:cd05285   1 AAVLHGPGDLRLEE--RPIPEPGPGEVLVRVRAVGICGSDVHYYKHGRIgdFVVKE-----------PMVLGHESAGTVV 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVEPTGTCRDryrwplspnvdkewCAACKKGYYNICSYLGLCG-AGVQsGGFAERVVMNESHCYK 159
Cdd:cd05285  68 AVGSGVTHLKVGDRVAIEPGVPCRT--------------CEFCKSGRYNLCPDMRFAAtPPVD-GTLCRYVNHPADFCHK 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  160 VPDFVPLDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA-RVY 238
Cdd:cd05285 133 LPDNVSLEEGALVEPLSVGVHACRRAGVRPGDTVLVFGAGPIGLLTAAVAKAFGATKVVVTDIDPSRLEFAKELGAtHTV 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  239 DPTAHAAKESIDYLRSIAdGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMwGHHKIQFSPMDITLHERKYTGSMC 318
Cdd:cd05285 213 NVRTEDTPESAEKIAELL-GGKGPDVVIECTGAESCIQTAIYATRPGGTVVLVGM-GKPEVTLPLSAASLREIDIRGVFR 290

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6319257  319 YtHHDFEAVIEALEEGRIDIDRarhMITGRVNIEDGLDgAIMKLINEKESTIKII 373
Cdd:cd05285 291 Y-ANTYPTAIELLASGKVDVKP---LITHRFPLEDAVE-AFETAAKGKKGVIKVV 340
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 1-373 9.25e-76

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: 238.97  E-value: 9.25e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFTNhLKEPHIvAPDELVIDIEWCGICGTDLHEYtdgpiffpedgHTHEISHNPLPqaMGHEMAGTVL 80
Cdd:cd08234   1 MKALVYEGPGELEVEE-VPVPEP-GPDEVLIKVAACGICGTDLHIY-----------EGEFGAAPPLV--PGHEFAGVVV 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVEPTGTCRDryrwplspnvdkewCAACKKGYYNICSYLGLCGAGVqSGGFAERVVMNESHCYKV 160
Cdd:cd08234  66 AVGSKVTGFKVGDRVAVDPNIYCGE--------------CFYCRRGRPNLCENLTAVGVTR-NGGFAEYVVVPAKQVYKI 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  161 PDFVPLDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA-RVYD 239
Cdd:cd08234 131 PDNLSFEEAALAEPLSCAVHGLDLLGIKPGDSVLVFGAGPIGLLLAQLLKLNGASRVTVAEPNEEKLELAKKLGAtETVD 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  240 PTahaakeSIDYLRSIADGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVnlaMWG----HHKIQFSPMDITLHERKYTG 315
Cdd:cd08234 211 PS------REDPEAQKEDNPYGFDVVIEATGVPKTLEQAIEYARRGGTVL---VFGvyapDARVSISPFEIFQKELTIIG 281

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6319257  316 SMCYTHHdFEAVIEALEEGRIDIDRarhMITGRVNIE---DGLDGAimklinEKESTIKII 373
Cdd:cd08234 282 SFINPYT-FPRAIALLESGKIDVKG---LVSHRLPLEevpEALEGM------RSGGALKVV 332
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 28-331 7.64e-72

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: 226.82  E-value: 7.64e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   28 ELVIDIEWCGICGTDLHEYTDGPIFFPedghtheishnPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTGTCRDry 107
Cdd:cd05188   1 EVLVRVEAAGLCGTDLHIRRGGYPPPP-----------KLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNLGCGT-- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  108 rwplspnvdkewCAACKKGyyniCSYLGLCGAGVQsGGFAERVVMNESHCYKVPDFVPLDVAALI-QPLAVCWHAI-RVC 185
Cdd:cd05188  68 ------------CELCREL----CPGGGILGEGLD-GGFAEYVVVPADNLVPLPDGLSLEEAALLpEPLATAYHALrRAG 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  186 EFKAGSTALIIGAGPIGLGTILALNAAGCKdIVVSEPAKVRRELAEKMGA-RVYDPTAHAAKESIdylrsIADGGDGFDY 264
Cdd:cd05188 131 VLKPGDTVLVLGAGGVGLLAAQLAKAAGAR-VIVTDRSDEKLELAKELGAdHVIDYKEEDLEEEL-----RLTGGGGADV 204

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6319257  265 TFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGHHKIQFSPMDITLHERKYTGSMCYTHHDFEAVIEAL 331
Cdd:cd05188 205 VIDAVGGPETLAQALRLLRPGGRIVVVGGTSGGPPLDDLRRLLFKELTIIGSTGGTREDFEEALDLL 271
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 18-375 6.38e-68

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: 218.60  E-value: 6.38e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   18 LKEPHIvAPDELVIDIEWCGICGTDLHEYTdgpiffpedghtheiSHNPL---PQAMGHEMAGTVLEVGPGVKNLKVGDK 94
Cdd:cd08261  17 IPEPVP-GAGEVLVRVKRVGICGSDLHIYH---------------GRNPFasyPRILGHELSGEVVEVGEGVAGLKVGDR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   95 VVVEPTGTCRDryrwplspnvdkewCAACKKGYYNICSYLGLcgAGVQS-GGFAERVVMNESHcYKVPDFVPLDVAALIQ 173
Cdd:cd08261  81 VVVDPYISCGE--------------CYACRKGRPNCCENLQV--LGVHRdGGFAEYIVVPADA-LLVPEGLSLDQAALVE 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  174 PLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKdIVVSEPAKVRRELAEKMGArvyDPTAHAAKE-SIDYL 252
Cdd:cd08261 144 PLAIGAHAVRRAGVTAGDTVLVVGAGPIGLGVIQVAKARGAR-VIVVDIDDERLEFARELGA---DDTINVGDEdVAARL 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  253 RSIADgGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGHHkIQFSpmDITLHERKYT--GSMCYTHHDFEAVIEA 330
Cdd:cd08261 220 RELTD-GEGADVVIDATGNPASMEEAVELVAHGGRVVLVGLSKGP-VTFP--DPEFHKKELTilGSRNATREDFPDVIDL 295

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 6319257  331 LEEGRIDIDRarhMITGRVNIEDGLDgAIMKLINEKESTIKIILT 375
Cdd:cd08261 296 LESGKVDPEA---LITHRFPFEDVPE-AFDLWEAPPGGVIKVLIE 336
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 24-339 3.19e-65

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 211.51  E-value: 3.19e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   24 VAPDELVIDIEWCGICGTDLHEYtdgpiffpeDGHTHEIshnPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTGTC 103
Cdd:COG1064  23 PGPGEVLVKVEACGVCHSDLHVA---------EGEWPVP---KLPLVPGHEIVGRVVAVGPGVTGFKVGDRVGVGWVDSC 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  104 RDryrwplspnvdkewCAACKKGYYNICSYLGLCGAGVQsGGFAERVVMNESHCYKVPDFVPLDVAAliqPLAvC----- 178
Cdd:COG1064  91 GT--------------CEYCRSGRENLCENGRFTGYTTD-GGYAEYVVVPARFLVKLPDGLDPAEAA---PLL-Cagita 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  179 WHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKvRRELAEKMGA-RVYDPTAHAAKESIDYLRsiad 257
Cdd:COG1064 152 YRALRRAGVGPGDRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPE-KLELARELGAdHVVNSSDEDPVEAVRELT---- 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  258 ggdGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMwGHHKIQFSPMDITLHERKYTGSMCYTHHDFEAVIEALEEGRID 337
Cdd:COG1064 227 ---GADVVIDTVGAPATVNAALALLRRGGRLVLVGL-PGGPIPLPPFDLILKERSIRGSLIGTRADLQEMLDLAAEGKIK 302


                ..
gi 6319257  338 ID 339
Cdd:COG1064 303 PE 304
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 25-374 4.02e-64

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. 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: 176223 [Multi-domain]  Cd Length: 341  Bit Score: 209.09  E-value: 4.02e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   25 APDELVIDIEWCGICGTDLHeYTDGPIFFPEDGHTHEISHNPLPQAMGHEMAGTVLEVGPGVKN-LKVGDKVVVEPTGTC 103
Cdd:cd08262  22 GPGQVLVKVLACGICGSDLH-ATAHPEAMVDDAGGPSLMDLGADIVLGHEFCGEVVDYGPGTERkLKVGTRVTSLPLLLC 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  104 rdryrwplspnvdkEWCAACKKGYYNicsylglcgagVQSGGFAERVVMNESHCYKVPDFVPLDVAALIQPLAVCWHAIR 183
Cdd:cd08262 101 --------------GQGASCGIGLSP-----------EAPGGYAEYMLLSEALLLRVPDGLSMEDAALTEPLAVGLHAVR 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  184 VCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA-RVYDPTAHAAKESIDYLRSIADGGDGf 262
Cdd:cd08262 156 RARLTPGEVALVIGCGPIGLAVIAALKARGVGPIVASDFSPERRALALAMGAdIVVDPAADSPFAAWAAELARAGGPKP- 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  263 DYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGhHKIQFSPMDITLHERKYTGSMCYTHHDFEAVIEALEEGRIDidrAR 342
Cdd:cd08262 235 AVIFECVGAPGLIQQIIEGAPPGGRIVVVGVCM-ESDNIEPALAIRKELTLQFSLGYTPEEFADALDALAEGKVD---VA 310

                       330       340       350
                ....*....|....*....|....*....|..
gi 6319257  343 HMITGRVNIeDGLDGAIMKLINEkESTIKIIL 374
Cdd:cd08262 311 PMVTGTVGL-DGVPDAFEALRDP-EHHCKILV 340
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 1-334 8.53e-61

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: 199.46  E-value: 8.53e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGK--GNIRFTNhLKEPHiVAPDELVIDIEWCGICGTDLHEYtdgpiffpeDGHTHEIshnPLPQAMGHEMAGT 78
Cdd:cd08258   1 MKALVKTGPgpGNVELRE-VPEPE-PGPGEVLIKVAAAGICGSDLHIY---------KGDYDPV---ETPVVLGHEFSGT 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   79 VLEVGPGVKNLKVGDKVVVEPTG-TCRDryrwplspnvdkewCAACKKGYYNICSYLGLCGAGvQSGGFAERVVMNESHC 157
Cdd:cd08258  67 IVEVGPDVEGWKVGDRVVSETTFsTCGR--------------CPYCRRGDYNLCPHRKGIGTQ-ADGGFAEYVLVPEESL 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  158 YKVPDFVPLDVAALIQPLAVCWHAI-RVCEFKAGSTALIIGAGPIGLgtilaLNAAGCK----DIVVS--EPAKVRRELA 230
Cdd:cd08258 132 HELPENLSLEAAALTEPLAVAVHAVaERSGIRPGDTVVVFGPGPIGL-----LAAQVAKlqgaTVVVVgtEKDEVRLDVA 206

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  231 EKMGARVYDptahAAKESIDYLRSIADGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGHHKIQFSPMDITLHE 310
Cdd:cd08258 207 KELGADAVN----GGEEDLAELVNEITDGDGADVVIECSGAVPALEQALELLRKGGRIVQVGIFGPLAASIDVERIIQKE 282

                       330       340
                ....*....|....*....|....
gi 6319257  311 RKYTGSMCYTHHDFEAVIEALEEG 334
Cdd:cd08258 283 LSVIGSRSSTPASWETALRLLASG 306
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 7-353 2.09e-57

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


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 191.68  E-value: 2.09e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    7 FGKGNIRFTNHLKEPHivAPDELVIDIEWCGICGTDLHEYTDGPIffpedGhTHEISHnplPQAMGHEMAGTVLEVGPGV 86
Cdd:cd08232   4 HAAGDLRVEERPAPEP--GPGEVRVRVAAGGICGSDLHYYQHGGF-----G-TVRLRE---PMVLGHEVSGVVEAVGPGV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   87 KNLKVGDKVVVEPTGTCRDryrwplspnvdkewCAACKKGYYNICSYLGLCGAG-----VQsGGFAERVVMNESHCYKVP 161
Cdd:cd08232  73 TGLAPGQRVAVNPSRPCGT--------------CDYCRAGRPNLCLNMRFLGSAmrfphVQ-GGFREYLVVDASQCVPLP 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  162 DFVPLDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGArvyDPT 241
Cdd:cd08232 138 DGLSLRRAALAEPLAVALHAVNRAGDLAGKRVLVTGAGPIGALVVAAARRAGAAEIVATDLADAPLAVARAMGA---DET 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  242 AHAAKESIDYLRsiADGGDgFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGhHKIQFSPMDITLHERKYTGSMCYtH 321
Cdd:cd08232 215 VNLARDPLAAYA--ADKGD-FDVVFEASGAPAALASALRVVRPGGTVVQVGMLG-GPVPLPLNALVAKELDLRGSFRF-D 289

                       330       340       350
                ....*....|....*....|....*....|..
gi 6319257  322 HDFEAVIEALEEGRIDIdraRHMITGRVNIED 353
Cdd:cd08232 290 DEFAEAVRLLAAGRIDV---RPLITAVFPLEE 318
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
26-365 3.34e-57

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 191.45  E-value: 3.34e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   26 PDELVIDIEWCGICGTDLHeYTDGpiFFPEdghtheishnPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTGTCRD 105
Cdd:COG1062  16 PGEVLVRIVAAGLCHSDLH-VRDG--DLPV----------PLPAVLGHEGAGVVEEVGPGVTGVAPGDHVVLSFIPSCGH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  106 ryrwplspnvdkewCAACKKGYYNIC-SYLGLCGAGVQSGG--------------------FAERVVMNESHCYKVPDFV 164
Cdd:COG1062  83 --------------CRYCASGRPALCeAGAALNGKGTLPDGtsrlssadgepvghffgqssFAEYAVVPERSVVKVDKDV 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  165 PLDVAALIQplavC---------WHAIRVcefKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA 235
Cdd:COG1062 149 PLELAALLG----CgvqtgagavLNTAKV---RPGDTVAVFGLGGVGLSAVQGARIAGASRIIAVDPVPEKLELARELGA 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  236 -RVYDPtahAAKESIDYLRSIADGgdGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGH-HKIQFSPMDITLHERKY 313
Cdd:COG1062 222 tHTVNP---ADEDAVEAVRELTGG--GVDYAFETTGNPAVIRQALEALRKGGTVVVVGLAPPgAEISLDPFQLLLTGRTI 296

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6319257  314 TGSM---CYTHHDFEAVIEALEEGRIDIDRarhMITGRVNIEDgldgaimklINE 365
Cdd:COG1062 297 RGSYfggAVPRRDIPRLVDLYRAGRLPLDE---LITRRYPLDE---------INE 339
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 26-353 1.08e-54

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


Pssm-ID: 176240 [Multi-domain]  Cd Length: 363  Bit Score: 185.05  E-value: 1.08e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   26 PDELVIDIEWCGICGTDLHeYTDGPIFFPedghtheishnpLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVE---PTGT 102
Cdd:cd08279  25 PGEVLVRIAAAGLCHSDLH-VVTGDLPAP------------LPAVLGHEGAGVVEEVGPGVTGVKPGDHVVLSwipACGT 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  103 CRdryrwplspnvdkeWCAAckkGYYNIC----SYLGLCGAGVQS---------------GGFAERVVMNESHCYKVPDF 163
Cdd:cd08279  92 CR--------------YCSR---GQPNLCdlgaGILGGQLPDGTRrftadgepvgamcglGTFAEYTVVPEASVVKIDDD 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  164 VPLDVAALIQplavC-----WHA-IRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA-R 236
Cdd:cd08279 155 IPLDRAALLG----CgvttgVGAvVNTARVRPGDTVAVIGCGGVGLNAIQGARIAGASRIIAVDPVPEKLELARRFGAtH 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  237 VYDPTAHAAKESIdylRSIADGGdGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWG-HHKIQFSPMDITLHERKYTG 315
Cdd:cd08279 231 TVNASEDDAVEAV---RDLTDGR-GADYAFEAVGRAATIRQALAMTRKGGTAVVVGMGPpGETVSLPALELFLSEKRLQG 306

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 6319257  316 SM---CYTHHDFEAVIEALEEGRIDIDRarhMITGRVNIED 353
Cdd:cd08279 307 SLygsANPRRDIPRLLDLYRAGRLKLDE---LVTRRYSLDE 344
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 1-375 2.88e-54

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: 183.57  E-value: 2.88e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFTNhLKEPhIVAPDELVIDIEWCGICGTDLHEYtdgpiffpEDGHTHEishnPLPQAMGHEMAGTVL 80
Cdd:cd08235   1 MKAAVLHGPNDVRLEE-VPVP-EPGPGEVLVKVRACGICGTDVKKI--------RGGHTDL----KPPRILGHEIAGEIV 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVEPTGTCRDryrwplspnvdkewCAACKKGYYNICSYLGLCGAGvQSGGFAERVVMNESHC--- 157
Cdd:cd08235  67 EVGDGVTGFKVGDRVFVAPHVPCGE--------------CHYCLRGNENMCPNYKKFGNL-YDGGFAEYVRVPAWAVkrg 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  158 --YKVPDFVPLDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA 235
Cdd:cd08235 132 gvLKLPDNVSFEEAALVEPLACCINAQRKAGIKPGDTVLVIGAGPIGLLHAMLAKASGARKVIVSDLNEFRLEFAKKLGA 211

