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Conserved domains on  [gi|15242240|ref|NP_200010|]
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GroES-like zinc-binding alcohol dehydrogenase family protein [Arabidopsis thaliana]

Protein Classification

NAD(P)-dependent alcohol dehydrogenase( domain architecture ID 11477070)

NAD(P)(H)-dependent alcohol dehydrogenase exhibits specificity for NAD(P)(H) as a cofactor in the interconversion of alcohols and aldehydes or ketones

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02702 PLN02702
L-idonate 5-dehydrogenase
1-364 0e+00

L-idonate 5-dehydrogenase


:

Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 756.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240    1 MGKGGMSQGEGSKVEEENMAAWLVGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHE 80
Cdd:PLN02702   1 MGKGGMSSGEGSGVEEENMAAWLVGVNTLKIQPFKLPPLGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   81 CAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCREGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEE 160
Cdd:PLN02702  81 CAGIIEEVGSEVKHLVVGDRVALEPGISCWRCNLCKEGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  161 GAMCEPLSVGVHACRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTNLEDV 240
Cdd:PLN02702 161 GAMCEPLSVGVHACRRANIGPETNVLVMGAGPIGLVTMLAARAFGAPRIVIVDVDDERLSVAKQLGADEIVLVSTNIEDV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  241 GSEVEQIQKAMGSNIDVTFDCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRYKNTWPLCLE 320
Cdd:PLN02702 241 ESEVEEIQKAMGGGIDVSFDCVGFNKTMSTALEATRAGGKVCLVGMGHNEMTVPLTPAAAREVDVVGVFRYRNTWPLCLE 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 15242240  321 FLTSGKIDVKPLITHRFGFSQKEVEDAFETSARGSNAIKVMFNL 364
Cdd:PLN02702 321 FLRSGKIDVKPLITHRFGFSQKEVEEAFETSARGGNAIKVMFNL 364
 
Name Accession Description Interval E-value
PLN02702 PLN02702
L-idonate 5-dehydrogenase
1-364 0e+00

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 756.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240    1 MGKGGMSQGEGSKVEEENMAAWLVGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHE 80
Cdd:PLN02702   1 MGKGGMSSGEGSGVEEENMAAWLVGVNTLKIQPFKLPPLGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   81 CAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCREGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEE 160
Cdd:PLN02702  81 CAGIIEEVGSEVKHLVVGDRVALEPGISCWRCNLCKEGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  161 GAMCEPLSVGVHACRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTNLEDV 240
Cdd:PLN02702 161 GAMCEPLSVGVHACRRANIGPETNVLVMGAGPIGLVTMLAARAFGAPRIVIVDVDDERLSVAKQLGADEIVLVSTNIEDV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  241 GSEVEQIQKAMGSNIDVTFDCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRYKNTWPLCLE 320
Cdd:PLN02702 241 ESEVEEIQKAMGGGIDVSFDCVGFNKTMSTALEATRAGGKVCLVGMGHNEMTVPLTPAAAREVDVVGVFRYRNTWPLCLE 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 15242240  321 FLTSGKIDVKPLITHRFGFSQKEVEDAFETSARGSNAIKVMFNL 364
Cdd:PLN02702 321 FLRSGKIDVKPLITHRFGFSQKEVEEAFETSARGGNAIKVMFNL 364
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
20-363 0e+00

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: 534.77  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  20 AAWLVGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGD 99
Cdd:cd05285   1 AAVLHGPGDLRLEERPIPEPGPGEVLVRVRAVGICGSDVHYYKHGRIGDFVVKEPMVLGHESAGTVVAVGSGVTHLKVGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 100 RVALEPGISCWRCNLCREGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEV 179
Cdd:cd05285  81 RVAIEPGVPCRTCEFCKSGRYNLCPDMRFAATPPVDGTLCRYVNHPADFCHKLPDNVSLEEGALVEPLSVGVHACRRAGV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 180 GPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVGSEVEQIQKAMGSN-IDVT 258
Cdd:cd05285 161 RPGDTVLVFGAGPIGLLTAAVAKAFGATKVVVTDIDPSRLEFAKELGATHTVNVRT--EDTPESAEKIAELLGGKgPDVV 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 259 FDCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRYKNTWPLCLEFLTSGKIDVKPLITHRFG 338
Cdd:cd05285 239 IECTGAESCIQTAIYATRPGGTVVLVGMGKPEVTLPLSAASLREIDIRGVFRYANTYPTAIELLASGKVDVKPLITHRFP 318
                       330       340
                ....*....|....*....|....*.
gi 15242240 339 FsqKEVEDAFETSARGSN-AIKVMFN 363
Cdd:cd05285 319 L--EDAVEAFETAAKGKKgVIKVVIE 342
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
20-362 4.25e-126

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: 365.62  E-value: 4.25e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  20 AAWLVGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTmrcADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGD 99
Cdd:COG1063   3 ALVLHGPGDLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRG---GYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 100 RVALEPGISCWRCNLCREGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEV 179
Cdd:COG1063  80 RVVVEPNIPCGECRYCRRGRYNLCENLQFLGIAGRDGGFAEYVRVPAANLVKVPDGLSDEAAALVEPLAVALHAVERAGV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 180 GPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVGSEVEQIqkAMGSNIDVTF 259
Cdd:COG1063 160 KPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARELGADAVVNPRE--EDLVEAVREL--TGGRGADVVI 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 260 DCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRY-KNTWPLCLEFLTSGKIDVKPLITHRFG 338
Cdd:COG1063 236 EAVGAPAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYtREDFPEALELLASGRIDLEPLITHRFP 315
                       330       340
                ....*....|....*....|....*
gi 15242240 339 FSqkEVEDAFETSA-RGSNAIKVMF 362
Cdd:COG1063 316 LD--DAPEAFEAAAdRADGAIKVVL 338
tdh TIGR00692
L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme ...
36-364 1.83e-57

L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme of threonine catabolism. Closely related proteins include sorbitol dehydrogenase, xylitol dehydrogenase, and benzyl alcohol dehydrogenase. Eukaryotic examples of this enzyme have been demonstrated experimentally but do not appear in database search results.E. coli His-90 modulates substrate specificity and is believed part of the active site. [Energy metabolism, Amino acids and amines]


Pssm-ID: 129775 [Multi-domain]  Cd Length: 340  Bit Score: 190.07  E-value: 1.83e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240    36 LPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLC 115
Cdd:TIGR00692  18 VPEPGPGEVLIKVLATSICGTDVHIYNWDEWAQSRIKPPQVVGHEVAGEVVGIGPGVEGIKVGDYVSVETHIVCGKCYAC 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   116 REGRYNLCPEMKFFA--TPpvhGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEVGPETnVLVMGAGPI 193
Cdd:TIGR00692  98 RRGQYHVCQNTKIFGvdTD---GCFAEYAVVPAQNIWKNPKSIPPEYATIQEPLGNAVHTVLAGPISGKS-VLVTGAGPI 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   194 GLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVGSEVEQIqkAMGSNIDVTFDCAGFNKTMSTALA 273
Cdd:TIGR00692 174 GLMAIAVAKASGAYPVIVSDPNEYRLELAKKMGATYVVNPFK--EDVVKEVADL--TDGEGVDVFLEMSGAPKALEQGLQ 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   274 ATRCGGKVCLVGMGHGIMTVPLTPAAA-REVDVVGVFRYK--NTWPLCLEFLTSGKIDVKPLITHRFGFsqKEVEDAFET 350
Cdd:TIGR00692 250 AVTPGGRVSLLGLPPGKVTIDFTNKVIfKGLTIYGITGRHmfETWYTVSRLIQSGKLDLDPIITHKFKF--DKFEKGFEL 327
                         330
                  ....*....|....
gi 15242240   351 SARGSNAiKVMFNL 364
Cdd:TIGR00692 328 MRSGQTG-KVILSL 340
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
42-151 8.11e-39

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: 133.89  E-value: 8.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240    42 HDVRVRMKAVGICGSDVHYLKTMrcaDFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCREGRYN 121
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGG---NPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYN 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 15242240   122 LCPEMKFFATpPVHGSLANQVVHPADLCFK 151
Cdd:pfam08240  78 LCPNGRFLGY-DRDGGFAEYVVVPERNLVP 106
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
46-162 1.01e-12