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  236 rvyDPTAHAAKESI-DYLRSIADgGDGFDYTFDCSGLEVTLNAAIQCLTFRGTaVNL--AMWGHHKIQFSPMDITLHERK 312
Cdd:cd08235 212 ---DYTIDAAEEDLvEKVRELTD-GRGADVVIVATGSPEAQAQALELVRKGGR-ILFfgGLPKGSTVNIDPNLIHYREIT 286

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319257  313 YTGSMCYTHHDFEAVIEALEEGRIDIDRarhMITGRVNIEDGLDGaiMKLINEKEStIKIILT 375
Cdd:cd08235 287 ITGSYAASPEDYKEALELIASGKIDVKD---LITHRFPLEDIEEA--FELAADGKS-LKIVIT 343
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 26-376 3.44e-52

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: 177.82  E-value: 3.44e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   26 PDELVIDIEWCGICGTDLHEYTDGPIFfpedghtheisHNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTGTCRD 105
Cdd:cd08254  26 PGEVLVKVKAAGVCHSDLHILDGGVPT-----------LTKLPLTLGHEIAGTVVEVGAGVTNFKVGDRVAVPAVIPCGA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  106 ryrwplspnvdkewCAACKKGYYNICSYLGLCGAGvQSGGFAERVVMNESHCYKVPDFVPLDVAAlIQPLAVC--WHAI- 182
Cdd:cd08254  95 --------------CALCRRGRGNLCLNQGMPGLG-IDGGFAEYIVVPARALVPVPDGVPFAQAA-VATDAVLtpYHAVv 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  183 RVCEFKAGSTALIIGAGPIGLGTILALNAAGCKdIVVSEPAKVRRELAEKMGA-RVYDPtahaaKESIDYLRSIADGGDG 261
Cdd:cd08254 159 RAGEVKPGETVLVIGLGGLGLNAVQIAKAMGAA-VIAVDIKEEKLELAKELGAdEVLNS-----LDDSPKDKKAAGLGGG 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  262 FDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMwGHHKIQFSPMDITLHERKYTGSMCYTHHDFEAVIEALEEGRIDIDRA 341
Cdd:cd08254 233 FDVIFDFVGTQPTFEDAQKAVKPGGRIVVVGL-GRDKLTVDLSDLIARELRIIGSFGGTPEDLPEVLDLIAKGKLDPQVE 311

                       330       340       350
                ....*....|....*....|....*....|....*..
gi 6319257  342 RHmitgrvniedGLD--GAIMKLINEKESTIKIILTP 376
Cdd:cd08254 312 TR----------PLDeiPEVLERLHKGKVKGRVVLVP 338
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 1-376 1.01e-50

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


Pssm-ID: 176244 [Multi-domain]  Cd Length: 344  Bit Score: 174.37  E-value: 1.01e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRfTNHLKEPHIVAPDELVIDIEWCGICGTDLHEYtDGPIFFPEdghtheishnplPQAMGHEMAGTVL 80
Cdd:cd08284   1 MKAVVFKGPGDVR-VEEVPIPQIQDPTDAIVKVTAAAICGSDLHIY-RGHIPSTP------------GFVLGHEFVGEVV 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVEPTGTCRDryrwplspnvdkewCAACKKGYYNICS---YLGLCGAGVQSGGFAE--RVVMNES 155
Cdd:cd08284  67 EVGPEVRTLKVGDRVVSPFTIACGE--------------CFYCRRGQSGRCAkggLFGYAGSPNLDGAQAEyvRVPFADG 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  156 HCYKVPDFVPLDVAALI-QPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMG 234
Cdd:cd08284 133 TLLKLPDGLSDEAALLLgDILPTGYFGAKRAQVRPGDTVAVIGCGPVGLCAVLSAQVLGAARVFAVDPVPERLERAAALG 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  235 ARVYDPTAHAAKESIDYlrsiADGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGHHKIQFSPMDITLHERKYT 314
Cdd:cd08284 213 AEPINFEDAEPVERVRE----ATEGRGADVVLEAVGGAAALDLAFDLVRPGGVISSVGVHTAEEFPFPGLDAYNKNLTLR 288

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319257  315 GSMCYTHHDFEAVIEALEEGRIDIDRarhMITGRVNIEDGLDGaiMKLINEKEsTIKIILTP 376
Cdd:cd08284 289 FGRCPVRSLFPELLPLLESGRLDLEF---LIDHRMPLEEAPEA--YRLFDKRK-VLKVVLDP 344
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 1-376 2.32e-49

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: 170.53  E-value: 2.32e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFTNhLKEPHIVAPDELVIDIEWCGICGTDLHEYTDGpifFPEDGHTHEIshnplpqamGHEMAGTVL 80
Cdd:cd05278   1 MKALVYLGPGKIGLEE-VPDPKIQGPHDAIVRVTATSICGSDLHIYRGG---VPGAKHGMIL---------GHEFVGEVV 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVE---PTGTCRDryrwplspnvdkewcaaCKKGYYNICSYL--GLCGAGVQSGGFAERVVMNE- 154
Cdd:cd05278  68 EVGSDVKRLKPGDRVSVPcitFCGRCRF-----------------CRRGYHAHCENGlwGWKLGNRIDGGQAEYVRVPYa 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  155 -SHCYKVPDFVPLDVAALIQP-LAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEK 232
Cdd:cd05278 131 dMNLAKIPDGLPDEDALMLSDiLPTGFHGAELAGIKPGSTVAVIGAGPVGLCAVAGARLLGAARIIAVDSNPERLDLAKE 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  233 MGA-RVYDPTAHAAKESIDYLrsiaDGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGHHKIQFSPMDITLHER 311
Cdd:cd05278 211 AGAtDIINPKNGDIVEQILEL----TGGRGVDCVIEAVGFEETFEQAVKVVRPGGTIANVGVYGKPDPLPLLGEWFGKNL 286

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6319257  312 KYTGSMCYTHHDFEAVIEALEEGRIDIDRarhMITGRVNIEDGLDG-AIMKliNEKESTIKIILTP 376
Cdd:cd05278 287 TFKTGLVPVRARMPELLDLIEEGKIDPSK---LITHRFPLDDILKAyRLFD--NKPDGCIKVVIRP 347
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 24-353 4.43e-44

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 157.04  E-value: 4.43e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   24 VAPDELVIDIEWCGICGTDLHEYtdgpiffpeDGHTHEIshnPLPQAMGHEMAGTVLEVGPGVKN------LKVGDKVVV 97
Cdd:cd08231  23 LEPGAVLVRVRLAGVCGSDVHTV---------AGRRPRV---PLPIILGHEGVGRVVALGGGVTTdvagepLKVGDRVTW 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   98 EPTGTCRDryrwplspnvdkewCAACKKG---------YYNICSYlglCGAGVQSGGFAERVVM-NESHCYKVPDFVPLD 167
Cdd:cd08231  91 SVGAPCGR--------------CYRCLVGdptkcenrkKYGHEAS---CDDPHLSGGYAEHIYLpPGTAIVRVPDNVPDE 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  168 VAALIQ-PLAVCWHAI-RVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGAR-VYDPTAHA 244
Cdd:cd08231 154 VAAPANcALATVLAALdRAGPVGAGDTVVVQGAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAREFGADaTIDIDELP 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  245 AKESIDYLRSIAdGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWG-HHKIQFSPMDITLHERKYTGSMCYTHHD 323
Cdd:cd08231 234 DPQRRAIVRDIT-GGRGADVVIEASGHPAAVPEGLELLRRGGTYVLVGSVApAGTVPLDPERIVRKNLTIIGVHNYDPSH 312

                       330       340       350
                ....*....|....*....|....*....|
gi 6319257  324 FEAVIEALEEGRIDIDRARhMITGRVNIED 353
Cdd:cd08231 313 LYRAVRFLERTQDRFPFAE-LVTHRYPLED 341
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 25-354 1.07e-43

L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as a threonine dehydrogenase. L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Zinc-dependent ADHs are medium chain dehydrogenase/reductase type proteins (MDRs) and have a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. In addition to alcohol dehydrogenases, this group includes quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176201 [Multi-domain]  Cd Length: 339  Bit Score: 155.56  E-value: 1.07e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   25 APDELVIDIEWCGICGTDLHEYTDGPIFFPEDGHTHeishnplpqamGHEMAGTVLEVGPGVKNLKVGDKVVVEPTGTCR 104
Cdd:cd08239  23 GPGEVLLRVKASGLCGSDLHYYYHGHRAPAYQGVIP-----------GHEPAGVVVAVGPGVTHFRVGDRVMVYHYVGCG 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  105 DryrwplspnvdkewCAACKKGYYNICSYlGLCGAGVQS-GGFAERVVMNESHCYKVPDFVPLDVAALIQ-PLAVCWHAI 182
Cdd:cd08239  92 A--------------CRNCRRGWMQLCTS-KRAAYGWNRdGGHAEYMLVPEKTLIPLPDDLSFADGALLLcGIGTAYHAL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  183 RVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGArvyDPTAHAAKESIDYLRSIAdGGDGF 262
Cdd:cd08239 157 RRVGVSGRDTVLVVGAGPVGLGALMLARALGAEDVIGVDPSPERLELAKALGA---DFVINSGQDDVQEIRELT-SGAGA 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  263 DYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGHHKIQFSPmDITLHERKYTGSMCYTHHDFEAVIEALEEGRIDIDRar 342
Cdd:cd08239 233 DVAIECSGNTAARRLALEAVRPWGRLVLVGEGGELTIEVSN-DLIRKQRTLIGSWYFSVPDMEECAEFLARHKLEVDR-- 309

                       330
                ....*....|..
gi 6319257  343 hMITGRVNIEDG 354
Cdd:cd08239 310 -LVTHRFGLDQA 320
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 21-353 3.59e-43

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenase and has the catalytic and structural zinc-binding sites characteristic of this group. 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. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176226 [Multi-domain]  Cd Length: 384  Bit Score: 155.37  E-value: 3.59e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   21 PHIVAPDELVIDIEWCGICGTDLHEY---TDGPIFFPedGHTHeishnpLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVV 97
Cdd:cd08265  46 VPNLKPDEILIRVKACGICGSDIHLYetdKDGYILYP--GLTE------FPVVIGHEFSGVVEKTGKNVKNFEKGDPVTA 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   98 EPTGTCrdryrwplspnvdkEWCAACKKGYYNICSYLGLCGAGVqSGGFAERVVMNESHCYKVPDFVPL-------DVAA 170
Cdd:cd08265 118 EEMMWC--------------GMCRACRSGSPNHCKNLKELGFSA-DGAFAEYIAVNARYAWEINELREIysedkafEAGA 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  171 LIQPLAVCWHAI--RVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA-RVYDPTAHAAKE 247
Cdd:cd08265 183 LVEPTSVAYNGLfiRGGGFRPGAYVVVYGAGPIGLAAIALAKAAGASKVIAFEISEERRNLAKEMGAdYVFNPTKMRDCL 262

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  248 SIDYLRSIAdGGDGFDYTFDCSGL-EVTLNAAIQCLTFRGTAVNLAMWGHH-KIQFSPMDItlHERKYTGSMCYT-HHDF 324
Cdd:cd08265 263 SGEKVMEVT-KGWGADIQVEAAGApPATIPQMEKSIAINGKIVYIGRAATTvPLHLEVLQV--RRAQIVGAQGHSgHGIF 339

                       330       340
                ....*....|....*....|....*....
gi 6319257  325 EAVIEALEEGRIDIDRarhMITGRVNIED 353
Cdd:cd08265 340 PSVIKLMASGKIDMTK---IITARFPLEG 365
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 26-288 2.12e-42

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


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 152.00  E-value: 2.12e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   26 PDELVIDIEWCGICGTDLH-----EYTDGPIffpedghtheishNPlPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPT 100
Cdd:cd05281  25 PGEVLIKVLAASICGTDVHiyewdEWAQSRI-------------KP-PLIFGHEFAGEVVEVGEGVTRVKVGDYVSAETH 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  101 GTCrdryrwplspnvdkEWCAACKKGYYNICSYLGLCGAGVQsGGFAERVVMNESHCYKVPDFVPLDVAALIQPLAVCWH 180
Cdd:cd05281  91 IVC--------------GKCYQCRTGNYHVCQNTKILGVDTD-GCFAEYVVVPEENLWKNDKDIPPEIASIQEPLGNAVH 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  181 AIRVCEFkAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGArvyDPTAHAAKESIDYLRSIADGGd 260
Cdd:cd05281 156 TVLAGDV-SGKSVLITGCGPIGLMAIAVAKAAGASLVIASDPNPYRLELAKKMGA---DVVINPREEDVVEVKSVTDGT- 230

                       250       260
                ....*....|....*....|....*...
gi 6319257  261 GFDYTFDCSGLEVTLNAAIQCLTFRGTA 288
Cdd:cd05281 231 GVDVVLEMSGNPKAIEQGLKALTPGGRV 258
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 1-362 3.43e-40

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: 146.17  E-value: 3.43e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFTNHLKEPHIVaPDELVIDIEWCGICGTDLHEYtDGPIffpedghtHEISHNPLPQAMGHEMAGTVL 80
Cdd:cd05284   1 MKAARLYEYGKPLRLEDVPVPEPG-PGQVLVRVGGAGVCHSDLHVI-DGVW--------GGILPYKLPFTLGHENAGWVE 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVEPTGTCRDryrwplspnvdkewCAACKKGYYNICSYLGLCGAGVQsGGFAERVVMNESHCYKV 160
Cdd:cd05284  71 EVGSGVDGLKEGDPVVVHPPWGCGT--------------CRYCRRGEENYCENARFPGIGTD-GGFAEYLLVPSRRLVKL 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  161 PDFVPLDVAAliqPLA----VCWHAIRvcefKA------GSTALIIGAGpiGLGTIL--ALNAAGCKDIVVSEPAKVRRE 228
Cdd:cd05284 136 PRGLDPVEAA---PLAdaglTAYHAVK----KAlpyldpGSTVVVIGVG--GLGHIAvqILRALTPATVIAVDRSEEALK 206

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  229 LAEKMGAR-VYDPTAHAAKEsidyLRSIAdGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGHHKIQFSPMDIT 307
Cdd:cd05284 207 LAERLGADhVLNASDDVVEE----VRELT-GGRGADAVIDFVGSDETLALAAKLLAKGGRYVIVGYGGHGRLPTSDLVPT 281

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6319257  308 lhERKYTGSMCYTHHDFEAVIEALEEGRIdidraRHMITgRVNIEDGLDgAIMKL 362
Cdd:cd05284 282 --EISVIGSLWGTRAELVEVVALAESGKV-----KVEIT-KFPLEDANE-ALDRL 327
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 26-317 6.16e-40

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


Pssm-ID: 176239 [Multi-domain]  Cd Length: 365  Bit Score: 146.10  E-value: 6.16e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   26 PDELVIDIEWCGICGTDLHeytdgpiffPEDGHTHEishnPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVveptgtcrd 105
Cdd:cd08278  27 PDEVLVRIVATGICHTDLV---------VRDGGLPT----PLPAVLGHEGAGVVEAVGSAVTGLKPGDHVV--------- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  106 ryrwpLSPNVDKEwCAACKKGYYNIC-SYLGLCGAGV----------------------QSGgFAERVVMNESHCYKVPD 162
Cdd:cd08278  85 -----LSFASCGE-CANCLSGHPAYCeNFFPLNFSGRrpdgstplslddgtpvhghffgQSS-FATYAVVHERNVVKVDK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  163 FVPLDVAAliqPL---------AVcwhaIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKM 233
Cdd:cd08278 158 DVPLELLA---PLgcgiqtgagAV----LNVLKPRPGSSIAVFGAGAVGLAAVMAAKIAGCTTIIAVDIVDSRLELAKEL 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  234 GAR-VYDPTAHAAKESIdylRSIAdgGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGHHK-IQFSPMDITLHER 311
Cdd:cd08278 231 GAThVINPKEEDLVAAI---REIT--GGGVDYALDTTGVPAVIEQAVDALAPRGTLALVGAPPPGAeVTLDVNDLLVSGK 305


                ....*.
gi 6319257  312 KYTGSM 317
Cdd:cd08278 306 TIRGVI 311
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 1-376 4.73e-39

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


Pssm-ID: 176243 [Multi-domain]  Cd Length: 386  Bit Score: 144.22  E-value: 4.73e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFTNhLKEPHIVAPDELVIDIEWCGICGTDLHEYtDGPIFFPEDGhtheishnplpQAMGHEMAGTVL 80
Cdd:cd08283   1 MKALVWHGKGDVRVEE-VPDPKIEDPTDAIVRVTATAICGSDLHLY-HGYIPGMKKG-----------DILGHEFMGVVE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVEPTGTCRDryrwplspnvdkewCAACKKGYYNIC----------SYLGLCGAGV-----QSGG 145
Cdd:cd08283  68 EVGPEVRNLKVGDRVVVPFTIACGE--------------CFYCKRGLYSQCdntnpsaemaKLYGHAGAGIfgyshLTGG 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  146 F----AE--RVVMNESHCYKVPDFVPLDVAAL---IQPLAvcWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKD 216
Cdd:cd08283 134 YaggqAEyvRVPFADVGPFKIPDDLSDEKALFlsdILPTG--YHAAELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAER 211