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 67.80  E-value: 1.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240     46 VRMKAVGICGSDVhyLKTMRcadfVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVAlepGIscwrcnlcregrynlcpe 125
Cdd:smart00829   1 IEVRAAGLNFRDV--LIALG----LYPGEAVLGGECAGVVTRVGPGVTGLAVGDRVM---GL------------------ 53
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 15242240    126 mkffatppVHGSLANQVVHPADLCFKLPENVSLEEGA 162
Cdd:smart00829  54 --------APGAFATRVVTDARLVVPIPDGWSFEEAA 82
 
Name Accession Description Interval E-value
PLN02702 PLN02702
L-idonate 5-dehydrogenase
1-364 0e+00

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 756.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240    1 MGKGGMSQGEGSKVEEENMAAWLVGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHE 80
Cdd:PLN02702   1 MGKGGMSSGEGSGVEEENMAAWLVGVNTLKIQPFKLPPLGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   81 CAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCREGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEE 160
Cdd:PLN02702  81 CAGIIEEVGSEVKHLVVGDRVALEPGISCWRCNLCKEGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  161 GAMCEPLSVGVHACRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTNLEDV 240
Cdd:PLN02702 161 GAMCEPLSVGVHACRRANIGPETNVLVMGAGPIGLVTMLAARAFGAPRIVIVDVDDERLSVAKQLGADEIVLVSTNIEDV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  241 GSEVEQIQKAMGSNIDVTFDCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRYKNTWPLCLE 320
Cdd:PLN02702 241 ESEVEEIQKAMGGGIDVSFDCVGFNKTMSTALEATRAGGKVCLVGMGHNEMTVPLTPAAAREVDVVGVFRYRNTWPLCLE 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 15242240  321 FLTSGKIDVKPLITHRFGFSQKEVEDAFETSARGSNAIKVMFNL 364
Cdd:PLN02702 321 FLRSGKIDVKPLITHRFGFSQKEVEEAFETSARGGNAIKVMFNL 364
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
20-363 0e+00

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: 534.77  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  20 AAWLVGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGD 99
Cdd:cd05285   1 AAVLHGPGDLRLEERPIPEPGPGEVLVRVRAVGICGSDVHYYKHGRIGDFVVKEPMVLGHESAGTVVAVGSGVTHLKVGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 100 RVALEPGISCWRCNLCREGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEV 179
Cdd:cd05285  81 RVAIEPGVPCRTCEFCKSGRYNLCPDMRFAATPPVDGTLCRYVNHPADFCHKLPDNVSLEEGALVEPLSVGVHACRRAGV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 180 GPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVGSEVEQIQKAMGSN-IDVT 258
Cdd:cd05285 161 RPGDTVLVFGAGPIGLLTAAVAKAFGATKVVVTDIDPSRLEFAKELGATHTVNVRT--EDTPESAEKIAELLGGKgPDVV 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 259 FDCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRYKNTWPLCLEFLTSGKIDVKPLITHRFG 338
Cdd:cd05285 239 IECTGAESCIQTAIYATRPGGTVVLVGMGKPEVTLPLSAASLREIDIRGVFRYANTYPTAIELLASGKVDVKPLITHRFP 318
                       330       340
                ....*....|....*....|....*.
gi 15242240 339 FsqKEVEDAFETSARGSN-AIKVMFN 363
Cdd:cd05285 319 L--EDAVEAFETAAKGKKgVIKVVIE 342
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
20-362 4.25e-126

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: 365.62  E-value: 4.25e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  20 AAWLVGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTmrcADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGD 99
Cdd:COG1063   3 ALVLHGPGDLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRG---GYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 100 RVALEPGISCWRCNLCREGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEV 179
Cdd:COG1063  80 RVVVEPNIPCGECRYCRRGRYNLCENLQFLGIAGRDGGFAEYVRVPAANLVKVPDGLSDEAAALVEPLAVALHAVERAGV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 180 GPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVGSEVEQIqkAMGSNIDVTF 259
Cdd:COG1063 160 KPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARELGADAVVNPRE--EDLVEAVREL--TGGRGADVVI 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 260 DCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRY-KNTWPLCLEFLTSGKIDVKPLITHRFG 338
Cdd:COG1063 236 EAVGAPAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYtREDFPEALELLASGRIDLEPLITHRFP 315
                       330       340
                ....*....|....*....|....*
gi 15242240 339 FSqkEVEDAFETSA-RGSNAIKVMF 362
Cdd:COG1063 316 LD--DAPEAFEAAAdRADGAIKVVL 338
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
25-361 7.59e-102

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: 304.16  E-value: 7.59e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  25 GINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALE 104
Cdd:cd08232   5 AAGDLRVEERPAPEPGPGEVRVRVAAGGICGSDLHYYQHGGFGTVRLREPMVLGHEVSGVVEAVGPGVTGLAPGQRVAVN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 105 PGISCWRCNLCREGRYNLCPEMKFFA----TPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEVG 180
Cdd:cd08232  85 PSRPCGTCDYCRAGRPNLCLNMRFLGsamrFPHVQGGFREYLVVDASQCVPLPDGLSLRRAALAEPLAVALHAVNRAGDL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 181 PETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVqvttnleDVGSEVEQIQKAMGSNIDVTFD 260
Cdd:cd08232 165 AGKRVLVTGAGPIGALVVAAARRAGAAEIVATDLADAPLAVARAMGADETV-------NLARDPLAAYAADKGDFDVVFE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 261 CAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRYKNTWPLCLEFLTSGKIDVKPLITHRFGFS 340
Cdd:cd08232 238 ASGAPAALASALRVVRPGGTVVQVGMLGGPVPLPLNALVAKELDLRGSFRFDDEFAEAVRLLAAGRIDVRPLITAVFPLE 317
                       330       340
                ....*....|....*....|.
gi 15242240 341 qkEVEDAFETSARGSNAIKVM 361
Cdd:cd08232 318 --EAAEAFALAADRTRSVKVQ 336
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
19-362 6.84e-95

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: 286.43  E-value: 6.84e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  19 MAAW-LVGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVH-YLKTMRcadfvVKEPMVIGHECAGIIEEVGEEVKHLV 96
Cdd:cd08236   1 MKALvLTGPGDLRYEDIPKPEPGPGEVLVKVKACGICGSDIPrYLGTGA-----YHPPLVLGHEFSGTVEEVGSGVDDLA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  97 VGDRVALEPGISCWRCNLCREGRYNLCPEMKFFATPpVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRR 176
Cdd:cd08236  76 VGDRVAVNPLLPCGKCEYCKKGEYSLCSNYDYIGSR-RDGAFAEYVSVPARNLIKIPDHVDYEEAAMIEPAAVALHAVRL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 177 AEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTT-NLEDVGSEVEqiqkamGSNI 255
Cdd:cd08236 155 AGITLGDTVVVIGAGTIGLLAIQWLKILGAKRVIAVDIDDEKLAVARELGADDTINPKEeDVEKVRELTE------GRGA 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 256 DVTFDCAGFNKTMSTALAATRCGGKVCLVGMGHGimTVPLTPAAA-----REVDVVGVFRYKNT------WPLCLEFLTS 324
Cdd:cd08236 229 DLVIEAAGSPATIEQALALARPGGKVVLVGIPYG--DVTLSEEAFekilrKELTIQGSWNSYSApfpgdeWRTALDLLAS 306
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 15242240 325 GKIDVKPLITHRFGFSqkEVEDAFETSARGSNA-IKVMF 362
Cdd:cd08236 307 GKIKVEPLITHRLPLE--DGPAAFERLADREEFsGKVLL 343
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
20-363 3.95e-85

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: 260.92  E-value: 3.95e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  20 AAWLVGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKtmrcADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGD 99
Cdd:cd08234   3 ALVYEGPGELEVEEVPVPEPGPDEVLIKVAACGICGTDLHIYE----GEFGAAPPLVPGHEFAGVVVAVGSKVTGFKVGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 100 RVALEPGISCWRCNLCREGRYNLCPEMKFFATPpVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEV 179
Cdd:cd08234  79 RVAVDPNIYCGECFYCRRGRPNLCENLTAVGVT-RNGGFAEYVVVPAKQVYKIPDNLSFEEAALAEPLSCAVHGLDLLGI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 180 GPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTNledvgsEVEQIQKAMGSNIDVTF 259
Cdd:cd08234 158 KPGDSVLVFGAGPIGLLLAQLLKLNGASRVTVAEPNEEKLELAKKLGATETVDPSRE------DPEAQKEDNPYGFDVVI 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 260 DCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTP--AAAREVDVVGVFRYKNTWPLCLEFLTSGKIDVKPLITHRF 337
Cdd:cd08234 232 EATGVPKTLEQAIEYARRGGTVLVFGVYAPDARVSISPfeIFQKELTIIGSFINPYTFPRAIALLESGKIDVKGLVSHRL 311
                       330       340
                ....*....|....*....|....*.
gi 15242240 338 GFSqkEVEDAFEtSARGSNAIKVMFN 363
Cdd:cd08234 312 PLE--EVPEALE-GMRSGGALKVVVV 334
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
37-360 4.68e-83

(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: 256.31  E-value: 4.68e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  37 PSVGPHDVRVRMKAVGICGSDVH-YLktmrcaD---FVVKE----------PMVIGHECAGIIEEVGEEVKHLVVGDRVA 102
Cdd:cd08233  20 PPVKPGEVKIKVAWCGICGSDLHeYL------DgpiFIPTEghphltgetaPVTLGHEFSGVVVEVGSGVTGFKVGDRVV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 103 LEPGISCWRCNLCREGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEVGPE 182
Cdd:cd08233  94 VEPTIKCGTCGACKRGLYNLCDSLGFIGLGGGGGGFAEYVVVPAYHVHKLPDNVPLEEAALVEPLAVAWHAVRRSGFKPG 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 183 TNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVGSEVEQIQKamGSNIDVTFDCA 262
Cdd:cd08233 174 DTALVLGAGPIGLLTILALKAAGASKIIVSEPSEARRELAEELGATIVLDPTE--VDVVAEVRKLTG--GGGVDVSFDCA 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 263 GFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRY-KNTWPLCLEFLTSGKIDVKPLITHRFGFSQ 341
Cdd:cd08233 250 GVQATLDTAIDALRPRGTAVNVAIWEKPISFNPNDLVLKEKTLTGSICYtREDFEEVIDLLASGKIDAEPLITSRIPLED 329
                       330       340
                ....*....|....*....|
gi 15242240 342 KeVEDAFETSARG-SNAIKV 360
Cdd:cd08233 330 I-VEKGFEELINDkEQHVKI 348
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
37-361 5.29e-78

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: 242.86  E-value: 5.29e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  37 PSVGPHDVRVRMKAVGICGSDVHylkTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCR 116
Cdd:cd08261  20 PVPGAGEVLVRVKRVGICGSDLH---IYHGRNPFASYPRILGHELSGEVVEVGEGVAGLKVGDRVVVDPYISCGECYACR 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 117 EGRYNLCPEMKFFAtppVH--GSLANQVVHPADlCFKLPENVSLEEGAMCEPLSVGVHACRRAEVGPETNVLVMGAGPIG 194
Cdd:cd08261  97 KGRPNCCENLQVLG---VHrdGGFAEYIVVPAD-ALLVPEGLSLDQAALVEPLAIGAHAVRRAGVTAGDTVLVVGAGPIG 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 195 LVTMLAARAFSVpRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVGSEVEQIqkAMGSNIDVTFDCAGFNKTMSTALAA 274
Cdd:cd08261 173 LGVIQVAKARGA-RVIVVDIDDERLEFARELGADDTINVGD--EDVAARLREL--TDGEGADVVIDATGNPASMEEAVEL 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 275 TRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRYKNT-WPLCLEFLTSGKIDVKPLITHRFGFSqkEVEDAFET-SA 352
Cdd:cd08261 248 VAHGGRVVLVGLSKGPVTFPDPEFHKKELTILGSRNATREdFPDVIDLLESGKVDPEALITHRFPFE--DVPEAFDLwEA 325

                ....*....
gi 15242240 353 RGSNAIKVM 361
Cdd:cd08261 326 PPGGVIKVL 334
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
20-361 1.50e-77

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: 242.12  E-value: 1.50e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  20 AAWLVGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVhylKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGD 99
Cdd:cd08235   3 AAVLHGPNDVRLEEVPVPEPGPGEVLVKVRACGICGTDV---KKIRGGHTDLKPPRILGHEIAGEIVEVGDGVTGFKVGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 100 RVALEPGISCWRCNLCREGRYNLCPEMK--FFATPpvhGSLANQVVHPA-----DLCFKLPENVSLEEGAMCEPLSVGVH 172
Cdd:cd08235  80 RVFVAPHVPCGECHYCLRGNENMCPNYKkfGNLYD---GGFAEYVRVPAwavkrGGVLKLPDNVSFEEAALVEPLACCIN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 173 ACRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVGSEVEQIQKAMG 252
Cdd:cd08235 157 AQRKAGIKPGDTVLVIGAGPIGLLHAMLAKASGARKVIVSDLNEFRLEFAKKLGADYTIDAAE--EDLVEKVRELTDGRG 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 253 snIDVTFDCAGFNKTMSTALAATRCGGKVCLV-GMGHGiMTVPLTPAA--AREVDVVGVFR-----YKNTwplcLEFLTS 324
Cdd:cd08235 235 --ADVVIVATGSPEAQAQALELVRKGGRILFFgGLPKG-STVNIDPNLihYREITITGSYAaspedYKEA----LELIAS 307
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 15242240 325 GKIDVKPLITHRFGFsqKEVEDAFETsARGSNAIKVM 361
Cdd:cd08235 308 GKIDVKDLITHRFPL--EDIEEAFEL-AADGKSLKIV 341
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
29-349 1.13e-72

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 229.23  E-value: 1.13e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  29 LKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKtmrcADF-VVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGI 107
Cdd:COG1064  13 LELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAE----GEWpVPKLPLVPGHEIVGRVVAVGPGVTGFKVGDRVGVGWVD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 108 SCWRCNLCREGRYNLCPEMKFFATpPVHGSLANQVVHPADLCFKLPENVSLEEGA--MCePLSVGVHACRRAEVGPETNV 185
Cdd:COG1064  89 SCGTCEYCRSGRENLCENGRFTGY-TTDGGYAEYVVVPARFLVKLPDGLDPAEAAplLC-AGITAYRALRRAGVGPGDRV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 186 LVMGAGPIGLVTMLAARAFSVpRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVgseVEQIQKAMGsnIDVTFDCAGFN 265
Cdd:COG1064 167 AVIGAGGLGHLAVQIAKALGA-EVIAVDRSPEKLELARELGADHVVNSSD--EDP---VEAVRELTG--ADVVIDTVGAP 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 266 KTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRY-KNTWPLCLEFLTSGKIDVkplITHRFGFSqkEV 344
Cdd:COG1064 239 ATVNAALALLRRGGRLVLVGLPGGPIPLPPFDLILKERSIRGSLIGtRADLQEMLDLAAEGKIKP---EVETIPLE--EA 313

                ....*
gi 15242240 345 EDAFE 349
Cdd:COG1064 314 NEALE 318
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
43-322 1.15e-70

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: 221.81  E-value: 1.15e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  43 DVRVRMKAVGICGSDVHYLKTMRcaDFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCREgrynl 122
Cdd:cd05188   1 EVLVRVEAAGLCGTDLHIRRGGY--PPPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNLGCGTCELCRE----- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 123 CPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAM-CEPLSVGVHACRRAE-VGPETNVLVMGAGPIGLVTMLA 200
Cdd:cd05188  74 LCPGGGILGEGLDGGFAEYVVVPADNLVPLPDGLSLEEAALlPEPLATAYHALRRAGvLKPGDTVLVLGAGGVGLLAAQL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 201 ARAFSvPRIVIVDVDENRLAVAKQLGADEIVQVTTNledvgSEVEQIQKAMGSNIDVTFDCAGFNKTMSTALAATRCGGK 280
Cdd:cd05188 154 AKAAG-ARVIVTDRSDEKLELAKELGADHVIDYKEE-----DLEEELRLTGGGGADVVIDAVGGPETLAQALRLLRPGGR 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15242240 281 VCLVGMGHGIMTVP-LTPAAAREVDVVGVFRY-KNTWPLCLEFL 322
Cdd:cd05188 228 IVVVGGTSGGPPLDdLRRLLFKELTIIGSTGGtREDFEEALDLL 271
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
37-325 6.78e-68