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  217 IVVSEPAKVRRELA-EKMGARVYDPTAHaaKESIDYLRSIAdGGDGFDYTFDCSGLE---------------------VT 274
Cdd:cd08283 212 VIAIDRVPERLEMArSHLGAETINFEEV--DDVVEALRELT-GGRGPDVCIDAVGMEahgsplhkaeqallkletdrpDA 288

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  275 LNAAIQCLTFRGTAVNLAMWGHHKIQFsPMDiTLHERKYTGSMCYTHHD--FEAVIEALEEGRIDidrARHMITGRVNIE 352
Cdd:cd08283 289 LREAIQAVRKGGTVSIIGVYGGTVNKF-PIG-AAMNKGLTLRMGQTHVQryLPRLLELIESGELD---PSFIITHRLPLE 363

                       410       420
                ....*....|....*....|....*
gi 6319257  353 DGLDGaiMKLINEKES-TIKIILTP 376
Cdd:cd08283 364 DAPEA--YKIFDKKEDgCIKVVLKP 386
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 16-348 7.02e-38

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 140.68  E-value: 7.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    16 NHLK-EPHI---VAPDELVIDIEWCGICGTDLHEYtdgpiffpedgHTHEISHNPL--PQAMGHEMAGTVLEVGPGVKNL 89
Cdd:PLN02702  27 NTLKiQPFKlppLGPHDVRVRMKAVGICGSDVHYL-----------KTMRCADFVVkePMVIGHECAGIIEEVGSEVKHL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    90 KVGDKVVVEPTGTCRDryrwplspnvdkewCAACKKGYYNICSYLGLCGAGVQSGGFAERVVMNESHCYKVPDFVPLDVA 169
Cdd:PLN02702  96 VVGDRVALEPGISCWR--------------CNLCKEGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   170 ALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGArvyDPTAHAAKESI 249
Cdd:PLN02702 162 AMCEPLSVGVHACRRANIGPETNVLVMGAGPIGLVTMLAARAFGAPRIVIVDVDDERLSVAKQLGA---DEIVLVSTNIE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   250 DYLRSIAD----GGDGFDYTFDCSGLEVTLNAAIQClTFRGTAVNLAMWGHHKIQFSPMDITLHERKYTGSMCYtHHDFE 325
Cdd:PLN02702 239 DVESEVEEiqkaMGGGIDVSFDCVGFNKTMSTALEA-TRAGGKVCLVGMGHNEMTVPLTPAAAREVDVVGVFRY-RNTWP 316

                        330       340
                 ....*....|....*....|...
gi 6319257   326 AVIEALEEGRIDIdraRHMITGR 348
Cdd:PLN02702 317 LCLEFLRSGKIDV---KPLITHR 336
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 66-374 1.23e-37

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: 137.79  E-value: 1.23e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   66 PLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVeptgtcrdryrwplspnvdkewcaackkgyynicsylglcgagvqSGG 145
Cdd:cd08255  19 PLPLPPGYSSVGRVVEVGSGVTGFKPGDRVFC---------------------------------------------FGP 53

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  146 FAERVVMNESHCYKVPDFVPLDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKV 225
Cdd:cd08255  54 HAERVVVPANLLVPLPDGLPPERAALTALAATALNGVRDAEPRLGERVAVVGLGLVGLLAAQLAKAAGAREVVGVDPDAA 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  226 RRELAEKMGarVYDPTAHAAKESIdylrsiadGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWG---------- 295
Cdd:cd08255 134 RRELAEALG--PADPVAADTADEI--------GGRGADVVIEASGSPSALETALRLLRDRGRVVLVGWYGlkplllgeef 203

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  296 HHK---IQFSPM-DITLHERKYTgsmcYTHH-DFEAVIEALEEGRIDidrarHMITGRVNIEDgLDGAIMKLINEKESTI 370
Cdd:cd08255 204 HFKrlpIRSSQVyGIGRYDRPRR----WTEArNLEEALDLLAEGRLE-----ALITHRVPFED-APEAYRLLFEDPPECL 273


                ....
gi 6319257  371 KIIL 374
Cdd:cd08255 274 KVVL 277
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 24-306 4.00e-37

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 138.03  E-value: 4.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    24 VAPDELVIDIEWCGICGTDLH-----EYTDGPIffpedghtheishnPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVE 98
Cdd:PRK05396  23 PGPNDVLIKVKKTAICGTDVHiynwdEWAQKTI--------------PVPMVVGHEFVGEVVEVGSEVTGFKVGDRVSGE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    99 PTGTCRDryrwplspnvdkewCAACKKGYYNICSY-LGLcgaGVQ-SGGFAERVVMNESHCYKVPDFVPLDVAALIQPL- 175
Cdd:PRK05396  89 GHIVCGH--------------CRNCRAGRRHLCRNtKGV---GVNrPGAFAEYLVIPAFNVWKIPDDIPDDLAAIFDPFg 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   176 -AVcwHAirVCEFK-AGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA-RVYDPtahaAKESI-DY 251
Cdd:PRK05396 152 nAV--HT--ALSFDlVGEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELARKMGAtRAVNV----AKEDLrDV 223

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6319257   252 LRSIADgGDGFDYTFDCSGLEVTLNAAIQCLTFRGtavNLAMWGhhkIQFSPMDI 306
Cdd:PRK05396 224 MAELGM-TEGFDVGLEMSGAPSAFRQMLDNMNHGG---RIAMLG---IPPGDMAI 271
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 26-356 8.10e-37

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: 137.35  E-value: 8.10e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   26 PDELVIDIEWCGICGTDLHEYTdgpiffpedGHTHEIshnPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTGTCRD 105
Cdd:cd08260  25 PDGVVVEVEACGVCRSDWHGWQ---------GHDPDV---TLPHVPGHEFAGVVVEVGEDVSRWRVGDRVTVPFVLGCGT 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  106 ryrwplspnvdkewCAACKKGYYNICSYLGLCGAGvQSGGFAERVVMNES--HCYKVPDFVPLDVAALIQ-PLAVCWHAI 182
Cdd:cd08260  93 --------------CPYCRAGDSNVCEHQVQPGFT-HPGSFAEYVAVPRAdvNLVRLPDDVDFVTAAGLGcRFATAFRAL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  183 RV-CEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVS-EPAKVrrELAEKMGA-RVYDPTahAAKESIDYLRSIADGg 259
Cdd:cd08260 158 VHqARVKPGEWVAVHGCGGVGLSAVMIASALGARVIAVDiDDDKL--ELARELGAvATVNAS--EVEDVAAAVRDLTGG- 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  260 dGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLA-MWGHHKIQFSPMD-ITLHERKYTGSMCYTHHDFEAVIEALEEGRID 337
Cdd:cd08260 233 -GAHVSVDALGIPETCRNSVASLRKRGRHVQVGlTLGEEAGVALPMDrVVARELEIVGSHGMPAHRYDAMLALIASGKLD 311

                       330
                ....*....|....*....
gi 6319257  338 IDRarhMITGRVNIEDGLD 356
Cdd:cd08260 312 PEP---LVGRTISLDEAPD 327
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 1-336 1.51e-36

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: 136.51  E-value: 1.51e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAY--FGKGNIRFTNH-LKEPhivAPDELVIDIEWCGICGTDLHEYT-DGPIFfpedghtheishNPLPQAMGHEMA 76
Cdd:cd08297   1 MKAAVVeeFGEKPYEVKDVpVPEP---GPGEVLVKLEASGVCHTDLHAALgDWPVK------------PKLPLIGGHEGA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   77 GTVLEVGPGVKNLKVGDKVVVEPT-GTCRDryrwplspnvdkewCAACKKGYYNICSYLGLCGAGVqSGGFAERVVMNES 155
Cdd:cd08297  66 GVVVAVGPGVSGLKVGDRVGVKWLyDACGK--------------CEYCRTGDETLCPNQKNSGYTV-DGTFAEYAIADAR 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  156 HCYKVPDFVPLDVAAliqPL----AVCWHAIRVCEFKAGSTALIIGAGPiGLGtILAL---NAAGCKDIVVsEPAKVRRE 228
Cdd:cd08297 131 YVTPIPDGLSFEQAA---PLlcagVTVYKALKKAGLKPGDWVVISGAGG-GLG-HLGVqyaKAMGLRVIAI-DVGDEKLE 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  229 LAEKMGARVY-DPTAH-AAKESIDylrsiADGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGHHKIQFSPMDI 306
Cdd:cd08297 205 LAKELGADAFvDFKKSdDVEAVKE-----LTGGGGAHAVVVTAVSAAAYEQALDYLRPGGTLVCVGLPPGGFIPLDPFDL 279

                       330       340       350
                ....*....|....*....|....*....|...
gi 6319257  307 TLHERKYTGSMCYTHHDfeaVIEALE---EGRI 336
Cdd:cd08297 280 VLRGITIVGSLVGTRQD---LQEALEfaaRGKV 309
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 26-350 5.28e-36

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: 134.75  E-value: 5.28e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   26 PDELVIDIEWCGICGTDLHeYTDGpiFFPedghtheisHNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVV---EPTGT 102
Cdd:cd08259  25 PGEVLIKVKAAGVCYRDLL-FWKG--FFP---------RGKYPLILGHEIVGTVEEVGEGVERFKPGDRVILyyyIPCGK 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  103 CRDryrwplspnvdkewcaaCKKGYYNICSYLGLCGAGVQsGGFAERVVMNESHCYKVPDFVPLDVAALIQ-PLAVCWHA 181
Cdd:cd08259  93 CEY-----------------CLSGEENLCRNRAEYGEEVD-GGFAEYVKVPERSLVKLPDNVSDESAALAAcVVGTAVHA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  182 IRVCEFKAGSTALIIGA-GPIGLGTILALNAAGCKDIVVSEPAKvRRELAEKMGArvyDPTAHAAKESIDylrsiADGGD 260
Cdd:cd08259 155 LKRAGVKKGDTVLVTGAgGGVGIHAIQLAKALGARVIAVTRSPE-KLKILKELGA---DYVIDGSKFSED-----VKKLG 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  261 GFDYTFDCSGLEvTLNAAIQCLTFRGTAVNLAMWGHHKIQFSPMDITLHERKYTGSMCYTHHDFEAVIEALEEGRI---- 336
Cdd:cd08259 226 GADVVIELVGSP-TIEESLRSLNKGGRLVLIGNVTPDPAPLRPGLLILKEIRIIGSISATKADVEEALKLVKEGKIkpvi 304

                       330       340
                ....*....|....*....|..
gi 6319257  337 -------DIDRA-RHMITGRVN 350
Cdd:cd08259 305 drvvsleDINEAlEDLKSGKVV 326
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
 1-374 8.56e-36

Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and structural zinc-binding sites of the zinc-dependent 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: 176218 [Multi-domain]  Cd Length: 350  Bit Score: 134.46  E-value: 8.56e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFtNHLKEPHIvAPDELVIDIEWCGICGTDLHEYTDGPIFFpedGHTHEISHNPLPQAMGHEMAGTVL 80
Cdd:cd08256   1 MRAVVCHGPQDYRL-EEVPVPRP-GPGEILVKVEACGICAGDIKCYHGAPSFW---GDENQPPYVKPPMIPGHEFVGRVV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKN--LKVGDKVVVE---PTGTCRdryrwplspnvdkewcaACKKGYYNICSYLGLcgAGVQS---GGFAERVVM 152
Cdd:cd08256  76 ELGEGAEErgVKVGDRVISEqivPCWNCR-----------------FCNRGQYWMCQKHDL--YGFQNnvnGGMAEYMRF 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  153 -NESHCYKVPDFVPLDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAE 231
Cdd:cd08256 137 pKEAIVHKVPDDIPPEDAILIEPLACALHAVDRANIKFDDVVVLAGAGPLGLGMIGAARLKNPKKLIVLDLKDERLALAR 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  232 KMGArvyDPTAHAAKEsiDYLRSIAD--GGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGhhkiQFSPMDIT-L 308
Cdd:cd08256 217 KFGA---DVVLNPPEV--DVVEKIKEltGGYGCDIYIEATGHPSAVEQGLNMIRKLGRFVEFSVFG----DPVTVDWSiI 287

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319257  309 HERK-------YTGSMCYthhdfEAVIEALEEGRIDIDrarHMITGRVNIEDGLDGaiMKLINEKESTIKIIL 374
Cdd:cd08256 288 GDRKeldvlgsHLGPYCY-----PIAIDLIASGRLPTD---GIVTHQFPLEDFEEA--FELMARGDDSIKVVL 350
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 27-159 1.33e-35

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


Pssm-ID: 400513 [Multi-domain]  Cd Length: 106  Bit Score: 126.57  E-value: 1.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257     27 DELVIDIEWCGICGTDLHEYTDGPIffpedghtheisHNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTGTCRDr 106
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNP------------PVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGK- 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 6319257    107 yrwplspnvdkewCAACKKGYYNICSYLGLCGAGVQsGGFAERVVMNESHCYK 159
Cdd:pfam08240  68 -------------CEYCREGRYNLCPNGRFLGYDRD-GGFAEYVVVPERNLVP 106
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 8-375 1.38e-35

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: 133.25  E-value: 1.38e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    8 GKGNIRFTNH-LKEPhivAPDELVIDIEWCGICGTDLHEYTDG-PIFFPEdghtheishnPLPQAMGHEMAGTVLEVGPG 85
Cdd:cd08269   3 GPGRFEVEEHpRPTP---GPGQVLVRVEGCGVCGSDLPAFNQGrPWFVYP----------AEPGGPGHEGWGRVVALGPG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   86 VKNLKVGDKVvveptgtcrdryrwplspnvdkewcaackkgyynicsylglcgAGVQSGGFAERVVMNESHCYKVPDFVP 165
Cdd:cd08269  70 VRGLAVGDRV-------------------------------------------AGLSGGAFAEYDLADADHAVPLPSLLD 106

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  166 lDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGArvyDPTAHAA 245
Cdd:cd08269 107 -GQAFPGEPLGCALNVFRRGWIRAGKTVAVIGAGFIGLLFLQLAAAAGARRVIAIDRRPARLALARELGA---TEVVTDD 182

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  246 KESI-DYLRSIaDGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTavnLAMWGHHkiQFSPMDITLHERKYTGS---MCYTH 321
Cdd:cd08269 183 SEAIvERVREL-TGGAGADVVIEAVGHQWPLDLAGELVAERGR---LVIFGYH--QDGPRPVPFQTWNWKGIdliNAVER 256

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  322 ------HDFEAVIEALEEGRIDIDrarHMITGRVNIEDgLDGAIMKLINEKESTIKIILT 375
Cdd:cd08269 257 dpriglEGMREAVKLIADGRLDLG---SLLTHEFPLEE-LGDAFEAARRRPDGFIKGVIV 312
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-356 1.75e-35

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family, including threonine dehydrogenase. 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: 176204 [Multi-domain]  Cd Length: 319  Bit Score: 133.14  E-value: 1.75e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFTNHLK-EPHivaPDELVIDIEWCGICGTDLhEYTDGpiffpedghtheisHNPLPQAMGHEMAGTV 79
Cdd:cd08242   1 MKALVLDGGLDLRVEDLPKpEPP---PGEALVRVLLAGICNTDL-EIYKG--------------YYPFPGVPGHEFVGIV 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   80 LEVGPGvkNLkVGDKVVVEPTGTCRDryrwplspnvdkewCAACKKGYYNICSY---LGLCGagvQSGGFAERVVMNESH 156
Cdd:cd08242  63 EEGPEA--EL-VGKRVVGEINIACGR--------------CEYCRRGLYTHCPNrtvLGIVD---RDGAFAEYLTLPLEN 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  157 CYKVPDFVPLDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKvRRELAEKMGAR 236
Cdd:cd08242 123 LHVVPDLVPDEQAVFAEPLAAALEILEQVPITPGDKVAVLGDGKLGLLIAQVLALTGPDVVLVGRHSE-KLALARRLGVE 201

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  237 VYDPTahaakesidylrSIADGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVnLAMWGHHKIQFSPMDITLHERKYTGS 316
Cdd:cd08242 202 TVLPD------------EAESEGGGFDVVVEATGSPSGLELALRLVRPRGTVV-LKSTYAGPASFDLTKAVVNEITLVGS 268

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 6319257  317 MCythHDFEAVIEALEEGRIDIDRarhMITGRVNIEDGLD 356
Cdd:cd08242 269 RC---GPFAPALRLLRKGLVDVDP---LITAVYPLEEALE 302
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 27-337 4.54e-35

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 132.50  E-value: 4.54e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    27 DELVIDIEWCGICGTDLHEYTDGPIffpedgHTHEISHnplPQAMGHEMAGTVLEVGPgvKNLKVGDKVVVEPTGTCRDr 106
Cdd:PRK09880  28 NGTLVQITRGGICGSDLHYYQEGKV------GNFVIKA---PMVLGHEVIGKIVHSDS--SGLKEGQTVAINPSKPCGH- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   107 yrwplspnvdkewCAACKKGYYNICSYLGLCGAG-----VQsGGFAERVVMNESHCYKVPDFVPLDVAALIQPLAVCWHA 181
Cdd:PRK09880  96 -------------CKYCLSHNENQCTTMRFFGSAmyfphVD-GGFTRYKVVDTAQCIPYPEKADEKVMAFAEPLAVAIHA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   182 IRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGArvyDPTAHAAKESIDylRSIADGGDg 261
Cdd:PRK09880 162 AHQAGDLQGKRVFVSGVGPIGCLIVAAVKTLGAAEIVCADVSPRSLSLAREMGA---DKLVNPQNDDLD--HYKAEKGY- 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6319257   262 FDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMwGHHKIQFSPMDITLHERKYTGSMCYThHDFEAVIEALEEGRID 337
Cdd:PRK09880 236 FDVSFEVSGHPSSINTCLEVTRAKGVMVQVGM-GGAPPEFPMMTLIVKEISLKGSFRFT-EEFNTAVSWLANGVIN 309
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 26-337 1.38e-34