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: 216.03  E-value: 6.78e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  37 PSVGPHDVRVRMKAVGICGSDVHylkTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEP-GISCWRCNLC 115
Cdd:cd08258  22 PEPGPGEVLIKVAAAGICGSDLH---IYKGDYDPVETPVVLGHEFSGTIVEVGPDVEGWKVGDRVVSETtFSTCGRCPYC 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 116 REGRYNLCPEMKFFATPpVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHAC-RRAEVGPETNVLVMGAGPIG 194
Cdd:cd08258  99 RRGDYNLCPHRKGIGTQ-ADGGFAEYVLVPEESLHELPENLSLEAAALTEPLAVAVHAVaERSGIRPGDTVVVFGPGPIG 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 195 LVTMLAARAFSVpRIVIVDV--DENRLAVAKQLGADeivQVTTNLEDVGSEVEQIQKamGSNIDVTFDCAGFNKTMSTAL 272
Cdd:cd08258 178 LLAAQVAKLQGA-TVVVVGTekDEVRLDVAKELGAD---AVNGGEEDLAELVNEITD--GDGADVVIECSGAVPALEQAL 251
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15242240 273 AATRCGGKVCLVGMGhGIMTVPLTPAAA--REVDVVGVFRYKNT-WPLCLEFLTSG 325
Cdd:cd08258 252 ELLRKGGRIVQVGIF-GPLAASIDVERIiqKELSVIGSRSSTPAsWETALRLLASG 306
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
29-357 1.09e-62

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 204.16  E-value: 1.09e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  29 LKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFvvkePMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGIS 108
Cdd:COG1062   4 LEIEEVELDEPRPGEVLVRIVAAGLCHSDLHVRDGDLPVPL----PAVLGHEGAGVVEEVGPGVTGVAPGDHVVLSFIPS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 109 CWRCNLCREGRYNLCpeMKFFA----------TPPVH-------------GSLANQVVHPADLCFKLPENVSLEEGAmce 165
Cdd:COG1062  80 CGHCRYCASGRPALC--EAGAAlngkgtlpdgTSRLSsadgepvghffgqSSFAEYAVVPERSVVKVDKDVPLELAA--- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 166 PLSVGVH-----ACRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIvqVTTNLEDV 240
Cdd:COG1062 155 LLGCGVQtgagaVLNTAKVRPGDTVAVFGLGGVGLSAVQGARIAGASRIIAVDPVPEKLELARELGATHT--VNPADEDA 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 241 gseVEQIQKAMGSNIDVTFDCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPA--AAREVDVVGVF--------- 309
Cdd:COG1062 233 ---VEAVRELTGGGVDYAFETTGNPAVIRQALEALRKGGTVVVVGLAPPGAEISLDPFqlLLTGRTIRGSYfggavprrd 309
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 15242240 310 --RYkntwplcLEFLTSGKIDVKPLITHRFGFSQkeVEDAFETSARGSNA 357
Cdd:COG1062 310 ipRL-------VDLYRAGRLPLDELITRRYPLDE--INEAFDDLRSGEVI 350
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
40-360 1.94e-62

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: 203.28  E-value: 1.94e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  40 GPHDVRVRMKAVGICGSDVHylkTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCREGR 119
Cdd:cd05278  24 GPHDAIVRVTATSICGSDLH---IYRGGVPGAKHGMILGHEFVGEVVEVGSDVKRLKPGDRVSVPCITFCGRCRFCRRGY 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 120 YNLC----PEMKFFATPPvhGSLANQVVHP-ADL-CFKLPENVSLEEGAMC-EPLSVGVHACRRAEVGPETNVLVMGAGP 192
Cdd:cd05278 101 HAHCenglWGWKLGNRID--GGQAEYVRVPyADMnLAKIPDGLPDEDALMLsDILPTGFHGAELAGIKPGSTVAVIGAGP 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 193 IGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIvqVTTNLEDVGSEVEQIQKamGSNIDVTFDCAGFNKTMSTAL 272
Cdd:cd05278 179 VGLCAVAGARLLGAARIIAVDSNPERLDLAKEAGATDI--INPKNGDIVEQILELTG--GRGVDCVIEAVGFEETFEQAV 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 273 AATRCGGKVCLVGM-GHGIMTVPLTPAAAREVDV-VGVFRYKNTWPLCLEFLTSGKIDVKPLITHRFGFSQkeVEDAFET 350
Cdd:cd05278 255 KVVRPGGTIANVGVyGKPDPLPLLGEWFGKNLTFkTGLVPVRARMPELLDLIEEGKIDPSKLITHRFPLDD--ILKAYRL 332
                       330
                ....*....|.
gi 15242240 351 -SARGSNAIKV 360
Cdd:cd05278 333 fDNKPDGCIKV 343
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
20-364 2.44e-62

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: 202.55  E-value: 2.44e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  20 AAWLVGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYL-KTMRCADFvvkEPMVIGHECAGIIEEVGEEVKHLVVG 98
Cdd:cd08239   3 GAVFPGDRTVELREFPVPVPGPGEVLLRVKASGLCGSDLHYYyHGHRAPAY---QGVIPGHEPAGVVVAVGPGVTHFRVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  99 DRVALEPGISCWRCNLCREGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAMcepLSVGV----HAC 174
Cdd:cd08239  80 DRVMVYHYVGCGACRNCRRGWMQLCTSKRAAYGWNRDGGHAEYMLVPEKTLIPLPDDLSFADGAL---LLCGIgtayHAL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 175 RRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIvqVTTNLEDVgSEVEQIQKAMGSn 254
Cdd:cd08239 157 RRVGVSGRDTVLVVGAGPVGLGALMLARALGAEDVIGVDPSPERLELAKALGADFV--INSGQDDV-QEIRELTSGAGA- 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 255 iDVTFDCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFrYKNTWPL--CLEFLTSGKIDVKPL 332
Cdd:cd08239 233 -DVAIECSGNTAARRLALEAVRPWGRLVLVGEGGELTIEVSNDLIRKQRTLIGSW-YFSVPDMeeCAEFLARHKLEVDRL 310
                       330       340       350
                ....*....|....*....|....*....|..
gi 15242240 333 ITHRFGFSQkeVEDAFETSARGSnAIKVMFNL 364
Cdd:cd08239 311 VTHRFGLDQ--APEAYALFAQGE-SGKVVFVF 339
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
42-360 2.53e-60

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 197.60  E-value: 2.53e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   42 HDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVgeEVKHLVVGDRVALEPGISCWRCNLCREGRYN 121
Cdd:PRK09880  28 NGTLVQITRGGICGSDLHYYQEGKVGNFVIKAPMVLGHEVIGKIVHS--DSSGLKEGQTVAINPSKPCGHCKYCLSHNEN 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  122 LCPEMKFFA----TPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEVGPETNVLVMGAGPIGLVT 197
Cdd:PRK09880 106 QCTTMRFFGsamyFPHVDGGFTRYKVVDTAQCIPYPEKADEKVMAFAEPLAVAIHAAHQAGDLQGKRVFVSGVGPIGCLI 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  198 MLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTnledvgSEVEQIQKAMGSnIDVTFDCAGFNKTMSTALAATRC 277
Cdd:PRK09880 186 VAAVKTLGAAEIVCADVSPRSLSLAREMGADKLVNPQN------DDLDHYKAEKGY-FDVSFEVSGHPSSINTCLEVTRA 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  278 GGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRYKNTWPLCLEFLTSGKIDVKPLITHRFGFSQkeVEDAFETSARGSNA 357
Cdd:PRK09880 259 KGVMVQVGMGGAPPEFPMMTLIVKEISLKGSFRFTEEFNTAVSWLANGVINPLPLLSAEYPFTD--LEEALIFAGDKTQA 336

                 ...
gi 15242240  358 IKV 360
Cdd:PRK09880 337 AKV 339
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
37-364 2.95e-60

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: 197.46  E-value: 2.95e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  37 PSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCR 116
Cdd:cd05281  21 PKPGPGEVLIKVLAASICGTDVHIYEWDEWAQSRIKPPLIFGHEFAGEVVEVGEGVTRVKVGDYVSAETHIVCGKCYQCR 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 117 EGRYNLCPEMKFFAtppVH--GSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEVgPETNVLVMGAGPIG 194
Cdd:cd05281 101 TGNYHVCQNTKILG---VDtdGCFAEYVVVPEENLWKNDKDIPPEIASIQEPLGNAVHTVLAGDV-SGKSVLITGCGPIG 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 195 LVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVttnLEDVGSEVEQIQKAMGsnIDVTFDCAGFNKTMSTALAA 274
Cdd:cd05281 177 LMAIAVAKAAGASLVIASDPNPYRLELAKKMGADVVINP---REEDVVEVKSVTDGTG--VDVVLEMSGNPKAIEQGLKA 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 275 TRCGGKVCLVGMGHGIMTVPLTPAAA-REVDVVGVFRYK--NTWPLCLEFLTSGKIDVKPLITHRFGFsqKEVEDAFETS 351
Cdd:cd05281 252 LTPGGRVSILGLPPGPVDIDLNNLVIfKGLTVQGITGRKmfETWYQVSALLKSGKVDLSPVITHKLPL--EDFEEAFELM 329
                       330
                ....*....|...
gi 15242240 352 ARGsNAIKVMFNL 364
Cdd:cd05281 330 RSG-KCGKVVLYP 341
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
37-363 1.25e-58