6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the zinc-dependent alcohol dehydrogenase-like family of medium chain dehydrogenases/reductases catalyzes the conversion of 6-hydroxyhexanoate and NAD(+) to 6-oxohexanoate + NADH and H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176202 [Multi-domain]  Cd Length: 350  Bit Score: 131.20  E-value: 1.38e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   26 PDELVIDIEWCGICGTDLHEYTDGpiFFPEDGHTHEISHN--PLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTGTC 103
Cdd:cd08240  25 GTEVLVKVTACGVCHSDLHIWDGG--YDLGGGKTMSLDDRgvKLPLVLGHEIVGEVVAVGPDAADVKVGDKVLVYPWIGC 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  104 RDryrwplspnvdkewCAACKKGYYNICS---YLGlcgaGVQSGGFAERVVMNESHCYKVPDFVPLDVAAliqPLA---- 176
Cdd:cd08240 103 GE--------------CPVCLAGDENLCAkgrALG----IFQDGGYAEYVIVPHSRYLVDPGGLDPALAA---TLAcsgl 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  177 VCWHAIRvcefKAGSTA-----LIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGAR-VYDPTAHAAKESId 250
Cdd:cd08240 162 TAYSAVK----KLMPLVadepvVIIGAGGLGLMALALLKALGPANIIVVDIDEAKLEAAKAAGADvVVNGSDPDAAKRI- 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  251 ylrsIADGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGhHKIQFSPMDITLHERKYTGSMCYTHHDFEAVIEA 330
Cdd:cd08240 237 ----IKAAGGGVDAVIDFVNNSATASLAFDILAKGGKLVLVGLFG-GEATLPLPLLPLRALTIQGSYVGSLEELRELVAL 311


                ....*..
gi 6319257  331 LEEGRID 337
Cdd:cd08240 312 AKAGKLK 318
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 20-317 6.75e-33

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: 126.46  E-value: 6.75e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   20 EPHIVAPDELVIDIEWCGICGTDLHeYTDGpiffpEDGHTHEishnplPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVep 99
Cdd:cd05283  18 ERRPLGPDDVDIKITYCGVCHSDLH-TLRN-----EWGPTKY------PLVPGHEIVGIVVAVGSKVTKFKVGDRVGV-- 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  100 tGTCRDRYRwplspnvdkeWCAACKKGYYNICS-------YLGLCGAGVQsGGFAERVVMNESHCYKVPDFVPLDVAAli 172
Cdd:cd05283  84 -GCQVDSCG----------TCEQCKSGEEQYCPkgvvtynGKYPDGTITQ-GGYADHIVVDERFVFKIPEGLDSAAAA-- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  173 qPLaVC-----WHAIRVCEFKAGSTALIIGAGpiGLG--TILALNAAGCKDIVVS-EPAKvrRELAEKMGARVYDPTAHA 244
Cdd:cd05283 150 -PL-LCagitvYSPLKRNGVGPGKRVGVVGIG--GLGhlAVKFAKALGAEVTAFSrSPSK--KEDALKLGADEFIATKDP 223

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319257  245 AKesidylrsIADGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMwGHHKIQFSPMDITLHERKYTGSM 317
Cdd:cd05283 224 EA--------MKKAAGSLDLIIDTVSASHDLDPYLSLLKPGGTLVLVGA-PEEPLPVPPFPLIFGRKSVAGSL 287
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 24-375 1.05e-32

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


Pssm-ID: 176238 [Multi-domain]  Cd Length: 365  Bit Score: 126.68  E-value: 1.05e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   24 VAP---DELVIDIEWCGICGTDLHeytdgpiffpedgHTHEISHNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPT 100
Cdd:cd08277  22 VAPpkaNEVRIKMLATSVCHTDIL-------------AIEGFKATLFPVILGHEGAGIVESVGEGVTNLKPGDKVIPLFI 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  101 GTCRDryrwplspnvdkewCAACKKGYYNICSYLGLCGAGVQSGG-------------------FAERVVMNESHCYKVP 161
Cdd:cd08277  89 GQCGE--------------CSNCRSGKTNLCQKYRANESGLMPDGtsrftckgkkiyhflgtstFSQYTVVDENYVAKID 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  162 DFVPLDVAALI-----QPLAVCWHAIRVCEfkaGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGAR 236
Cdd:cd08277 155 PAAPLEHVCLLgcgfsTGYGAAWNTAKVEP---GSTVAVFGLGAVGLSAIMGAKIAGASRIIGVDINEDKFEKAKEFGAT 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  237 VYDPTAHAAKESIDYLRSIADGgdGFDYTFDCSGLEVTLNAAIQ-CLTFRGTAVNLAMWGHHKIQFSPMDITLhERKYTG 315
Cdd:cd08277 232 DFINPKDSDKPVSEVIREMTGG--GVDYSFECTGNADLMNEALEsTKLGWGVSVVVGVPPGAELSIRPFQLIL-GRTWKG 308

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319257  316 SM---CYTHHDFEAVIEALEEGRIDIDRArhmITGRVNIEDGLDGaiMKLINEKEStIKIILT 375
Cdd:cd08277 309 SFfggFKSRSDVPKLVSKYMNKKFDLDEL---ITHVLPFEEINKG--FDLMKSGEC-IRTVIT 365
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 26-375 2.26e-32

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


Pssm-ID: 176182 [Multi-domain]  Cd Length: 365  Bit Score: 125.63  E-value: 2.26e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   26 PDELVIDIEWCGICGTDLHeYTDGPIffpedghtheisHNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTGTCRD 105
Cdd:cd05279  25 AGEVRIKVVATGVCHTDLH-VIDGKL------------PTPLPVILGHEGAGIVESIGPGVTTLKPGDKVIPLFGPQCGK 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  106 ryrwplspnvdkewCAACKKGYYNICSYL-GLCGAGVQSGG-------------------FAERVVMNESHCYKVPDFVP 165
Cdd:cd05279  92 --------------CKQCLNPRPNLCSKSrGTNGRGLMSDGtsrftckgkpihhflgtstFAEYTVVSEISLAKIDPDAP 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  166 LDVAALIQplavC------WHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA-RVY 238
Cdd:cd05279 158 LEKVCLIG----CgfstgyGAAVNTAKVTPGSTCAVFGLGGVGLSVIMGCKAAGASRIIAVDINKDKFEKAKQLGAtECI 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  239 DPtAHAAKESIDYLRSIADGgdGFDYTFDCSGLEVTLNAAIQCLTFRG---TAVNLAMWGhHKIQFSPMDItLHERKYTG 315
Cdd:cd05279 234 NP-RDQDKPIVEVLTEMTDG--GVDYAFEVIGSADTLKQALDATRLGGgtsVVVGVPPSG-TEATLDPNDL-LTGRTIKG 308

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319257  316 SM---CYTHHDFEAVIEALEEGRIDIDRarhMITGRVNIEDGLDGAImkLINEKEStIKIILT 375
Cdd:cd05279 309 TVfggWKSKDSVPKLVALYRQKKFPLDE---LITHVLPFEEINDGFD--LMRSGES-IRTILT 365
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 1-363 3.75e-31

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


Pssm-ID: 176242 [Multi-domain]  Cd Length: 375  Bit Score: 122.32  E-value: 3.75e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRfTNHLKEPHIVAPDELVIDIEWCGICGTDLHEYtdgpiffpeDGHTHEishnPLPQAMGHEMAGTVL 80
Cdd:cd08282   1 MKAVVYGGPGNVA-VEDVPDPKIEHPTDAIVRITTTAICGSDLHMY---------RGRTGA----EPGLVLGHEAMGEVE 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVeptgtcrdryrwplsP-NVDKEWCAACKKGYYNICSYL---------GLCGAGVQSGGFAE-- 148
Cdd:cd08282  67 EVGSAVESLKVGDRVVV---------------PfNVACGRCRNCKRGLTGVCLTVnpgraggayGYVDMGPYGGGQAEyl 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  149 RVVMNESHCYKVP---------DFVPL-DVaaliqpLAVCWHAIRVCEFKAGSTALIIGAGPIGLgtiLALNAA---GCK 215
Cdd:cd08282 132 RVPYADFNLLKLPdrdgakekdDYLMLsDI------FPTGWHGLELAGVQPGDTVAVFGAGPVGL---MAAYSAilrGAS 202

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  216 DIVVSEPAKVRRELAEKMGARVYDPTAHAAKESIDYLRsiadgGDGFDYTFDCSGLEvtlnaaiqCLTFRGTAV-NLAMw 294
Cdd:cd08282 203 RVYVVDHVPERLDLAESIGAIPIDFSDGDPVEQILGLE-----PGGVDRAVDCVGYE--------ARDRGGEAQpNLVL- 268

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319257  295 ghhkiqFSPMDITlherKYTGSM----CYTHHDFEAVIEALEEGRIDID------RARHMITGRVNIEDgLDGAIMKLI 363
Cdd:cd08282 269 ------NQLIRVT----RPGGGIgivgVYVAEDPGAGDAAAKQGELSFDfgllwaKGLSFGTGQAPVKK-YNRQLRDLI 336
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 18-356 1.04e-30

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


Pssm-ID: 176241 [Multi-domain]  Cd Length: 371  Bit Score: 121.33  E-value: 1.04e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   18 LKEPhivAPDELVIDIEWCGICGTDLHEYT-DGPiffpedghtheishNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVV 96
Cdd:cd08281  28 LDPP---GPGEVLVKIAAAGLCHSDLSVINgDRP--------------RPLPMALGHEAAGVVVEVGEGVTDLEVGDHVV 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   97 VEPTGTCRDryrwplspnvdkewCAACKKGYYNicsylgLCGAGVQSGG--------------------------FAERV 150
Cdd:cd08281  91 LVFVPSCGH--------------CRPCAEGRPA------LCEPGAAANGagtllsggrrlrlrggeinhhlgvsaFAEYA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  151 VMNESHCYKVPDFVPLDVAALIQpLAV---CWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRR 227
Cdd:cd08281 151 VVSRRSVVKIDKDVPLEIAALFG-CAVltgVGAVVNTAGVRPGQSVAVVGLGGVGLSALLGAVAAGASQVVAVDLNEDKL 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  228 ELAEKMGA-RVYDPTAHAAKESIDYLRsiadgGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWG-HHKIQFSPMD 305
Cdd:cd08281 230 ALARELGAtATVNAGDPNAVEQVRELT-----GGGVDYAFEMAGSVPALETAYEITRRGGTTVTAGLPDpEARLSVPALS 304

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6319257  306 ITLHERKYTGSM---CYTHHDFEAVIEALEEGRIDIDRarhMITGRV---NIEDGLD 356
Cdd:cd08281 305 LVAEERTLKGSYmgsCVPRRDIPRYLALYLSGRLPVDK---LLTHRLpldEINEGFD 358
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 66-349 6.11e-30

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: 117.94  E-value: 6.11e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   66 PLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVveptGTCRDryrwplspnvdkewcaackkgyynicsylglcgagvqsGG 145
Cdd:COG0604  56 GLPFIPGSDAAGVVVAVGEGVTGFKVGDRVA----GLGRG--------------------------------------GG 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  146 FAERVVMNESHCYKVPDFVPLDVAALIqPLAVC--WHA-IRVCEFKAGSTALIIGA-GpiGLGTILA--LNAAGCKDI-V 218
Cdd:COG0604  94 YAEYVVVPADQLVPLPDGLSFEEAAAL-PLAGLtaWQAlFDRGRLKPGETVLVHGAaG--GVGSAAVqlAKALGARVIaT 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  219 VSEPAKvrRELAEKMGA-RVYDPTAHAAKESIdylRSIAdGGDGFDYTFDCSGLEvTLNAAIQCLTFRGTAVNLAMWGHH 297
Cdd:COG0604 171 ASSPEK--AELLRALGAdHVIDYREEDFAERV---RALT-GGRGVDVVLDTVGGD-TLARSLRALAPGGRLVSIGAASGA 243

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  298 KIQFSPMDITLHERKYTGS--MCYT----HHDFEAVIEALEEGRID--IDR----------ARHMITGRV 349
Cdd:COG0604 244 PPPLDLAPLLLKGLTLTGFtlFARDpaerRAALAELARLLAAGKLRpvIDRvfpleeaaeaHRLLESGKH 313
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
200-333 6.16e-29

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 109.62  E-value: 6.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    200 PIGLGTILALNAAGCKdIVVSEPAKVRRELAEKMGA-RVYDPTAhaaKESIDYLRSIAdGGDGFDYTFDCSGLEVTLNAA 278
Cdd:pfam00107   1 GVGLAAIQLAKAAGAK-VIAVDGSEEKLELAKELGAdHVINPKE---TDLVEEIKELT-GGKGVDVVFDCVGSPATLEQA 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6319257    279 IQCLTFRGTAVNLAMwGHHKIQFSPMDITLHERKYTGSMCYTHHDFEAVIEALEE 333
Cdd:pfam00107  76 LKLLRPGGRVVVVGL-PGGPLPLPLAPLLLKELTILGSFLGSPEEFPEALDLLAS 129
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
 1-376 9.98e-29

formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol dehydrogenases and glutathione-dependant formaldehyde dehydrogenases (FDH) of the zinc-dependent/medium chain alcohol dehydrogenase family. The MDR family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176247 [Multi-domain]  Cd Length: 345  Bit Score: 115.10  E-value: 9.98e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFtNHLKEPHIVAPDELVIDIEWCGICGTDLHEYTdgpiffpedGHThEISHnplPQAMGHEMAGTVL 80
Cdd:cd08287   1 MRATVIHGPGDIRV-EEVPDPVIEEPTDAVIRVVATCVCGSDLWPYR---------GVS-PTRA---PAPIGHEFVGVVE 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVEptgtcrdryrWPLSPNVdkewCAACKKGYYNICSYLGLCGAGVqSGGFAE--RVVMNESHCY 158
Cdd:cd08287  67 EVGSEVTSVKPGDFVIAP----------FAISDGT----CPFCRAGFTTSCVHGGFWGAFV-DGGQGEyvRVPLADGTLV 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  159 KVPDfVPLDVAALIQPL-------AVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAE 231
Cdd:cd08287 132 KVPG-SPSDDEDLLPSLlalsdvmGTGHHAAVSAGVRPGSTVVVVGDGAVGLCAVLAAKRLGAERIIAMSRHEDRQALAR 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  232 KMGARvyDPTAHAAKESIDYLRSIAdGGDGFDYTFDCSGLEVTLNAAIQClTFRGTAVNLAMWGHHKIQFSPMDITLHER 311
Cdd:cd08287 211 EFGAT--DIVAERGEEAVARVRELT-GGVGADAVLECVGTQESMEQAIAI-ARPGGRVGYVGVPHGGVELDVRELFFRNV 286

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319257  312 KYTGSMCYTHHDFEAVIEALEEGRIDidrarhmiTGRV-NIEDGLDGAI--MKLINEKEsTIKIILTP 376
Cdd:cd08287 287 GLAGGPAPVRRYLPELLDDVLAGRIN--------PGRVfDLTLPLDEVAegYRAMDERR-AIKVLLRP 345
PRK10083 PRK10083
putative oxidoreductase; Provisional
 25-375 4.69e-28

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 113.30  E-value: 4.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    25 APDELVIDIEWCGICGTDLHEYTdgpiffpedghtheiSHNPL---PQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTG 101
Cdd:PRK10083  23 AAGEVRVKVKLAGICGSDSHIYR---------------GHNPFakyPRVIGHEFFGVIDAVGEGVDAARIGERVAVDPVI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   102 TCRDryrwplspnvdkewCAACKKGYYNICSYLGLCGAGvQSGGFAERVVMNESHCYKVPDFVPLDVAALIQPLAVCWHA 181
Cdd:PRK10083  88 SCGH--------------CYPCSIGKPNVCTSLVVLGVH-RDGGFSEYAVVPAKNAHRIPDAIADQYAVMVEPFTIAANV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   182 IRVCEFKAGSTALIIGAGPIGLGTILALNAA-GCKDIVVSEPAKVRRELAEKMGArvyDPTAHAAKESIDylRSIADGGD 260
Cdd:PRK10083 153 TGRTGPTEQDVALIYGAGPVGLTIVQVLKGVyNVKAVIVADRIDERLALAKESGA---DWVINNAQEPLG--EALEEKGI 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   261 GFDYTFDCSGLEVTLNAAIqclTFRGTAVNLAMWGhhkiqFSPMDITLHERKYTG---SMCYTHHD---FEAVIEALEEG 334
Cdd:PRK10083 228 KPTLIIDAACHPSILEEAV---TLASPAARIVLMG-----FSSEPSEIVQQGITGkelSIFSSRLNankFPVVIDWLSKG 299