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 193.12  E-value: 1.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   37 PSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCR 116
Cdd:PRK05396  21 PEPGPNDVLIKVKKTAICGTDVHIYNWDEWAQKTIPVPMVVGHEFVGEVVEVGSEVTGFKVGDRVSGEGHIVCGHCRNCR 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  117 EGRYNLCPEMKFFAtppVH--GSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEVGPETnVLVMGAGPIG 194
Cdd:PRK05396 101 AGRRHLCRNTKGVG---VNrpGAFAEYLVIPAFNVWKIPDDIPDDLAAIFDPFGNAVHTALSFDLVGED-VLITGAGPIG 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  195 LVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVT-TNLEDVGSEVEqiqkaMGSNIDVTFDCAGFNKTMSTALA 273
Cdd:PRK05396 177 IMAAAVAKHVGARHVVITDVNEYRLELARKMGATRAVNVAkEDLRDVMAELG-----MTEGFDVGLEMSGAPSAFRQMLD 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  274 ATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRYK--NTWPLCLEFLTSGkIDVKPLITHRFGFsqKEVEDAFETS 351
Cdd:PRK05396 252 NMNHGGRIAMLGIPPGDMAIDWNKVIFKGLTIKGIYGREmfETWYKMSALLQSG-LDLSPIITHRFPI--DDFQKGFEAM 328
                        330
                 ....*....|..
gi 15242240  352 ARGsNAIKVMFN 363
Cdd:PRK05396 329 RSG-QSGKVILD 339
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
37-354 1.20e-57

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: 190.54  E-value: 1.20e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  37 PSVGPHDVRVRMKAVGICGSDVHYLkTMRcADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCR 116
Cdd:cd08254  22 PEPGPGEVLVKVKAAGVCHSDLHIL-DGG-VPTLTKLPLTLGHEIAGTVVEVGAGVTNFKVGDRVAVPAVIPCGACALCR 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 117 EGRYNLCPEMKFFATpPVHGSLANQVVHPAD-LCfKLPENVSLEEGA-MCEPLSVGVHAC-RRAEVGPETNVLVMGAGPI 193
Cdd:cd08254 100 RGRGNLCLNQGMPGL-GIDGGFAEYIVVPARaLV-PVPDGVPFAQAAvATDAVLTPYHAVvRAGEVKPGETVLVIGLGGL 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 194 GLVTMLAARAFSVpRIVIVDVDENRLAVAKQLGADEivqVTTNLEDvgSEVEQIQKAMGSNIDVTFDCAGFNKTMSTALA 273
Cdd:cd08254 178 GLNAVQIAKAMGA-AVIAVDIKEEKLELAKELGADE---VLNSLDD--SPKDKKAAGLGGGFDVIFDFVGTQPTFEDAQK 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 274 ATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRY-KNTWPLCLEFLTSGKIDvkPLITHRfgfSQKEVEDAFETSA 352
Cdd:cd08254 252 AVKPGGRIVVVGLGRDKLTVDLSDLIARELRIIGSFGGtPEDLPEVLDLIAKGKLD--PQVETR---PLDEIPEVLERLH 326

                ..
gi 15242240 353 RG 354
Cdd:cd08254 327 KG 328
tdh TIGR00692
L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme ...
36-364 1.83e-57

L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme of threonine catabolism. Closely related proteins include sorbitol dehydrogenase, xylitol dehydrogenase, and benzyl alcohol dehydrogenase. Eukaryotic examples of this enzyme have been demonstrated experimentally but do not appear in database search results.E. coli His-90 modulates substrate specificity and is believed part of the active site. [Energy metabolism, Amino acids and amines]


Pssm-ID: 129775 [Multi-domain]  Cd Length: 340  Bit Score: 190.07  E-value: 1.83e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240    36 LPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLC 115
Cdd:TIGR00692  18 VPEPGPGEVLIKVLATSICGTDVHIYNWDEWAQSRIKPPQVVGHEVAGEVVGIGPGVEGIKVGDYVSVETHIVCGKCYAC 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   116 REGRYNLCPEMKFFA--TPpvhGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEVGPETnVLVMGAGPI 193
Cdd:TIGR00692  98 RRGQYHVCQNTKIFGvdTD---GCFAEYAVVPAQNIWKNPKSIPPEYATIQEPLGNAVHTVLAGPISGKS-VLVTGAGPI 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   194 GLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVGSEVEQIqkAMGSNIDVTFDCAGFNKTMSTALA 273
Cdd:TIGR00692 174 GLMAIAVAKASGAYPVIVSDPNEYRLELAKKMGATYVVNPFK--EDVVKEVADL--TDGEGVDVFLEMSGAPKALEQGLQ 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   274 ATRCGGKVCLVGMGHGIMTVPLTPAAA-REVDVVGVFRYK--NTWPLCLEFLTSGKIDVKPLITHRFGFsqKEVEDAFET 350
Cdd:TIGR00692 250 AVTPGGRVSLLGLPPGKVTIDFTNKVIfKGLTIYGITGRHmfETWYTVSRLIQSGKLDLDPIITHKFKF--DKFEKGFEL 327
                         330
                  ....*....|....
gi 15242240   351 SARGSNAiKVMFNL 364
Cdd:TIGR00692 328 MRSGQTG-KVILSL 340
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
20-357 2.55e-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: 182.74  E-value: 2.55e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  20 AAWLVGIN-TLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKtmrcADFVVKEPMVIGHECAGIIEEVGEEVKHLVVG 98
Cdd:cd08279   3 AAVLHEVGkPLEIEEVELDDPGPGEVLVRIAAAGLCHSDLHVVT----GDLPAPLPAVLGHEGAGVVEEVGPGVTGVKPG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  99 DRVALEPGISCWRCNLCREGRYNLCPE------MKFFATP--------PVH-----GSLANQVVHPADLCFKLPENVSLE 159
Cdd:cd08279  79 DHVVLSWIPACGTCRYCSRGQPNLCDLgagilgGQLPDGTrrftadgePVGamcglGTFAEYTVVPEASVVKIDDDIPLD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 160 EGAMcepLSVGV-----HACRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVT 234
Cdd:cd08279 159 RAAL---LGCGVttgvgAVVNTARVRPGDTVAVIGCGGVGLNAIQGARIAGASRIIAVDPVPEKLELARRFGATHTVNAS 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 235 TnlEDVGSEVEQIQKAMGsnIDVTFDCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPA--AAREVDVVGVF--- 309
Cdd:cd08279 236 E--DDAVEAVRDLTDGRG--ADYAFEAVGRAATIRQALAMTRKGGTAVVVGMGPPGETVSLPALelFLSEKRLQGSLygs 311
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 15242240 310 -RYKNTWPLCLEFLTSGKIDVKPLITHRFGFSQkeVEDAFETSARGSNA 357
Cdd:cd08279 312 aNPRRDIPRLLDLYRAGRLKLDELVTRRYSLDE--INEAFADMLAGENA 358
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
37-360 8.17e-54

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: 181.07  E-value: 8.17e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  37 PSVGPHDVRVRMKAVGICGSDvhyLKTMRCADFV---------VKEPMVIGHECAGIIEEVGEEVKH--LVVGDRVALEP 105
Cdd:cd08256  20 PRPGPGEILVKVEACGICAGD---IKCYHGAPSFwgdenqppyVKPPMIPGHEFVGRVVELGEGAEErgVKVGDRVISEQ 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 106 GISCWRCNLCREGRYNLCPEMKFFA-TPPVHGSLANQVVHPAD-LCFKLPENVSLEEGAMCEPLSVGVHACRRAEVGPET 183
Cdd:cd08256  97 IVPCWNCRFCNRGQYWMCQKHDLYGfQNNVNGGMAEYMRFPKEaIVHKVPDDIPPEDAILIEPLACALHAVDRANIKFDD 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 184 NVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADeivqVTTNLEDVGSEVEQIQKAMGSNIDVTFDCAG 263
Cdd:cd08256 177 VVVLAGAGPLGLGMIGAARLKNPKKLIVLDLKDERLALARKFGAD----VVLNPPEVDVVEKIKELTGGYGCDIYIEATG 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 264 FNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAR-EVDVVGVFRYKNTWPLCLEFLTSGKIDVKPLITHRfgFSQK 342
Cdd:cd08256 253 HPSAVEQGLNMIRKLGRFVEFSVFGDPVTVDWSIIGDRkELDVLGSHLGPYCYPIAIDLIASGRLPTDGIVTHQ--FPLE 330
                       330
                ....*....|....*...
gi 15242240 343 EVEDAFETSARGSNAIKV 360
Cdd:cd08256 331 DFEEAFELMARGDDSIKV 348
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
20-307 7.97e-52