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 6319257   335 RIDIDrarHMITGRVNIEDGLDGAIMKLINEKESTiKIILT 375
Cdd:PRK10083 300 LIDPE---KLITHTFDFQHVADAIELFEKDQRHCC-KVLLT 336
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 1-274 8.19e-28

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


Pssm-ID: 176246 [Multi-domain]  Cd Length: 345  Bit Score: 112.73  E-value: 8.19e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFTNHLKePHIVAPDELVIDIEWCGICGTDLH-------EYTDGPIffpedghtheishnplpqaMGH 73
Cdd:cd08286   1 MKALVYHGPGKISWEDRPK-PTIQEPTDAIVKMLKTTICGTDLHilkgdvpTVTPGRI-------------------LGH 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   74 EMAGTVLEVGPGVKNLKVGDKVVVEPTGTCRDryrwplspnvdkewCAACKKGYYNICSY----LGLCGAGVQsggfAE- 148
Cdd:cd08286  61 EGVGVVEEVGSAVTNFKVGDRVLISCISSCGT--------------CGYCRKGLYSHCESggwiLGNLIDGTQ----AEy 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  149 -RVVMNESHCYKVPDFVPLDVAALI-------QPLAVCwhAIRVcefKAGSTALIIGAGPIGLGTILALNAAGCKDIVVS 220
Cdd:cd08286 123 vRIPHADNSLYKLPEGVDEEAAVMLsdilptgYECGVL--NGKV---KPGDTVAIVGAGPVGLAALLTAQLYSPSKIIMV 197

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6319257  221 EPAKVRRELAEKMGA-RVYDPTAHAAKESIDYLrsiaDGGDGFDYTFDCSGLEVT 274
Cdd:cd08286 198 DLDDNRLEVAKKLGAtHTVNSAKGDAIEQVLEL----TDGRGVDVVIEAVGIPAT 248
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
1-313 1.27e-26

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 109.15  E-value: 1.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257     1 MRALAYFGKGNIRFTNHLKePHIVAPDELVIDIEWCGICGTDLheytdgPIFFPEDGHTHEIShnplpqaMGHEMAGTVL 80
Cdd:PRK10309   1 MKSVVNDTDGIVRVAESPI-PEIKHQDDVLVKVASSGLCGSDI------PRIFKNGAHYYPIT-------LGHEFSGYVE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    81 EVGPGVKNLKVGDKVVVEPTGTCRDryrwplspnvdkewCAACKKGYYNICSYLGLCGAGvQSGGFAERVVMNESHCYKV 160
Cdd:PRK10309  67 AVGSGVDDLHPGDAVACVPLLPCFT--------------CPECLRGFYSLCAKYDFIGSR-RDGGNAEYIVVKRKNLFAL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   161 PDFVPLDVAALIQPLAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGA-RVYD 239
Cdd:PRK10309 132 PTDMPIEDGAFIEPITVGLHAFHLAQGCEGKNVIIIGAGTIGLLAIQCAVALGAKSVTAIDINSEKLALAKSLGAmQTFN 211

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6319257   240 PTAHAAKESIDYLRSIAdggdgFD-YTFDCSGLEVTLNAAIQcltFRGTAVNLAMWG--HHkiqfspmDITLHERKY 313
Cdd:PRK10309 212 SREMSAPQIQSVLRELR-----FDqLILETAGVPQTVELAIE---IAGPRAQLALVGtlHH-------DLHLTSATF 273
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-341 3.03e-26

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: 108.61  E-value: 3.03e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRAlAYFGKGNIRFTnhLKEPHIVAPD--ELVIDIEWCGICGTDLHeYTDGPIFFPEdghtheishnplPQAMGHEMAGT 78
Cdd:cd08263   1 MKA-AVLKGPNPPLT--IEEIPVPRPKegEILIRVAACGVCHSDLH-VLKGELPFPP------------PFVLGHEISGE 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   79 VLEVGPGVKN---LKVGDKVVVE---PTGTCRdryrwplspnvdkeWCAackKGYYNICSYL------------------ 134
Cdd:cd08263  65 VVEVGPNVENpygLSVGDRVVGSfimPCGKCR--------------YCA---RGKENLCEDFfaynrlkgtlydgttrlf 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  135 GLCGAGVQ---SGGFAERVVMNESHCYKVPDFVPLDVAALIQplavC-----WHAIR-VCEFKAGSTALIIGAGPIGLGT 205
Cdd:cd08263 128 RLDGGPVYmysMGGLAEYAVVPATALAPLPESLDYTESAVLG----CagftaYGALKhAADVRPGETVAVIGVGGVGSSA 203

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  206 ILALNAAGCKDIVVSEPAKVRRELAEKMGArvyDPTAHAAKEsiDYLRSIAD--GGDGFDYTFDCSGLEVTLNAAIQCLT 283
Cdd:cd08263 204 IQLAKAFGASPIIAVDVRDEKLAKAKELGA---THTVNAAKE--DAVAAIREitGGRGVDVVVEALGKPETFKLALDVVR 278

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319257  284 FRGTAV--NLAMWGhhkiQFSPMDITLHER---KYTGSMCY-THHDFEAVIEALEEGRIDIDRA 341
Cdd:cd08263 279 DGGRAVvvGLAPGG----ATAEIPITRLVRrgiKIIGSYGArPRQDLPELVGLAASGKLDPEAL 338
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 26-339 4.02e-26

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


Pssm-ID: 176207 [Multi-domain]  Cd Length: 330  Bit Score: 107.41  E-value: 4.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   26 PDELVIDIEWCGICGTDLHEyTDGPIFFPedghtheishnPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVE-PTGTCR 104
Cdd:cd08245  24 PGEVLIKIEACGVCHTDLHA-AEGDWGGS-----------KYPLVPGHEIVGEVVEVGAGVEGRKVGDRVGVGwLVGSCG 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  105 DryrwplspnvdkewCAACKKGYYNICSYLGLCGAGVQsGGFAERVVMNESHCYKVPDFVPLDVAAliqPLaVC-----W 179
Cdd:cd08245  92 R--------------CEYCRRGLENLCQKAVNTGYTTQ-GGYAEYMVADAEYTVLLPDGLPLAQAA---PL-LCagitvY 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  180 HAIRVCEFKAGSTALIIGAGPIG-LGTILAlNAAGCKDIVVS-EPAKvrRELAEKMGARVYDPTAHAakesidyLRSIAD 257
Cdd:cd08245 153 SALRDAGPRPGERVAVLGIGGLGhLAVQYA-RAMGFETVAITrSPDK--RELARKLGADEVVDSGAE-------LDEQAA 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  258 GGdGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGHHKIQFSPMDITLHERKYTGSMCYTHHDFEAVIEALEEGRID 337
Cdd:cd08245 223 AG-GADVILVTVVSGAAAEAALGGLRRGGRIVLVGLPESPPFSPDIFPLIMKRQSIAGSTHGGRADLQEALDFAAEGKVK 301


                ..
gi 6319257  338 ID 339
Cdd:cd08245 302 PM 303
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 26-241 2.88e-25

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


Pssm-ID: 176258 [Multi-domain]  Cd Length: 329  Bit Score: 104.96  E-value: 2.88e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   26 PDELVIDIEWCGICGTDLHEyTDGpiffpedghthEISHNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTG-TCR 104
Cdd:cd08298  29 PGEVLIKVEACGVCRTDLHI-VEG-----------DLPPPKLPLIPGHEIVGRVEAVGPGVTRFSVGDRVGVPWLGsTCG 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  105 DryrwplspnvdkewCAACKKGYYNICSYLGLCGAGVQsGGFAERVVMNESHCYKVPD-FVPLDVAALIQPLAVCWHAIR 183
Cdd:cd08298  97 E--------------CRYCRSGRENLCDNARFTGYTVD-GGYAEYMVADERFAYPIPEdYDDEEAAPLLCAGIIGYRALK 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6319257  184 VCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKvRRELAEKMGA-RVYDPT 241
Cdd:cd08298 162 LAGLKPGQRLGLYGFGASAHLALQIARYQGAEVFAFTRSGE-HQELARELGAdWAGDSD 219
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 1-286 8.88e-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: 103.73  E-value: 8.88e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRAL---AYFGKGNIRFTNHLKEPhiVAPDELVIDIEWCGICGTDL----HEYTDGPiffpedghtheishnPLPQAMGH 73
Cdd:cd08241   1 MKAVvckELGGPEDLVLEEVPPEP--GAPGEVRIRVEAAGVNFPDLlmiqGKYQVKP---------------PLPFVPGS 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   74 EMAGTVLEVGPGVKNLKVGDKVVveptgtcrdryrwplspnvdkewcaackkgyynicsylglcgAGVQSGGFAERVVMN 153
Cdd:cd08241  64 EVAGVVEAVGEGVTGFKVGDRVV------------------------------------------ALTGQGGFAEEVVVP 101

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  154 ESHCYKVPDFVPLDVAAliqPLAVC----WHA-IRVCEFKAGSTALIIGA-GPIGLGTI-LAlNAAGCKDI-VVSEPAKv 225
Cdd:cd08241 102 AAAVFPLPDGLSFEEAA---ALPVTygtaYHAlVRRARLQPGETVLVLGAaGGVGLAAVqLA-KALGARVIaAASSEEK- 176

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319257  226 rRELAEKMGA-RVYDptaHAAKESIDYLRSIAdGGDGFDYTFDCSGLEVTlNAAIQCLTFRG 286
Cdd:cd08241 177 -LALARALGAdHVID---YRDPDLRERVKALT-GGRGVDVVYDPVGGDVF-EASLRSLAWGG 232
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
 24-281 6.21e-24

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


Pssm-ID: 176260 [Multi-domain]  Cd Length: 368  Bit Score: 101.92  E-value: 6.21e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   24 VAP---DELVIDIEWCGICGTDlhEYTdgpiffpEDGHTHEIShnpLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPT 100
Cdd:cd08300  22 VAPpkaGEVRIKILATGVCHTD--AYT-------LSGADPEGL---FPVILGHEGAGIVESVGEGVTSVKPGDHVIPLYT 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  101 GTCRDryrwplspnvdkewCAACKKGYYNICSYL-GLCGAGVQSGG-------------------FAERVVMNESHCYKV 160
Cdd:cd08300  90 PECGE--------------CKFCKSGKTNLCQKIrATQGKGLMPDGtsrfsckgkpiyhfmgtstFSEYTVVAEISVAKI 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  161 PDFVPLDVAALIQplavC-----WHA-IRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMG 234
Cdd:cd08300 156 NPEAPLDKVCLLG----CgvttgYGAvLNTAKVEPGSTVAVFGLGAVGLAVIQGAKAAGASRIIGIDINPDKFELAKKFG 231

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 6319257  235 ARVY-DPTAHaAKESIDYLRSIADGgdGFDYTFDCSGLEVTLNAAIQC 281
Cdd:cd08300 232 ATDCvNPKDH-DKPIQQVLVEMTDG--GVDYTFECIGNVKVMRAALEA 276
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 1-340 2.00e-23

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: 99.56  E-value: 2.00e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAY--FGKGNIRFTNHLKEPHIvAPDELVIDIEWCGICGTDLHEYtdgpiffpeDGHTHEISHNPLPQAMGHEMAGT 78
Cdd:cd05289   1 MKAVRIheYGGPEVLELADVPTPEP-GPGEVLVKVHAAGVNPVDLKIR---------EGLLKAAFPLTLPLIPGHDVAGV 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   79 VLEVGPGVKNLKVGDKVvveptgtcrdryrwplspnvdkewcaackkgyynicsyLGLCGAGvQSGGFAERVVMNESHCY 158
Cdd:cd05289  71 VVAVGPGVTGFKVGDEV--------------------------------------FGMTPFT-RGGAYAEYVVVPADELA 111

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  159 KVPDFVPLDVAALIqPLA--VCWHAI-RVCEFKAGSTALIIGA-GpiGLGTI---LALnAAGCKDIVVSEPAKvrRELAE 231
Cdd:cd05289 112 LKPANLSFEEAAAL-PLAglTAWQALfELGGLKAGQTVLIHGAaG--GVGSFavqLAK-ARGARVIATASAAN--ADFLR 185

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  232 KMGA-RVYDPTAHAAKEsidylrsiADGGDGFDYTFDCSGLEvTLNAAIQCLTFRGTAVNLAmwghhkiQFSPMDITLHE 310
Cdd:cd05289 186 SLGAdEVIDYTKGDFER--------AAAPGGVDAVLDTVGGE-TLARSLALVKPGGRLVSIA-------GPPPAEQAAKR 249

                       330       340       350
                ....*....|....*....|....*....|....*
gi 6319257  311 RKYTGSMCYTH---HDFEAVIEALEEGRI--DIDR 340
Cdd:cd05289 250 RGVRAGFVFVEpdgEQLAELAELVEAGKLrpVVDR 284
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 25-377 4.40e-23

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 98.96  E-value: 4.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    25 APDELVIDIEWCGICGTDLHEYTDgpiFFPEdghtheishNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVV---VEPTG 101
Cdd:PRK13771  24 GKDEVVIKVNYAGLCYRDLLQLQG---FYPR---------MKYPVILGHEVVGTVEEVGENVKGFKPGDRVAsllYAPDG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   102 TCRdryrwplspnvdkewcaACKKGYYNICSYLGLCGAGVQsGGFAERVVMNESHCYKVPDFVPlDVAALIQP--LAVCW 179
Cdd:PRK13771  92 TCE-----------------YCRSGEEAYCKNRLGYGEELD-GFFAEYAKVKVTSLVKVPPNVS-DEGAVIVPcvTGMVY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   180 HAIRVCEFKAGSTALIIGAGPiGLGtILALnaagckdivvsepakvrrELAEKMGARVYDPTAHAAKESIdyLRSIADGG 259
Cdd:PRK13771 153 RGLRRAGVKKGETVLVTGAGG-GVG-IHAI------------------QVAKALGAKVIAVTSSESKAKI--VSKYADYV 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   260 -DGFDYTFDCSGLEvTLNAAIQCL---TFRGTAVNLAmWGHHKIQFSPMD-----------ITLHERKYTGSMCYTHHDF 324
Cdd:PRK13771 211 iVGSKFSEEVKKIG-GADIVIETVgtpTLEESLRSLN-MGGKIIQIGNVDpsptyslrlgyIILKDIEIIGHISATKRDV 288

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6319257   325 EAVIEALEEGRIdidraRHMITGRVNIEDgLDGAiMKLINEKESTIKIILTPN 377
Cdd:PRK13771 289 EEALKLVAEGKI-----KPVIGAEVSLSE-IDKA-LEELKDKSRIGKILVKPS 334
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 1-376 4.02e-22

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


Pssm-ID: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 96.54  E-value: 4.02e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNIRFTNhlKEPHIVAPDELVIDIEWCGICGTDLHEYTDGPIFFPEDghtheishnplpQAMGHEMAGTVL 80
Cdd:cd08285   1 MKAFAMLGIGKVGWIE--KPIPVCGPNDAIVRPTAVAPCTSDVHTVWGGAPGERHG------------MILGHEAVGVVE 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   81 EVGPGVKNLKVGDKVVVeptgtcrdryrwplsPNVDKEW-CAACKKGYYNICSylGLCG----AGVQSGGFAERVVMNES 155
Cdd:cd08285  67 EVGSEVKDFKPGDRVIV---------------PAITPDWrSVAAQRGYPSQSG--GMLGgwkfSNFKDGVFAEYFHVNDA 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  156 --HCYKVPDFVPlDVAALIQP--LAVCWHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAE 231
Cdd:cd08285 130 daNLAPLPDGLT-DEQAVMLPdmMSTGFHGAELANIKLGDTVAVFGIGPVGLMAVAGARLRGAGRIIAVGSRPNRVELAK 208

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  232 KMGARVY-DPTAHAAKESIdyLRsiADGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGHH---KIQFSPMDIT 307
Cdd:cd08285 209 EYGATDIvDYKNGDVVEQI--LK--LTGGKGVDAVIIAGGGQDTFEQALKVLKPGGTISNVNYYGEDdylPIPREEWGVG 284

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6319257  308 LHERKYTGSMCYTHHD-FEAVIEALEEGRIDIDR-ARHMITGRVNIEDGLDgaIMKliNEKESTIKIILTP 376
Cdd:cd08285 285 MGHKTINGGLCPGGRLrMERLASLIEYGRVDPSKlLTHHFFGFDDIEEALM--LMK--DKPDDLIKPVIIF 351
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 66-289 5.92e-21

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: 93.09  E-value: 5.92e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   66 PLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTGTCRdryrwplspnvdkeWCAACKKGYYNICSYLGLCGAGVqSGG 145
Cdd:cd08266  56 PLPHILGSDGAGVVEAVGPGVTNVKPGQRVVIYPGISCG--------------RCEYCLAGRENLCAQYGILGEHV-DGG 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  146 FAERVVMNESHCYKVPDFVPLDVAALIqPLA--VCWHAI----RVcefKAGSTALIIGAGP-IGLGTILALNAAGCKDIV 218
Cdd:cd08266 121 YAEYVAVPARNLLPIPDNLSFEEAAAA-PLTflTAWHMLvtraRL---RPGETVLVHGAGSgVGSAAIQIAKLFGATVIA 196

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319257  219 -VSEPAKVRRelAEKMGA-RVYDptaHAAKESIDYLRSIAdGGDGFDYTFDCSGlEVTLNAAIQCLTFRGTAV 289
Cdd:cd08266 197 tAGSEDKLER--AKELGAdYVID---YRKEDFVREVRELT-GKRGVDVVVEHVG-AATWEKSLKSLARGGRLV 262
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 1-374 6.96e-21

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


Pssm-ID: 176192 [Multi-domain]  Cd Length: 355  Bit Score: 93.05  E-value: 6.96e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYF-GKGNIRFTNhLKEPHIVaPDELVIDIEWCGICGTDlHEYTDGPIFFPEDGHTHEIshnplpqaMGHEMAGTV 79
Cdd:cd08230   1 MKAIAVKpGKPGVRVVD-IPEPEPT-PGEVLVRTLEVGVCGTD-REIVAGEYGTAPPGEDFLV--------LGHEALGVV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   80 LEVGPGvKNLKVGDKVVveptGTCRdryRWPLSpnvdkewCAACKKGYYNICS---YL--GLCGAGvqsGGFAERVVMNE 154
Cdd:cd08230  70 EEVGDG-SGLSPGDLVV----PTVR---RPPGK-------CLNCRIGRPDFCEtgeYTerGIKGLH---GFMREYFVDDP 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  155 SHCYKVPDFVpLDVAALIQPLAV---CW-HAIRVCE---FKAGSTALIIGAGPIGLGTILALNAAGCKDIVVS--EPAKV 225
Cdd:cd08230 132 EYLVKVPPSL-ADVGVLLEPLSVvekAIeQAEAVQKrlpTWNPRRALVLGAGPIGLLAALLLRLRGFEVYVLNrrDPPDP 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  226 RRELAEKMGARVYDptahaakESIDYLRSIADGGdGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGHH-KIQFSP- 303
Cdd:cd08230 211 KADIVEELGATYVN-------SSKTPVAEVKLVG-EFDLIIEATGVPPLAFEALPALAPNGVVILFGVPGGGrEFEVDGg 282

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319257  304 ---MDITLHERKYTGSMCYTHHDFEAVIEALEEGRIDI-DRARHMITGRVNIEDGLDGaimkLINEKESTIKIIL 374
Cdd:cd08230 283 elnRDLVLGNKALVGSVNANKRHFEQAVEDLAQWKYRWpGVLERLITRRVPLEEFAEA----LTEKPDGEIKVVI 353
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 1-247 1.28e-20

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase family. However, this subgroup does not contain the characteristic catalytic zinc site. Also, it contains an atypical structural zinc-binding pattern: DxxCxxCxxxxxxxC. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176225 [Multi-domain]  Cd Length: 325  Bit Score: 92.03  E-value: 1.28e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAY--FGKGNIRFTNhLKEPHiVAPDELVIDIEWCGICGTDLheYTDGPIFFpedghtheishNPLPQAMGHEMAGT 78
Cdd:cd08264   1 MKALVFekSGIENLKVED-VKDPK-PGPGEVLIRVKMAGVNPVDY--NVINAVKV-----------KPMPHIPGAEFAGV 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   79 VLEVGPGVKNLKVGDKVVVEP---TGTCRdryrwplspnvdkewcaACKKGYYNICSYLGLCGAGVQsGGFAERVVMNES 155
Cdd:cd08264  66 VEEVGDHVKGVKKGDRVVVYNrvfDGTCD-----------------MCLSGNEMLCRNGGIIGVVSN-GGYAEYIVVPEK 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  156 HCYKVPDFVPLDVAALIqPLAV--CWHAIRVCEFKAGSTALIIGA-GPIGlgtILALNAA---GCKDIVVSepakvRREL 229
Cdd:cd08264 128 NLFKIPDSISDELAASL-PVAAltAYHALKTAGLGPGETVVVFGAsGNTG---IFAVQLAkmmGAEVIAVS-----RKDW 198

                       250       260
                ....*....|....*....|.
gi 6319257  230 AEKMGARV---YDPTAHAAKE 247
Cdd:cd08264 199 LKEFGADEvvdYDEVEEKVKE 219
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 25-238 1.43e-19

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 (ADHs), 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: 176256 [Multi-domain]  Cd Length: 333  Bit Score: 88.84  E-value: 1.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   25 APDELVIDIEWCGICGTDlheytdgpiFFPEDGHtheISHNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVE-PTGTC 103
Cdd:cd08296  24 GPGEVLIKVEACGVCHSD---------AFVKEGA---MPGLSYPRVPGHEVVGRIDAVGEGVSRWKVGDRVGVGwHGGHC 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  104 RDryrwplspnvdkewCAACKKGYYNICSYLGLCGAgVQSGGFAERVVMNESHCYKVPD-FVPLDVAaliqPLAvC---- 178
Cdd:cd08296  92 GT--------------CDACRRGDFVHCENGKVTGV-TRDGGYAEYMLAPAEALARIPDdLDAAEAA----PLL-Cagvt 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319257  179 -WHAIRVCEFKAGSTALIIGAGpiGLGTiLAL---NAAGCKDIVVSEPAKvRRELAEKMGARVY 238
Cdd:cd08296 152 tFNALRNSGAKPGDLVAVQGIG--GLGH-LAVqyaAKMGFRTVAISRGSD-KADLARKLGAHHY 211
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 66-290 1.82e-19

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: 88.27  E-value: 1.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   66 PLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVveptgtcrdryrwplspnvdkeWCAAckkgyynicsylglcgagvqSGG 145
Cdd:cd05286  53 PLPFVLGVEGAGVVEAVGPGVTGFKVGDRVA----------------------YAGP--------------------PGA 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  146 FAERVVMNESHCYKVPDFVPLDVAA--LIQPLAVcWHAIR-VCEFKAGSTALI-IGAGpiGLGTILA--LNAAGCKDI-V 218
Cdd:cd05286  91 YAEYRVVPASRLVKLPDGISDETAAalLLQGLTA-HYLLReTYPVKPGDTVLVhAAAG--GVGLLLTqwAKALGATVIgT 167

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319257  219 VSEPAKVrrELAEKMGAR---VYDPTAHAAKesidyLRSIADGGdGFDYTFDCSGLEvTLNAAIQCLTFRGTAVN 290
Cdd:cd05286 168 VSSEEKA--ELARAAGADhviNYRDEDFVER-----VREITGGR-GVDVVYDGVGKD-TFEGSLDSLRPRGTLVS 233
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
 24-316 1.92e-19

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


Pssm-ID: 176259 [Multi-domain]  Cd Length: 373  Bit Score: 89.29  E-value: 1.92e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   24 VAP---DELVIDIEWCGICGTDLHeYTDGPIFfpedghtheishNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVvept 100
Cdd:cd08299  27 VAPpkaHEVRIKIVATGICRSDDH-VVSGKLV------------TPFPVILGHEAAGIVESVGEGVTTVKPGDKVI---- 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  101 gtcrdryrwPL-SPNVDKewCAACKKGYYNICSYLGLCGA-GVQSGG-------------------FAERVVMNESHCYK 159
Cdd:cd08299  90 ---------PLfVPQCGK--CRACLNPESNLCLKNDLGKPqGLMQDGtsrftckgkpihhflgtstFSEYTVVDEIAVAK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  160 VPDFVPLDVAALIQplavCWH------AIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKM 233
Cdd:cd08299 159 IDAAAPLEKVCLIG----CGFstgygaAVNTAKVTPGSTCAVFGLGGVGLSAIMGCKAAGASRIIAVDINKDKFAKAKEL 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  234 GA-RVYDPTahaakesiDYLRSIAD-----GGDGFDYTFDCSGLEVTLNAAIQCLTFR-GTAVNL-AMWGHHKIQFSPMD 305
Cdd:cd08299 235 GAtECINPQ--------DYKKPIQEvltemTDGGVDFSFEVIGRLDTMKAALASCHEGyGVSVIVgVPPSSQNLSINPML 306

                       330
                ....*....|.
gi 6319257  306 ItLHERKYTGS 316
Cdd:cd08299 307 L-LTGRTWKGA 316
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 70-348 3.78e-18

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: 84.16  E-value: 3.78e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   70 AMGHEMAGTVLEVGPGVKNLKVGDKVVveptgtcrdryrwplspnvdkewcaackkgyynicsylglcgaGVQSGGFAER 149
Cdd:cd05195  30 PLGLECSGIVTRVGSGVTGLKVGDRVM-------------------------------------------GLAPGAFATH 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  150 VVMNESHCYKVPDFVPLDVAALIqPLAVC--WHA-IRVCEFKAGSTALII-GAGPIGLGTI-LALnAAGCKDIV-VSEPA 223
Cdd:cd05195  67 VRVDARLVVKIPDSLSFEEAATL-PVAYLtaYYAlVDLARLQKGESVLIHaAAGGVGQAAIqLAQ-HLGAEVFAtVGSEE 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  224 KvrRELAEKMgarvYDPTAH-AAKESIDYLRSI--ADGGDGFDYTFDC-SGLevTLNAAIQCLTFRGTAVNLA---MWGH 296
Cdd:cd05195 145 K--REFLREL----GGPVDHiFSSRDLSFADGIlrATGGRGVDVVLNSlSGE--LLRASWRCLAPFGRFVEIGkrdILSN 216

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319257  297 HKIQFSPMDitlHERKYTG----SMCYTHHD-----FEAVIEALEEGRI------------DIDRARHMITGR 348
Cdd:cd05195 217 SKLGMRPFL---RNVSFSSvdldQLARERPEllrelLREVLELLEAGVLkplpptvvpsasEIDAFRLMQSGK 286
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 24-316 4.30e-18

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


Pssm-ID: 176261 [Multi-domain]  Cd Length: 369  Bit Score: 85.04  E-value: 4.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   24 VAPD---ELVIDIEWCGICGTDLHeytdgpiFFPEDGHTHEishnpLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPT 100
Cdd:cd08301  22 VAPPqamEVRIKILHTSLCHTDVY-------FWEAKGQTPL-----FPRILGHEAAGIVESVGEGVTDLKPGDHVLPVFT 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  101 GTCRDryrwplspnvdkewCAACKKGYYNICSYLGL-CGAGVQSGG--------------------FAERVVMNESHCYK 159
Cdd:cd08301  90 GECKE--------------CRHCKSEKSNMCDLLRInTDRGVMINDgksrfsingkpiyhfvgtstFSEYTVVHVGCVAK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  160 VPDFVPLDVAALIQplavC------WHAIRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDI--VVSEPAKVrrELAE 231
Cdd:cd08301 156 INPEAPLDKVCLLS----CgvstglGAAWNVAKVKKGSTVAIFGLGAVGLAVAEGARIRGASRIigVDLNPSKF--EQAK 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  232 KMGARVY-DPTAHAAKESiDYLRSIADGgdGFDYTFDCSGLEVTLNAAIQCL-TFRGTAVNLAMWGH-HKIQFSPMDItL 308
Cdd:cd08301 230 KFGVTEFvNPKDHDKPVQ-EVIAEMTGG--GVDYSFECTGNIDAMISAFECVhDGWGVTVLLGVPHKdAVFSTHPMNL-L 305


                ....*...
gi 6319257  309 HERKYTGS 316
Cdd:cd08301 306 NGRTLKGT 313
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 66-301 6.46e-17

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: 80.95  E-value: 6.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   66 PLPQA---MGHEMAGTVLEVGPGVKNLKVGDKVvveptgtcrdryrwplspnvdkewCAackkgyynicsylgLcgagVQ 142
Cdd:cd05276  53 PPPGAsdiLGLEVAGVVVAVGPGVTGWKVGDRV------------------------CA--------------L----LA 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  143 SGGFAERVVMNESHCYKVPDFVPLDVAALIqPLAVC--WHAIR-VCEFKAGSTALI-IGAGPIGLGTILALNAAGCKDIV 218
Cdd:cd05276  91 GGGYAEYVVVPAGQLLPVPEGLSLVEAAAL-PEVFFtaWQNLFqLGGLKAGETVLIhGGASGVGTAAIQLAKALGARVIA 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  219 -VSEPAKVrrELAEKMGARV---YDPTAHAAKesidyLRSIADGGdGFDYTFDCSGLEvTLNAAIQCLTFRGTAVNLAMW 294
Cdd:cd05276 170 tAGSEEKL--EACRALGADVainYRTEDFAEE-----VKEATGGR-GVDVILDMVGGD-YLARNLRALAPDGRLVLIGLL 240


                ....*..
gi 6319257  295 GHHKIQF 301
Cdd:cd05276 241 GGAKAEL 247
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
 26-333 7.19e-17

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 81.38  E-value: 7.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    26 PDELVIDIEWCGICGTDLHEYTDgpiffpEDGHTHeishnpLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEP-TGTCR 104
Cdd:PLN02514  34 PEDVVIKVIYCGICHTDLHQIKN------DLGMSN------YPMVPGHEVVGEVVEVGSDVSKFTVGDIVGVGViVGCCG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   105 DryrwplspnvdkewCAACKKGYYNIC-----SYLGLCGAG-VQSGGFAERVVMNESHCYKVPD-FVPLDVAALIQPLAV 177
Cdd:PLN02514 102 E--------------CSPCKSDLEQYCnkriwSYNDVYTDGkPTQGGFASAMVVDQKFVVKIPEgMAPEQAAPLLCAGVT 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   178 CWHAIRvcEFKAGSTAL---IIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGARVYDPTAHAAkesidylrS 254
Cdd:PLN02514 168 VYSPLS--HFGLKQSGLrggILGLGGVGHMGVKIAKAMGHHVTVISSSDKKREEALEHLGADDYLVSSDAA--------E 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319257   255 IADGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMwGHHKIQFSPMDITLHERKYTGSMCYTHHDFEAVIEALEE 333
Cdd:PLN02514 238 MQEAADSLDYIIDTVPVFHPLEPYLSLLKLDGKLILMGV-INTPLQFVTPMLMLGRKVITGSFIGSMKETEEMLEFCKE 315
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 65-349 7.84e-17

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


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 80.72  E-value: 7.84e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   65 NPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVvveptgtcrdryrwplspnvdkewcaackkgyynicsyLGLCGAgVQSG 144
Cdd:cd08267  56 RPFPPIPGMDFAGEVVAVGSGVTRFKVGDEV--------------------------------------FGRLPP-KGGG 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  145 GFAERVVMNESHCYKVPDFVPLDVAALIqPLAVC--WHAIR-VCEFKAGSTALIIGA-GpiGLGTI---LAlNAAGCKDI 217
Cdd:cd08267  97 ALAEYVVAPESGLAKKPEGVSFEEAAAL-PVAGLtaLQALRdAGKVKPGQRVLINGAsG--GVGTFavqIA-KALGAHVT 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  218 VVSEPAKVrrELAEKMGA-RVYDPTahaaKESIDYLRsiaDGGDGFDYTFDCSGLE-VTLNAAIQCLTFRGTAVNLAmwG 295
Cdd:cd08267 173 GVCSTRNA--ELVRSLGAdEVIDYT----TEDFVALT---AGGEKYDVIFDAVGNSpFSLYRASLALKPGGRYVSVG--G 241

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319257  296 HHKIQFSPMDITLH-----ERKYTGSMCY-THHDFEAVIEALEEGRI-----------DIDRA-RHMITGRV 349
Cdd:cd08267 242 GPSGLLLVLLLLPLtlgggGRRLKFFLAKpNAEDLEQLAELVEEGKLkpvidsvypleDAPEAyRRLKSGRA 313
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
 19-237 7.24e-16

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 78.15  E-value: 7.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    19 KEPHIVAPDELVIDIEWCGICGTDLH----EYTDGPiffpedGHTheishnplpqaMGHEMAGTVLEVGPGVKNLKVGDK 94
Cdd:PRK09422  18 KTLRPLKHGEALVKMEYCGVCHTDLHvangDFGDKT------GRI-----------LGHEGIGIVKEVGPGVTSLKVGDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    95 VVV----EPTGTCrdryrwplspnvdkEWCAAckkGYYNICSYLGLCGAGVqSGGFAERVVMNESHCYKVPDfvPLDVAA 170
Cdd:PRK09422  81 VSIawffEGCGHC--------------EYCTT---GRETLCRSVKNAGYTV-DGGMAEQCIVTADYAVKVPE--GLDPAQ 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319257   171 L--IQPLAV-CWHAIRVCEFKAGSTALIIGAGpiGLGTiLAL----NAAGCKDIVVS-EPAKVrrELAEKMGARV 237
Cdd:PRK09422 141 AssITCAGVtTYKAIKVSGIKPGQWIAIYGAG--GLGN-LALqyakNVFNAKVIAVDiNDDKL--ALAKEVGADL 210
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 26-356 1.67e-14