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: 175.44  E-value: 7.97e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  20 AAWLVGINT-LKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVG 98
Cdd:cd05284   3 AARLYEYGKpLRLEDVPVPEPGPGQVLVRVGGAGVCHSDLHVIDGVWGGILPYKLPFTLGHENAGWVEEVGSGVDGLKEG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  99 DRVALEPGISCWRCNLCREGRYNLCPEMKFfatPPV--HGSLANQVVHPADLCFKLPENVSLEEGAmcePLS-VGV---H 172
Cdd:cd05284  83 DPVVVHPPWGCGTCRYCRRGEENYCENARF---PGIgtDGGFAEYLLVPSRRLVKLPRGLDPVEAA---PLAdAGLtayH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 173 ACRRA--EVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTtnlEDVGSEVEQIQKA 250
Cdd:cd05284 157 AVKKAlpYLDPGSTVVVIGVGGLGHIAVQILRALTPATVIAVDRSEEALKLAERLGADHVLNAS---DDVVEEVRELTGG 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15242240 251 MGsnIDVTFDCAGFNKTMSTALAATRCGGKVCLVGMGhGIMTVPLTPAAAREVDVVG 307
Cdd:cd05284 234 RG--ADAVIDFVGSDETLALAAKLLAKGGRYVIVGYG-GHGRLPTSDLVPTEISVIG 287
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
24-360 9.45e-52

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: 175.52  E-value: 9.45e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  24 VGINTLKIQPFLLPSV-GPHDVRVRMKAVGICGSDVHYLKtmrcADFV-VKEPMVIGHECAGIIEEVGEEVKHLVVGDRV 101
Cdd:cd08286   7 HGPGKISWEDRPKPTIqEPTDAIVKMLKTTICGTDLHILK----GDVPtVTPGRILGHEGVGVVEEVGSAVTNFKVGDRV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 102 ALEPGISCWRCNLCREGRYNLCPEMKFFATPPVHGSLANQVVHP-ADLC-FKLPENVSLEEGAMCEPLSVGVHAC--RRA 177
Cdd:cd08286  83 LISCISSCGTCGYCRKGLYSHCESGGWILGNLIDGTQAEYVRIPhADNSlYKLPEGVDEEAAVMLSDILPTGYECgvLNG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 178 EVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVGSEVEQIQKAMGsnIDV 257
Cdd:cd08286 163 KVKPGDTVAIVGAGPVGLAALLTAQLYSPSKIIMVDLDDNRLEVAKKLGATHTVNSAK--GDAIEQVLELTDGRG--VDV 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 258 TFDCAGFNKTMSTALAATRCGGKVCLVGMgHGI-MTVPLTPAAAREVDVVGVFRYKNTWPLCLEFLTSGKIDVKPLITHR 336
Cdd:cd08286 239 VIEAVGIPATFELCQELVAPGGHIANVGV-HGKpVDLHLEKLWIKNITITTGLVDTNTTPMLLKLVSSGKLDPSKLVTHR 317
                       330       340
                ....*....|....*....|....*.
gi 15242240 337 FGFSqkEVEDAFETS--ARGSNAIKV 360
Cdd:cd08286 318 FKLS--EIEKAYDTFsaAAKHKALKV 341
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
37-361 6.36e-51

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: 173.26  E-value: 6.36e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  37 PSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPM--------VIGHECAGIIEEVGEEVKH-LVVGDRVALEPGI 107
Cdd:cd08262  19 PEPGPGQVLVKVLACGICGSDLHATAHPEAMVDDAGGPSlmdlgadiVLGHEFCGEVVDYGPGTERkLKVGTRVTSLPLL 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 108 SCWRCNLCREGRYNLCPemkffatppvhGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEVGPETNVLV 187
Cdd:cd08262  99 LCGQGASCGIGLSPEAP-----------GGYAEYMLLSEALLLRVPDGLSMEDAALTEPLAVGLHAVRRARLTPGEVALV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 188 MGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTNLEDVGSEVEQIQKAMGSNiDVTFDCAGFNKT 267
Cdd:cd08262 168 IGCGPIGLAVIAALKARGVGPIVASDFSPERRALALAMGADIVVDPAADSPFAAWAAELARAGGPKP-AVIFECVGAPGL 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 268 MSTALAATRCGGKVCLVGM-GHGIMTVPLTpAAAREVDVVGVFRY-KNTWPLCLEFLTSGKIDVKPLITHRFGFSqkEVE 345
Cdd:cd08262 247 IQQIIEGAPPGGRIVVVGVcMESDNIEPAL-AIRKELTLQFSLGYtPEEFADALDALAEGKVDVAPMVTGTVGLD--GVP 323
                       330
                ....*....|....*.
gi 15242240 346 DAFETSARGSNAIKVM 361
Cdd:cd08262 324 DAFEALRDPEHHCKIL 339
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
18-360 1.19e-49

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: 170.13  E-value: 1.19e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  18 NMAAWLVGINT-LKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCAdfvVKEPMVIGHECAGIIEEVGEEV---- 92
Cdd:cd08231   1 ARAAVLTGPGKpLEIREVPLPDLEPGAVLVRVRLAGVCGSDVHTVAGRRPR---VPLPIILGHEGVGRVVALGGGVttdv 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  93 --KHLVVGDRVALEPGISCWRCNLCREGRYNLCPEMKFF------ATPPVHGSLANQVVHPADLCF-KLPENVSLE--EG 161
Cdd:cd08231  78 agEPLKVGDRVTWSVGAPCGRCYRCLVGDPTKCENRKKYgheascDDPHLSGGYAEHIYLPPGTAIvRVPDNVPDEvaAP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 162 AMCePLSVGVHACRRA-EVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDV 240
Cdd:cd08231 158 ANC-ALATVLAALDRAgPVGAGDTVVVQGAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAREFGADATIDIDE--LPD 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 241 GSEVEQIQKAMGSN-IDVTFDCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAA--REVDVVGVFRYKntwPL 317
Cdd:cd08231 235 PQRRAIVRDITGGRgADVVIEASGHPAAVPEGLELLRRGGTYVLVGSVAPAGTVPLDPERIvrKNLTIIGVHNYD---PS 311
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 15242240 318 CL----EFL--TSGKIDVKPLITHRfgFSQKEVEDAFEtSARGSNAIKV 360
Cdd:cd08231 312 HLyravRFLerTQDRFPFAELVTHR--YPLEDINEALE-LAESGTALKV 357
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
39-362 1.54e-49

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: 169.36  E-value: 1.54e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  39 VGPHDVRVRMKAVGICGSDVHYLKtmrcADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCREG 118
Cdd:cd08284  23 QDPTDAIVKVTAAAICGSDLHIYR----GHIPSTPGFVLGHEFVGEVVEVGPEVRTLKVGDRVVSPFTIACGECFYCRRG 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 119 RYNLCPEMKFF---ATPPVHGSLANQVVHP-ADL-CFKLPENVSLEEG-AMCEPLSVGVHACRRAEVGPETNVLVMGAGP 192
Cdd:cd08284  99 QSGRCAKGGLFgyaGSPNLDGAQAEYVRVPfADGtLLKLPDGLSDEAAlLLGDILPTGYFGAKRAQVRPGDTVAVIGCGP 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 193 IGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGAdeivqVTTNLEDvGSEVEQIQKAM-GSNIDVTFDCAGFNKTMSTA 271
Cdd:cd08284 179 VGLCAVLSAQVLGAARVFAVDPVPERLERAAALGA-----EPINFED-AEPVERVREATeGRGADVVLEAVGGAAALDLA 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 272 LAATRCGGKVCLVGMGH-GIMTVPLTPAAAREVDV-VGVFRYKNTWPLCLEFLTSGKIDVKPLITHRFGFSqkEVEDAFE 349
Cdd:cd08284 253 FDLVRPGGVISSVGVHTaEEFPFPGLDAYNKNLTLrFGRCPVRSLFPELLPLLESGRLDLEFLIDHRMPLE--EAPEAYR 330
                       330
                ....*....|...
gi 15242240 350 TSARGSnAIKVMF 362
Cdd:cd08284 331 LFDKRK-VLKVVL 342
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
20-349 1.02e-47

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: 165.11  E-value: 1.02e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  20 AAWLVGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHylkTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGD 99
Cdd:cd08285   3 AFAMLGIGKVGWIEKPIPVCGPNDAIVRPTAVAPCTSDVH---TVWGGAPGERHGMILGHEAVGVVEEVGSEVKDFKPGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 100 RVALEPGISCWRCNLCREGRYNLCPEM----KFfaTPPVHGSLANQV-VHPADLCF-KLPENVSLEEGAMC-EPLSVGVH 172
Cdd:cd08285  80 RVIVPAITPDWRSVAAQRGYPSQSGGMlggwKF--SNFKDGVFAEYFhVNDADANLaPLPDGLTDEQAVMLpDMMSTGFH 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 173 ACRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTtnledVGSEVEQIQKAM- 251
Cdd:cd08285 158 GAELANIKLGDTVAVFGIGPVGLMAVAGARLRGAGRIIAVGSRPNRVELAKEYGATDIVDYK-----NGDVVEQILKLTg 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 252 GSNIDVTFDCAGFNKTMSTALAATRCGGKV-CLVGMGHGIMtVPLtpaaAREVDVVGVFRYKNTWPLC----------LE 320
Cdd:cd08285 233 GKGVDAVIIAGGGQDTFEQALKVLKPGGTIsNVNYYGEDDY-LPI----PREEWGVGMGHKTINGGLCpggrlrmerlAS 307
                       330       340
                ....*....|....*....|....*....
gi 15242240 321 FLTSGKIDVKPLITHRFgFSQKEVEDAFE 349
Cdd:cd08285 308 LIEYGRVDPSKLLTHHF-FGFDDIEEALM 335
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
21-355 1.62e-47

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: 164.92  E-value: 1.62e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  21 AWLVG----INTLKIQPfllPsvGPHDVRVRMKAVGICGSDVHYLKtmrcADFVVKEPMVIGHECAGIIEEVGEEVKHLV 96
Cdd:cd05279   6 LWEKGkplsIEEIEVAP---P--KAGEVRIKVVATGVCHTDLHVID----GKLPTPLPVILGHEGAGIVESIGPGVTTLK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  97 VGDRVALEPGISCWRCNLCREGRYNLCpeMKFFATP-----------------PVH-----GSLANQVVHPADLCFKLPE 154
Cdd:cd05279  77 PGDKVIPLFGPQCGKCKQCLNPRPNLC--SKSRGTNgrglmsdgtsrftckgkPIHhflgtSTFAEYTVVSEISLAKIDP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 155 NVSLEEGAM--CePLSVGVHAC-RRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIV 231
Cdd:cd05279 155 DAPLEKVCLigC-GFSTGYGAAvNTAKVTPGSTCAVFGLGGVGLSVIMGCKAAGASRIIAVDINKDKFEKAKQLGATECI 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 232 QVTTNLEDVgseVEQIQKAMGSNIDVTFDCAGFNKTMSTALAATRCGGKVC-LVGMGHGIMTVPLTPAAARE-----VDV 305
Cdd:cd05279 234 NPRDQDKPI---VEVLTEMTDGGVDYAFEVIGSADTLKQALDATRLGGGTSvVVGVPPSGTEATLDPNDLLTgrtikGTV 310
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 15242240 306 VGVFRYKNTWPLCLEFLTSGKIDVKPLITHRFGFsqKEVEDAFETSARGS 355
Cdd:cd05279 311 FGGWKSKDSVPKLVALYRQKKFPLDELITHVLPF--EEINDGFDLMRSGE 358
PRK10083 PRK10083
putative oxidoreductase; Provisional
27-349 2.14e-47

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 163.76  E-value: 2.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   27 NTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHylkTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPG 106
Cdd:PRK10083  10 NSLAIEERPIPQPAAGEVRVKVKLAGICGSDSH---IYRGHNPFAKYPRVIGHEFFGVIDAVGEGVDAARIGERVAVDPV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  107 ISCWRCNLCREGRYNLCPEMKFFAtppVH--GSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEVGPETN 184
Cdd:PRK10083  87 ISCGHCYPCSIGKPNVCTSLVVLG---VHrdGGFSEYAVVPAKNAHRIPDAIADQYAVMVEPFTIAANVTGRTGPTEQDV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  185 VLVMGAGPIGLVTMLA-ARAFSVPRIVIVDVDENRLAVAKQLGADEIVQvtTNLEDVGSEVEQiqkamgSNIDVT--FDC 261
Cdd:PRK10083 164 ALIYGAGPVGLTIVQVlKGVYNVKAVIVADRIDERLALAKESGADWVIN--NAQEPLGEALEE------KGIKPTliIDA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  262 AGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRYKNTWPLCLEFLTSGKIDVKPLITHRFGFsq 341
Cdd:PRK10083 236 ACHPSILEEAVTLASPAARIVLMGFSSEPSEIVQQGITGKELSIFSSRLNANKFPVVIDWLSKGLIDPEKLITHTFDF-- 313

                 ....*...
gi 15242240  342 KEVEDAFE 349
Cdd:PRK10083 314 QHVADAIE 321
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
41-360 9.70e-47

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: 163.48  E-value: 9.70e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  41 PHDVRVRMKAVGICGSDVH----YLKTMrcadfvvKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCR 116
Cdd:cd08283  25 PTDAIVRVTATAICGSDLHlyhgYIPGM-------KKGDILGHEFMGVVEEVGPEVRNLKVGDRVVVPFTIACGECFYCK 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 117 EGRYNLC------PEMK---------FF----ATPPVHGSLANQVVHP-ADL-CFKLPENVSLEEGA-MCEPLSVGVHAC 174
Cdd:cd08283  98 RGLYSQCdntnpsAEMAklyghagagIFgyshLTGGYAGGQAEYVRVPfADVgPFKIPDDLSDEKALfLSDILPTGYHAA 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 175 RRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVtTNLEDVGSEVEQIQKamGSN 254
Cdd:cd08283 178 ELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLGAETINF-EEVDDVVEALRELTG--GRG 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 255 IDVTFDCAGFN-------KTMST--------------ALAATRCGGKVCLVGM-GHGIMTVPLTPAAAREVDVVG----V 308
Cdd:cd08283 255 PDVCIDAVGMEahgsplhKAEQAllkletdrpdalreAIQAVRKGGTVSIIGVyGGTVNKFPIGAAMNKGLTLRMgqthV 334
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 15242240 309 FRYkntWPLCLEFLTSGKIDVKPLITHRFGFSqkEVEDAFET-SARGSNAIKV 360
Cdd:cd08283 335 QRY---LPRLLELIESGELDPSFIITHRLPLE--DAPEAYKIfDKKEDGCIKV 382
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
37-349 4.61e-46

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: 160.46  E-value: 4.61e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  37 PSVGPHDVRVRMKAVGICGSDVHylkTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCR 116
Cdd:cd08260  21 PEPPPDGVVVEVEACGVCRSDWH---GWQGHDPDVTLPHVPGHEFAGVVVEVGEDVSRWRVGDRVTVPFVLGCGTCPYCR 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 117 EGRYNLCPEMkffaTPP---VHGSLANQV-VHPADL-CFKLPENVSLEEGAmceplSVGvhaCR----------RAEVGP 181
Cdd:cd08260  98 AGDSNVCEHQ----VQPgftHPGSFAEYVaVPRADVnLVRLPDDVDFVTAA-----GLG---CRfatafralvhQARVKP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 182 ETNVLVMGAGPIGLVTMLAARAFSVpRIVIVDVDENRLAVAKQLGADEIVQVTTnLEDVGSEVEQIqkaMGSNIDVTFDC 261
Cdd:cd08260 166 GEWVAVHGCGGVGLSAVMIASALGA-RVIAVDIDDDKLELARELGAVATVNASE-VEDVAAAVRDL---TGGGAHVSVDA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 262 AGFNKTMSTALAATRCGGKVCLVGM---GHGIMTVPLTPAAAREVDVVGVF-----RYkntwPLCLEFLTSGKIDVKPLI 333
Cdd:cd08260 241 LGIPETCRNSVASLRKRGRHVQVGLtlgEEAGVALPMDRVVARELEIVGSHgmpahRY----DAMLALIASGKLDPEPLV 316
                       330
                ....*....|....*.
gi 15242240 334 THRFGFSqkEVEDAFE 349
Cdd:cd08260 317 GRTISLD--EAPDALA 330
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
29-359 5.03e-45