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: 74.16  E-value: 1.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   26 PDELVIDIEWCGICGTDLHEYTDGPIFfpedghtheishnPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVvveptgtcrd 105
Cdd:cd08249  26 PDEVLVKVKAVALNPVDWKHQDYGFIP-------------SYPAILGCDFAGTVVEVGSGVTRFKVGDRV---------- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  106 ryrwplspnvdkewCAACKkgyynicsylGLCGAGVQSGGFAERVVMNESHCYKVPDFVPLDVAALIqPLAVC--WHAIR 183
Cdd:cd08249  83 --------------AGFVH----------GGNPNDPRNGAFQEYVVADADLTAKIPDNISFEEAATL-PVGLVtaALALF 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  184 VCEF-----------KAGSTALIIGAG-PIGLGTILALNAAGCKDIVVSEPAkvRRELAEKMGA-RVYDptaHAAKESID 250
Cdd:cd08249 138 QKLGlplpppkpspaSKGKPVLIWGGSsSVGTLAIQLAKLAGYKVITTASPK--NFDLVKSLGAdAVFD---YHDPDVVE 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  251 YLRSIAdgGDGFDYTFDCSGLEVTLNAAIQCL--TFRGTAVNLamwghhkiqfSPMDITLHER---KYTGSMCYT----- 320
Cdd:cd08249 213 DIRAAT--GGKLRYALDCISTPESAQLCAEALgrSGGGKLVSL----------LPVPEETEPRkgvKVKFVLGYTvfgei 280

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 6319257  321 -------HHDFEAVIEALEEGRIDIDRARHMITGRVNIEDGLD 356
Cdd:cd08249 281 pedrefgEVFWKYLPELLEEGKLKPHPVRVVEGGLEGVQEGLD 323
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
 25-252 1.75e-14

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 74.14  E-value: 1.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    25 APDELVIDIEWCGICGTDLHEYTDgpiffpEDGHTHeishnpLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEP-TGTC 103
Cdd:PLN02586  36 GDEDVTVKILYCGVCHSDLHTIKN------EWGFTR------YPIVPGHEIVGIVTKLGKNVKKFKEGDRVGVGViVGSC 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   104 RDryrwplspnvdkewCAACKKGYYNIC-----SYLGLCGAGVQS-GGFAERVVMNESHCYKVPDFVPLDVAAliqPLaV 177
Cdd:PLN02586 104 KS--------------CESCDQDLENYCpkmifTYNSIGHDGTKNyGGYSDMIVVDQHFVLRFPDNLPLDAGA---PL-L 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   178 CWHAIRVCEFK------AGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGARVY----DPTA-HAAK 246
Cdd:PLN02586 166 CAGITVYSPMKyygmtePGKHLGVAGLGGLGHVAVKIGKAFGLKVTVISSSSNKEDEAINRLGADSFlvstDPEKmKAAI 245


                 ....*.
gi 6319257   247 ESIDYL 252
Cdd:PLN02586 246 GTMDYI 251
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 1-289 2.02e-14

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: 73.77  E-value: 2.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAY--FGKGNIRFTNHLKEPHiVAPDELVIDIEWCGICGTDlheytdgpIFFPEDGHTHEIshnPLPQAMGHEMAGT 78
Cdd:cd08253   1 MRAIRYheFGAPDVLRLGDLPVPT-PGPGEVLVRVHASGVNPVD--------TYIRAGAYPGLP---PLPYVPGSDGAGV 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   79 VLEVGPGVKNLKVGDKVvveptgtcrdryrwplspnvdkewcaackkgyynicsYLGLCGAGVQSGGFAERVVMNESHCY 158
Cdd:cd08253  69 VEAVGEGVDGLKVGDRV-------------------------------------WLTNLGWGRRQGTAAEYVVVPADQLV 111

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  159 KVPDFVPLDV-AALIQPLAVCWHA-IRVCEFKAGSTALIIG-AGPIGLGTI-LALnAAGCKDI-VVSEPAKvrRELAEKM 233
Cdd:cd08253 112 PLPDGVSFEQgAALGIPALTAYRAlFHRAGAKAGETVLVHGgSGAVGHAAVqLAR-WAGARVIaTASSAEG--AELVRQA 188

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6319257  234 GAR-VYDptaHAAKESIDYLRSiADGGDGFDYTFDCSGlEVTLNAAIQCLTFRGTAV 289
Cdd:cd08253 189 GADaVFN---YRAEDLADRILA-ATAGQGVDVIIEVLA-NVNLAKDLDVLAPGGRIV 240
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 66-348 4.27e-13

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 69.34  E-value: 4.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257      66 PLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVveptgtcrdryrwplspnvdkewcaackkgyynicsylglcgaGVQSGG 145
Cdd:smart00829  21 PGEAVLGGECAGVVTRVGPGVTGLAVGDRVM-------------------------------------------GLAPGA 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257     146 FAERVVMNESHCYKVPDFVPLDVAALIqPLAVC--WHAIR-VCEFKAGSTALI-IGAGPIGLGTI-LALnAAGCKDIV-V 219
Cdd:smart00829  58 FATRVVTDARLVVPIPDGWSFEEAATV-PVVFLtaYYALVdLARLRPGESVLIhAAAGGVGQAAIqLAR-HLGAEVFAtA 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257     220 SEPAKvrRELAEKMG---ARVYDPTahaakeSIDYLRSI--ADGGDGFDYTFDC-SGlEvTLNAAIQCLTFRGTAVNLA- 292
Cdd:smart00829 136 GSPEK--RDFLRALGipdDHIFSSR------DLSFADEIlrATGGRGVDVVLNSlSG-E-FLDASLRCLAPGGRFVEIGk 205

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319257     293 --MWGHHKIqfsPMDITLHERKYTG----SMCyTHHD-----FEAVIEALEEGRI--------DIDRA----RHMITGR 348
Cdd:smart00829 206 rdIRDNSQL---AMAPFRPNVSYHAvdldALE-EGPDrirelLAEVLELFAEGVLrplpvtvfPISDAedafRYMQQGK 280
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 66-340 8.28e-13

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


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 69.10  E-value: 8.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   66 PLPQAMGH----EMAGTVLEVGPGVKNLKVGDKVVveptgtcrdryrwplsPNVDKEWCAACKKGYYNICSYlglcGAGV 141
Cdd:cd08276  52 PPPVKDPLiplsDGAGEVVAVGEGVTRFKVGDRVV----------------PTFFPNWLDGPPTAEDEASAL----GGPI 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  142 QsGGFAERVVMNESHCYKVPDFVPLDVAALIqPLA--VCWHAIRVCE-FKAGSTALIIGAGPIGLGTILALNAAGCKDIV 218
Cdd:cd08276 112 D-GVLAEYVVLPEEGLVRAPDHLSFEEAATL-PCAglTAWNALFGLGpLKPGDTVLVQGTGGVSLFALQFAKAAGARVIA 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  219 V-SEPAKvrRELAEKMGARvydptahaakESIDYlRSIAD---------GGDGFDYTfdcsgLEV----TLNAAIQCLTF 284
Cdd:cd08276 190 TsSSDEK--LERAKALGAD----------HVINY-RTTPDwgeevlkltGGRGVDHV-----VEVggpgTLAQSIKAVAP 251

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6319257  285 RGTAVNLAMWGHHKIQFSPMDITLHERKYTGSMCYTHHDFEAVIEALEEGRID--IDR 340
Cdd:cd08276 252 GGVISLIGFLSGFEAPVLLLPLLTKGATLRGIAVGSRAQFEAMNRAIEAHRIRpvIDR 309
sorbose_phosphate_red cd08238
L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, ...
 3-346 1.05e-12

L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, catalyzes the NADPH-dependent conversion of l-sorbose 1-phosphate to d-glucitol 6-phosphate in the metabolism of L-sorbose to (also converts d-fructose 1-phosphate to d-mannitol 6-phosphate). 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.


Pssm-ID: 176200 [Multi-domain]  Cd Length: 410  Bit Score: 69.01  E-value: 1.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    3 ALAYFGKGNIRF-TNHLKEPhivAPDELVIDIEWCGICGTDLHEYTDGPIF--FPEDGHTHeishnplPQAMGHEMAGTV 79
Cdd:cd08238   5 AWRMYGKGDLRLeKFELPEI---ADDEILVRVISDSLCFSTWKLALQGSDHkkVPNDLAKE-------PVILGHEFAGTI 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   80 LEVGPGVKN-LKVGDKVVVEPTGTCRDRYrwplspnvdkeWCAackkGY-YNICsylglcgagvqsGGFAERVV----MN 153
Cdd:cd08238  75 LKVGKKWQGkYKPGQRFVIQPALILPDGP-----------SCP----GYsYTYP------------GGLATYHIipneVM 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  154 ESHCYKVPDFVPLDVAALIQPLAvC----WHAIR---------VCEFKAGSTALIIG-AGPIGLGTI-LALNAA-GCKDI 217
Cdd:cd08238 128 EQDCLLIYEGDGYAEASLVEPLS-CvigaYTANYhlqpgeyrhRMGIKPGGNTAILGgAGPMGLMAIdYAIHGPiGPSLL 206

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  218 VVSEPAKVR--------RELAEKMGARVYDPTAHAAKESIDYLRSIAdGGDGFDYTF------DCSGLEVTLNAAIQCLT 283
Cdd:cd08238 207 VVTDVNDERlaraqrlfPPEAASRGIELLYVNPATIDDLHATLMELT-GGQGFDDVFvfvpvpELVEEADTLLAPDGCLN 285

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319257  284 FRGTAVNLAMWGHhkIQFSpmDITLHERKYTGSMCYTHHDFEAVIEALEEGRIDIDRarhMIT 346
Cdd:cd08238 286 FFAGPVDKNFSAP--LNFY--NVHYNNTHYVGTSGGNTDDMKEAIDLMAAGKLNPAR---MVT 341
PLN02827 PLN02827
Alcohol dehydrogenase-like
 26-281 1.42e-12

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 68.78  E-value: 1.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    26 PDELVIDIEWCGICGTDLHEYTDGPIFfpedghtheishnplPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTGTCRD 105
Cdd:PLN02827  37 PLEIRIKVVSTSLCRSDLSAWESQALF---------------PRIFGHEASGIVESIGEGVTEFEKGDHVLTVFTGECGS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   106 ryrwplspnvdkewCAACKKGYYNICSYLGLCGAGVQS--------------------GGFAERVVMNESHCYKVPDFVP 165
Cdd:PLN02827 102 --------------CRHCISGKSNMCQVLGLERKGVMHsdqktrfsikgkpvyhycavSSFSEYTVVHSGCAVKVDPLAP 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   166 LDVAALIQ-----PLAVCWhaiRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGARVYDP 240
Cdd:PLN02827 168 LHKICLLScgvaaGLGAAW---NVADVSKGSSVVIFGLGTVGLSVAQGAKLRGASQIIGVDINPEKAEKAKTFGVTDFIN 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 6319257   241 TAHAAKESIDYLRSIADGGDgfDYTFDCSGLEVTLNAAIQC 281
Cdd:PLN02827 245 PNDLSEPIQQVIKRMTGGGA--DYSFECVGDTGIATTALQS 283
PLN02740 PLN02740
Alcohol dehydrogenase-like
 28-317 1.84e-11

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 65.20  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    28 ELVIDIEWCGICGTDLHEYTDgpiffpedghTHEiSHNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTGTCRDry 107
Cdd:PLN02740  37 EVRIKILYTSICHTDLSAWKG----------ENE-AQRAYPRILGHEAAGIVESVGEGVEDLKAGDHVIPIFNGECGD-- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   108 rwplspnvdkewCAACKKGYYNICSYL------------GLCGAGVQSGG-----------FAERVVMNESHCYKVPDFV 164
Cdd:PLN02740 104 ------------CRYCKRDKTNLCETYrvdpfksvmvndGKTRFSTKGDGqpiyhflntstFTEYTVLDSACVVKIDPNA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   165 PLDVAALIQ-----PLAVCWHAIRVcefKAGSTALIIGAGPIGLGTILALNAAGCKDI--VVSEPAKVrrELAEKMGARV 237
Cdd:PLN02740 172 PLKKMSLLScgvstGVGAAWNTANV---QAGSSVAIFGLGAVGLAVAEGARARGASKIigVDINPEKF--EKGKEMGITD 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   238 YDPTAHAAKESIDYLRSIADGgdGFDYTFDCSG-LEVTLNAAIQCLTFRGTAVNLAMWGHHK-IQFSPMDItLHERKYTG 315
Cdd:PLN02740 247 FINPKDSDKPVHERIREMTGG--GVDYSFECAGnVEVLREAFLSTHDGWGLTVLLGIHPTPKmLPLHPMEL-FDGRSITG 323


                 ..
gi 6319257   316 SM 317
Cdd:PLN02740 324 SV 325
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 1-270 2.00e-11

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: 64.70  E-value: 2.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRA--LAYFGKGNIRFTNHLKEPHiVAPDELVIDIEWCGI--CGTDLHEYTDGPIFFPEdghtheishnpLPQAMGHEMA 76
Cdd:cd08244   1 MRAirLHEFGPPEVLVPEDVPDPV-PGPGQVRIAVAAAGVhfVDTQLRSGWGPGPFPPE-----------LPYVPGGEVA 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   77 GTVLEVGPGVKNLKVGDKVVVEptgtcrdryrwplspnvdkewcaackkgyynicsylglcgAGVQSGGFAERVVMNESH 156
Cdd:cd08244  69 GVVDAVGPGVDPAWLGRRVVAH----------------------------------------TGRAGGGYAELAVADVDS 108

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  157 CYKVPDFVPLDVA-ALIQPLAVCWHAIRVCEFKAGSTALIIGAGPiGLGTIL--ALNAAGCKDI-VVSEPAKVrrELAEK 232
Cdd:cd08244 109 LHPVPDGLDLEAAvAVVHDGRTALGLLDLATLTPGDVVLVTAAAG-GLGSLLvqLAKAAGATVVgAAGGPAKT--ALVRA 185

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 6319257  233 MGARVYdptahaakesIDYLRS-------IADGGDGFDYTFDCSG 270
Cdd:cd08244 186 LGADVA----------VDYTRPdwpdqvrEALGGGGVTVVLDGVG 220
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 25-290 4.75e-11

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


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 63.39  E-value: 4.75e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   25 APDELVIDIEWCGICGTDLHEYTDGPIFFPedghtheishnPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTgtcr 104
Cdd:cd08268  26 GAGEVLIRVEAIGLNRADAMFRRGAYIEPP-----------PLPARLGYEAAGVVEAVGAGVTGFAVGDRVSVIPA---- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  105 dryrwpLSPNvdkewcaackkgyynicsylglcgagvQSGGFAERVVMNESHCYKVPDFV-PLDVAALIQPLAVCWHA-I 182
Cdd:cd08268  91 ------ADLG---------------------------QYGTYAEYALVPAAAVVKLPDGLsFVEAAALWMQYLTAYGAlV 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  183 RVCEFKAGSTALIIGA-GPIGLGTIL--------------------ALNAAGCKDIVVSEPAKVRRELAEKMGAR----V 237
Cdd:cd08268 138 ELAGLRPGDSVLITAAsSSVGLAAIQianaagatviattrtsekrdALLALGAAHVIVTDEEDLVAEVLRITGGKgvdvV 217

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6319257  238 YDPTAHAAKEsiDYLRSIADGGDGFDYtfDCSGLEVT----LNAAIQCLTFRGTAVN 290
Cdd:cd08268 218 FDPVGGPQFA--KLADALAPGGTLVVY--GALSGEPTpfplKAALKKSLTFRGYSLD 270
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 66-297 5.09e-11

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 63.35  E-value: 5.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   66 PLPQAMGHEMAGTVLEVGPGVKNLKVGDKVvveptgtcrdryrwplspnvdkewcaackkgYYnicsylglCGAGV--QS 143
Cdd:cd08272  56 PLPAILGCDVAGVVEAVGEGVTRFRVGDEV-------------------------------YG--------CAGGLggLQ 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  144 GGFAERVVMNESHCYKVPDFVPLDVAALIqPLAV--CWHA-IRVCEFKAGSTALI-IGAGpiGLGTI---LALnAAGCKD 216
Cdd:cd08272  97 GSLAEYAVVDARLLALKPANLSMREAAAL-PLVGitAWEGlVDRAAVQAGQTVLIhGGAG--GVGHVavqLAK-AAGARV 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  217 IVVSEPAKvrRELAEKMGArvyDPTAHAAKESIDYlrsIAD--GGDGFDYTFDCSGLEvTLNAAIQCLTFRGTAVNLAMW 294
Cdd:cd08272 173 YATASSEK--AAFARSLGA---DPIIYYRETVVEY---VAEhtGGRGFDVVFDTVGGE-TLDASFEAVALYGRVVSILGG 243


                ...
gi 6319257  295 GHH 297
Cdd:cd08272 244 ATH 246
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
 69-238 7.87e-10

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: 60.12  E-value: 7.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   69 QAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTgtcrdryRWplspNVDKEWCAAckkGYYNICSYLGLCGAGVQSGGFAE 148
Cdd:cd08246  83 HIGGSDASGIVWAVGEGVKNWKVGDEVVVHCS-------VW----DGNDPERAG---GDPMFDPSQRIWGYETNYGSFAQ 148

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  149 RVVMNESHCYKVPDFVPLDVAA---LIQPLA----VCWHAIRVcefKAGSTALIIGAGPiGLGTI---LALNAAGCKDIV 218
Cdd:cd08246 149 FALVQATQLMPKPKHLSWEEAAaymLVGATAyrmlFGWNPNTV---KPGDNVLIWGASG-GLGSMaiqLARAAGANPVAV 224

                       170       180
                ....*....|....*....|
gi 6319257  219 VSEPAKvrRELAEKMGARVY 238
Cdd:cd08246 225 VSSEEK--AEYCRALGAEGV 242
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 25-286 9.35e-10

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: 59.58  E-value: 9.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   25 APDELVIDIEWCGICGTDLHeYTDGpIFFPEdghtheishNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVeptgtcr 104
Cdd:cd08250  29 GPGEVLVKNRFVGINASDIN-FTAG-RYDPG---------VKPPFDCGFEGVGEVVAVGEGVTDFKVGDAVAT------- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  105 dryrwplspnvdkewcaackkgyynicsylglcgagVQSGGFAERVVMNESHCYKVP----DFVPLDVAALIQPLAVcwh 180
Cdd:cd08250  91 ------------------------------------MSFGAFAEYQVVPARHAVPVPelkpEVLPLLVSGLTASIAL--- 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  181 aIRVCEFKAGSTALIIGAGPiGLGTILA--LNAAGCKDI-VVSEPAKVrrELAEKMGArvyDPTAHAAKESID-YLRSia 256
Cdd:cd08250 132 -EEVGEMKSGETVLVTAAAG-GTGQFAVqlAKLAGCHVIgTCSSDEKA--EFLKSLGC---DRPINYKTEDLGeVLKK-- 202

                       250       260       270
                ....*....|....*....|....*....|
gi 6319257  257 DGGDGFDYTFDCSGLEvTLNAAIQCLTFRG 286
Cdd:cd08250 203 EYPKGVDVVYESVGGE-MFDTCVDNLALKG 231
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 66-343 4.15e-09

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: 57.67  E-value: 4.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   66 PLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVvePTGTcrdryrwplspnvdkewcaackkgyynicsylglcgagvqSGG 145
Cdd:cd05282  55 PLPAVPGNEGVGVVVEVGSGVSGLLVGQRVL--PLGG----------------------------------------EGT 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  146 FAERVVMNESHCYKVPDFVPLDVAA--LIQPLAV---CWHAIRVCEFKagstALIIGAGPIGLGTILA--LNAAGCKDIV 218
Cdd:cd05282  93 WQEYVVAPADDLIPVPDSISDEQAAmlYINPLTAwlmLTEYLKLPPGD----WVIQNAANSAVGRMLIqlAKLLGFKTIN 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  219 VsepakVRR-ELAEKMGARVYDPTAHAAKESIDylRSIAD--GGDGFDYTFDCSGLEVTlNAAIQCLTFRGTAVNLAMWG 295
Cdd:cd05282 169 V-----VRRdEQVEELKALGADEVIDSSPEDLA--QRVKEatGGAGARLALDAVGGESA-TRLARSLRPGGTLVNYGLLS 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6319257  296 HHKIQFSP-----MDITL---HERKYTGSMCYT--HHDFEAVIEALEEGRIDIDRARH 343
Cdd:cd05282 241 GEPVPFPRsvfifKDITVrgfWLRQWLHSATKEakQETFAEVIKLVEAGVLTTPVGAK 298
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 67-292 7.83e-09

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: 56.90  E-value: 7.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   67 LPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEptgtcrdryrwplspnvdkewcaackkgyynicsylglcGAGVQSGGF 146
Cdd:cd08271  56 YPHVPGVDGAGVVVAVGAKVTGWKVGDRVAYH---------------------------------------ASLARGGSF 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  147 AERVVMNESHCYKVPDFVPLDVAALIQ-PLAVCWHAI-RVCEFKAGSTALIIGAGPiGLGTILA--LNAAGCKDIVVSEP 222
Cdd:cd08271  97 AEYTVVDARAVLPLPDSLSFEEAAALPcAGLTAYQALfKKLRIEAGRTILITGGAG-GVGSFAVqlAKRAGLRVITTCSK 175

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319257  223 AKVrrELAEKMGAR-VYD-PTAHAAKESIDYLrsiadGGDGFDYTFDCSGLEVTLNAAiQCLTFRGTAVNLA 292
Cdd:cd08271 176 RNF--EYVKSLGADhVIDyNDEDVCERIKEIT-----GGRGVDAVLDTVGGETAAALA-PTLAFNGHLVCIQ 239
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-289 2.19e-08

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: 55.35  E-value: 2.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    1 MRALAYFGKGNI----RFTNHLKEPhivAPDELVIDIEWCGICGTDL----HEYTDGPiffpedghtheishnPLPQAMG 72
Cdd:cd08273   1 NREVVVTRRGGPevlkVVEADLPEP---AAGEVVVKVEASGVSFADVqmrrGLYPDQP---------------PLPFTPG 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   73 HEMAGTVLEVGPGVKNLKVGDKVVveptgtcrdryrwplspnvdkewcaackkgyynicsylglcgAGVQSGGFAERVVM 152
Cdd:cd08273  63 YDLVGRVDALGSGVTGFEVGDRVA------------------------------------------ALTRVGGNAEYINL 100

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  153 NESHCYKVPDfvPLDVAAliqplAVC--------WHAI-RVCEFKAGSTALIIGA-GPIGLGTIlalnaagckdivvsep 222
Cdd:cd08273 101 DAKYLVPVPE--GVDAAE-----AVClvlnyvtaYQMLhRAAKVLTGQRVLIHGAsGGVGQALL---------------- 157

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  223 akvrrELAEKMGARVYDpTAHAAKES---------IDY------LRSIADGgdGFDYTFDCSGLEvTLNAAIQCLTFRGT 287
Cdd:cd08273 158 -----ELALLAGAEVYG-TASERNHAalrelgatpIDYrtkdwlPAMLTPG--GVDVVFDGVGGE-SYEESYAALAPGGT 228


                ..
gi 6319257  288 AV 289
Cdd:cd08273 229 LV 230
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 26-274 3.40e-08

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: 54.90  E-value: 3.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   26 PDELVIDIEWCGICGTDLheytdgpifFPEDGHTHeiSHNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVveptgtcrd 105
Cdd:cd08275  26 SGEVRVRVEACGLNFADL---------MARQGLYD--SAPKPPFVPGFECAGTVEAVGEGVKDFKVGDRVM--------- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  106 ryrwplspnvdkewcaackkgyynicsylglcgAGVQSGGFAERVVMNESHCYKVPDFVPLDVAA--LIQPLAVcWHAIR 183
Cdd:cd08275  86 ---------------------------------GLTRFGGYAEVVNVPADQVFPLPDGMSFEEAAafPVNYLTA-YYALF 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  184 -VCEFKAGSTALI-IGAGPIGLgtilalnAAG--CK---DIVV---SEPAKVrrELAEKMGAR-VYDptahaaKESIDYL 252
Cdd:cd08275 132 eLGNLRPGQSVLVhSAAGGVGL-------AAGqlCKtvpNVTVvgtASASKH--EALKENGVThVID------YRTQDYV 196

                       250       260
                ....*....|....*....|...
gi 6319257  253 RSIAD-GGDGFDYTFDCSGLEVT 274
Cdd:cd08275 197 EEVKKiSPEGVDIVLDALGGEDT 219
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 1-379 6.20e-08

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 53.88  E-value: 6.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257     1 MRALAYFGKGNIRfTNHLKEPHIVAP--DELVIDIEWCGICGTDLHEYTDGpiFFPEDGHTheishnplpQAMGHEMAGT 78
Cdd:PTZ00354   2 MRAVTLKGFGGVD-VLKIGESPKPAPkrNDVLIKVSAAGVNRADTLQRQGK--YPPPPGSS---------EILGLEVAGY 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    79 VLEVGPGVKNLKVGDKVVveptgtcrdryrwplspnvdkewcaackkgyynicsylglcgAGVQSGGFAERVVMNESHCY 158
Cdd:PTZ00354  70 VEDVGSDVKRFKEGDRVM------------------------------------------ALLPGGGYAEYAVAHKGHVM 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   159 KVPDFVPLDVAALIqPLA--VCWHAI-RVCEFKAGSTALI-IGAGPIGLGTILALNAAGCKDIV-VSEPAKVrrELAEKM 233
Cdd:PTZ00354 108 HIPQGYTFEEAAAI-PEAflTAWQLLkKHGDVKKGQSVLIhAGASGVGTAAAQLAEKYGAATIItTSSEEKV--DFCKKL 184

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   234 GARVYDPTAHAAKESIDYLRSIadGGDGFDYTFDCSGLE-VTLNAAIqcLTFRGTAVNLAMWGHHKIqfSPMDIT--LHE 310
Cdd:PTZ00354 185 AAIILIRYPDEEGFAPKVKKLT--GEKGVNLVLDCVGGSyLSETAEV--LAVDGKWIVYGFMGGAKV--EKFNLLplLRK 258

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   311 R-KYTGSMCYTHHD---------FE-AVIEALEEGRIDIdrarhmITGRV-NIEDGLDGaiMKLINEKESTIKIILTPNN 378
Cdd:PTZ00354 259 RaSIIFSTLRSRSDeykadlvasFErEVLPYMEEGEIKP------IVDRTyPLEEVAEA--HTFLEQNKNIGKVVLTVNE 330


                 .
gi 6319257   379 H 379
Cdd:PTZ00354 331 P 331
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 67-270 1.51e-06

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: 49.91  E-value: 1.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   67 LPQAMGHEMAGTVLEVGPGVKNLKVGDKVvveptgtcrdryrwplspnvdkeWCAAckkgyynicsylglcgAGVQSGGF 146
Cdd:cd08248  73 FPLTLGRDCSGVVVDIGSGVKSFEIGDEV-----------------------WGAV----------------PPWSQGTH 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  147 AERVVMNESHCYKVPDFVPLDVAALIqPLAVC--WHAI-RVC----EFKAGSTALIIGA-GPIGLGTILALNAAGCKdIV 218
Cdd:cd08248 114 AEYVVVPENEVSKKPKNLSHEEAASL-PYAGLtaWSALvNVGglnpKNAAGKRVLILGGsGGVGTFAIQLLKAWGAH-VT 191

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  219 VSEPAKVrRELAEKMGarvydptahaAKESIDY--------LRSIadggDGFDYTFDCSG 270
Cdd:cd08248 192 TTCSTDA-IPLVKSLG----------ADDVIDYnnedfeeeLTER----GKFDVILDTVG 236
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
 27-293 1.64e-06

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 49.64  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    27 DELVIDIEWCGICGTDLHEYTDGPIFfpedghtheishNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEP-TGTCrd 105
Cdd:PLN02178  32 NDVTVKILFCGVCHSDLHTIKNHWGF------------SRYPIIPGHEIVGIATKVGKNVTKFKEGDRVGVGViIGSC-- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   106 ryrwplspnvdkEWCAACKKGYYNIC-----SYLGLCGAGVQS-GGFAERVVMNESHCYKVPDFVPLDVAAliqPLaVCW 179
Cdd:PLN02178  98 ------------QSCESCNQDLENYCpkvvfTYNSRSSDGTRNqGGYSDVIVVDHRFVLSIPDGLPSDSGA---PL-LCA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   180 HAIRVCEFK-------AGSTALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRRELAEKMGARVYDPTAHAAKesidyl 252
Cdd:PLN02178 162 GITVYSPMKyygmtkeSGKRLGVNGLGGLGHIAVKIGKAFGLRVTVISRSSEKEREAIDRLGADSFLVTTDSQK------ 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 6319257   253 rsIADGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAM 293
Cdd:PLN02178 236 --MKEAVGTMDFIIDTVSAEHALLPLFSLLKVSGKLVALGL 274
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 63-295 1.24e-05

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: 46.65  E-value: 1.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   63 SHNPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVeptgtcrdryrwplspnvdkewcaackkgyynicsylglcGAGVQ 142
Cdd:cd08251  33 TMPPYPFTPGFEASGVVRAVGPHVTRLAVGDEVIA----------------------------------------GTGES 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  143 SGGFAERVVMNESHCYKVPDFVPL-DVAALIQPLAVCWHAIRVCEFKAGSTALIIGAgpiglgtilalnAAGCKDIVVse 221
Cdd:cd08251  73 MGGHATLVTVPEDQVVRKPASLSFeEACALPVVFLTVIDAFARAGLAKGEHILIQTA------------TGGTGLMAV-- 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  222 pakvrrELAEKMGARVYDPTAHAAKesIDYLRSIadggdGFDYTFDC---------------SGLEVTLNA----AIQ-- 280
Cdd:cd08251 139 ------QLARLKGAEIYATASSDDK--LEYLKQL-----GVPHVINYveedfeeeimrltggRGVDVVINTlsgeAIQkg 205

                       250
                ....*....|....*..
gi 6319257  281 --CLTFRGTAVNLAMWG 295
Cdd:cd08251 206 lnCLAPGGRYVEIAMTA 222
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 65-101 3.03e-05

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: 45.67  E-value: 3.03e-05
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 6319257   65 NPLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPTG 101
Cdd:cd08290  61 PEPPAVGGNEGVGEVVKVGSGVKSLKPGDWVIPLRPG 97
PRK10754 PRK10754
NADPH:quinone reductase;
67-96 1.54e-04

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 43.57  E-value: 1.54e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 6319257    67 LPQAMGHEMAGTVLEVGPGVKNLKVGDKVV 96
Cdd:PRK10754  57 LPSGLGTEAAGVVSKVGSGVKHIKVGDRVV 86
Glu_dehyd_C pfam16912
Glucose dehydrogenase C-terminus;
167-353 1.84e-04

Glucose dehydrogenase C-terminus;


Pssm-ID: 407146 [Multi-domain]  Cd Length: 211  Bit Score: 42.32  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    167 DVAALIQPLAVCWHAIRVCEfKAGS-------TALIIGAGPIGLGTILALNAAGCKDIVVSEPAKVRR----ELAEKMGA 235
Cdd:pfam16912   2 DVGFLVEPLSIVEKAIEHAE-ASRSrfewrprSALVLGNGPLGLLALAMLRVQRGFDRVYCLGRRDRPdptiDLVEELGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257    236 rvydpTAHAAKESidYLRSIADGGDGFDYTFDCSGLEVTLNAAIQCLTFRGTAVNLAMWGHHKIQFSP----MDITLHER 311
Cdd:pfam16912  81 -----TYVDSRET--PVDEIPAAHEPMDLVYEATGYAPHAFEAIDALAPNGVAALLGVPTSWTFEIDGgalhRELVLHNK 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 6319257    312 KYTGSMCYTHHDFEAVIEALeeGRIDIDRARHMITGRVNIED 353
Cdd:pfam16912 154 ALVGSVNANRRHFEAAADTL--AAAPEWFLDALVTGVVPLDE 193
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
 167-239 2.18e-04

Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439939 [Multi-domain]  Cd Length: 270  Bit Score: 42.82  E-value: 2.18e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319257  167 DVAALIQPLAvcwhaiRVCEFKAGSTALIIGAGPIGLGTILALNAAGCKDIVVS--EPAKVrRELAEKMGARVYD 239
Cdd:COG0169 104 DGIGFVRALR------EAGVDLAGKRVLVLGAGGAARAVAAALAEAGAAEITIVnrTPERA-EALAARLGVRAVP 171
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 189-240 4.88e-04

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 39.86  E-value: 4.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6319257    189 AGSTALIIGAGPIGLGTILALNAAGCKDIVVSE--PAKVrRELAEKMGARVYDP 240
Cdd:pfam01488  11 KDKKVLLIGAGEMGELVAKHLLAKGAKEVTIANrtIERA-QELAEKFGGVEALP 63
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
 66-213 7.98e-04

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


Pssm-ID: 176252 [Multi-domain]  Cd Length: 324  Bit Score: 41.16  E-value: 7.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257   66 PLPQAMGHEMAGTVLEVGPGVKNLKVGDKVVVEPtgtcrdryrwplspnvdkewcaackkgyynicsylglcgagvQSGG 145
Cdd:cd08292  57 ELPAIGGSEAVGVVDAVGEGVKGLQVGQRVAVAP------------------------------------------VHGT 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319257  146 FAERVVMNESHCYKVPDFVPLDVAA--LIQPLavcwhairvcefkagSTALIIGAGPIGLGTILALNAAG 213
Cdd:cd08292  95 WAEYFVAPADGLVPLPDGISDEVAAqlIAMPL---------------SALMLLDFLGVKPGQWLIQNAAG 149
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 190-250 9.33e-04

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 39.56  E-value: 9.33e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319257  190 GSTALIIGAGPIGLGTILALNAAGCKDIVVS--EPAKvRRELAEKMGARVYDPTAHAAKESID 250
Cdd:cd01065  19 GKKVLILGAGGAARAVAYALAELGAAKIVIVnrTLEK-AKALAERFGELGIAIAYLDLEELLA 80
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 189-237 3.15e-03

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 39.40  E-value: 3.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6319257   189 AGSTALIIGAGPIGLGTILALNAAGCKDIVVS----EPAKvrrELAEKMGARV 237
Cdd:PRK00045 181 SGKKVLVIGAGEMGELVAKHLAEKGVRKITVAnrtlERAE---ELAEEFGGEA 230
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 189-239 5.37e-03

Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440142 [Multi-domain]  Cd Length: 425  Bit Score: 38.94  E-value: 5.37e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6319257  189 AGSTALIIGAGPIGLGTILALNAAGCKDIVVS----EPAkvrRELAEKMGARVYD 239
Cdd:COG0373 181 SGKTVLVIGAGEMGELAARHLAAKGVKRITVAnrtlERA---EELAEEFGGEAVP 232
 
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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