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: 158.30  E-value: 5.03e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  29 LKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKtmrcADFVVKEPMVIGHECAGIIEEVGEEVKH---LVVGDRVALEP 105
Cdd:cd08263  13 LTIEEIPVPRPKEGEILIRVAACGVCHSDLHVLK----GELPFPPPFVLGHEISGEVVEVGPNVENpygLSVGDRVVGSF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 106 GISCWRCNLCREGRYNLCPemKFFA-------------------TPPVH----GSLANQVVHPADLCFKLPENVSLEEGA 162
Cdd:cd08263  89 IMPCGKCRYCARGKENLCE--DFFAynrlkgtlydgttrlfrldGGPVYmysmGGLAEYAVVPATALAPLPESLDYTESA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 163 M--CEPLSVGVHACRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQvtTNLEDV 240
Cdd:cd08263 167 VlgCAGFTAYGALKHAADVRPGETVAVIGVGGVGSSAIQLAKAFGASPIIAVDVRDEKLAKAKELGATHTVN--AAKEDA 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 241 GSEVEQIQKAMGsnIDVTFDCAGFNKTMSTALAATRCGGKVCLVGMGHGIMT--VPLTPAAAREVDVVGVFRYK--NTWP 316
Cdd:cd08263 245 VAAIREITGGRG--VDVVVEALGKPETFKLALDVVRDGGRAVVVGLAPGGATaeIPITRLVRRGIKIIGSYGARprQDLP 322
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 15242240 317 LCLEFLTSGKIDVKPLITHRFGFsqKEVEDAFETSARGSNAIK 359
Cdd:cd08263 323 ELVGLAASGKLDPEALVTHKYKL--EEINEAYENLRKGLIHGR 363
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
29-359 9.02e-45

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: 157.66  E-value: 9.02e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  29 LKIQPFLLPSVGPHDVRVRMKAVGICGSDVHylktMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGiS 108
Cdd:cd08278  15 FVLEDVELDDPRPDEVLVRIVATGICHTDLV----VRDGGLPTPLPAVLGHEGAGVVEAVGSAVTGLKPGDHVVLSFA-S 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 109 CWRCNLCREGRYNLCPEM---KFFAT-------------PPVHG------SLANQVVHPADLCFKLPENVSLEEGAmceP 166
Cdd:cd08278  90 CGECANCLSGHPAYCENFfplNFSGRrpdgstplslddgTPVHGhffgqsSFATYAVVHERNVVKVDKDVPLELLA---P 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 167 LSVGVHA-----CRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVg 241
Cdd:cd08278 167 LGCGIQTgagavLNVLKPRPGSSIAVFGAGAVGLAAVMAAKIAGCTTIIAVDIVDSRLELAKELGATHVINPKE--EDL- 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 242 seVEQIQKAMGSNIDVTFDCAGFNKTMSTALAATRCGGKVCLVGMG--HGIMTVPLTPAAAREVDVVGV---------Fr 310
Cdd:cd08278 244 --VAAIREITGGGVDYALDTTGVPAVIEQAVDALAPRGTLALVGAPppGAEVTLDVNDLLVSGKTIRGViegdsvpqeF- 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 15242240 311 ykntWPLCLEFLTSGKIDVKPLITHrfgFSQKEVEDAFETSARGSnAIK 359
Cdd:cd08278 321 ----IPRLIELYRQGKFPFDKLVTF---YPFEDINQAIADSESGK-VIK 361
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
20-362 2.04e-44

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: 155.48  E-value: 2.04e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  20 AAWLVGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLK-TMRcadfvvkEPMVIGHECAGIIEEVGEEvkHLVvG 98
Cdd:cd08242   3 ALVLDGGLDLRVEDLPKPEPPPGEALVRVLLAGICNTDLEIYKgYYP-------FPGVPGHEFVGIVEEGPEA--ELV-G 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  99 DRVALEPGISCWRCNLCREGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAE 178
Cdd:cd08242  73 KRVVGEINIACGRCEYCRRGLYTHCPNRTVLGIVDRDGAFAEYLTLPLENLHVVPDLVPDEQAVFAEPLAAALEILEQVP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 179 VGPETNVLVMGAGPIGLVTMLAARAFsVPRIVIVDVDENRLAVAKQLGAdeivqVTTNLEDVGSEveqiqkamGSNIDVT 258
Cdd:cd08242 153 ITPGDKVAVLGDGKLGLLIAQVLALT-GPDVVLVGRHSEKLALARRLGV-----ETVLPDEAESE--------GGGFDVV 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 259 FDCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVV----GVFrykntwPLCLEFLTSGKIDVKPLIT 334
Cdd:cd08242 219 VEATGSPSGLELALRLVRPRGTVVLKSTYAGPASFDLTKAVVNEITLVgsrcGPF------APALRLLRKGLVDVDPLIT 292
                       330       340
                ....*....|....*....|....*...
gi 15242240 335 HRFGFSqkEVEDAFETSARgSNAIKVMF 362
Cdd:cd08242 293 AVYPLE--EALEAFERAAE-PGALKVLL 317
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
36-361 8.86e-44

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: 153.67  E-value: 8.86e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  36 LPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGiscwrcnlc 115
Cdd:cd08269  14 RPTPGPGQVLVRVEGCGVCGSDLPAFNQGRPWFVYPAEPGGPGHEGWGRVVALGPGVRGLAVGDRVAGLSG--------- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 116 regrynlcpemkffatppvhGSLANQVVHPADLCFKLPENvSLEEGAMCEPLSVGVHACRRAEVGPETNVLVMGAGPIGL 195
Cdd:cd08269  85 --------------------GAFAEYDLADADHAVPLPSL-LDGQAFPGEPLGCALNVFRRGWIRAGKTVAVIGAGFIGL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 196 VTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQvttnlEDVGSEVEQIQKAMGSN-IDVTFDCAGFNKTMSTALAA 274
Cdd:cd08269 144 LFLQLAAAAGARRVIAIDRRPARLALARELGATEVVT-----DDSEAIVERVRELTGGAgADVVIEAVGHQWPLDLAGEL 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 275 TRCGGKVCLVGM-GHGIMTVPLTPAAAREVDVVG-VFR----YKNTWPLCLEFLTSGKIDVKPLITHRFGFsqKEVEDAF 348
Cdd:cd08269 219 VAERGRLVIFGYhQDGPRPVPFQTWNWKGIDLINaVERdpriGLEGMREAVKLIADGRLDLGSLLTHEFPL--EELGDAF 296
                       330
                ....*....|....
gi 15242240 349 ETS-ARGSNAIKVM 361
Cdd:cd08269 297 EAArRRPDGFIKGV 310
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
29-309 5.07e-43

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: 152.38  E-value: 5.07e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  29 LKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYL---------KTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGD 99
Cdd:cd08240  13 LEEVEIDTPKPPGTEVLVKVTACGVCHSDLHIWdggydlgggKTMSLDDRGVKLPLVLGHEIVGEVVAVGPDAADVKVGD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 100 RVALEPGISCWRCNLCREGRYNLCPEMKFFATPPvHGSLANQVVHPADLCFKLPENVSLEEGAM--CEPLSVGVHACRRA 177
Cdd:cd08240  93 KVLVYPWIGCGECPVCLAGDENLCAKGRALGIFQ-DGGYAEYVIVPHSRYLVDPGGLDPALAATlaCSGLTAYSAVKKLM 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 178 EVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVqvttNLEDVGsEVEQIQKAMGSNIDV 257
Cdd:cd08240 172 PLVADEPVVIIGAGGLGLMALALLKALGPANIIVVDIDEAKLEAAKAAGADVVV----NGSDPD-AAKRIIKAAGGGVDA 246
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15242240 258 TFDCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVF 309
Cdd:cd08240 247 VIDFVNNSATASLAFDILAKGGKLVLVGLFGGEATLPLPLLPLRALTIQGSY 298
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
20-356 3.41e-42

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: 149.77  E-value: 3.41e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  20 AAWLVGINT-LKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCAdfvVKEPMVIGHECAGIIEEVGEEVKHLVVG 98
Cdd:cd08259   3 AAILHKPNKpLQIEEVPDPEPGPGEVLIKVKAAGVCYRDLLFWKGFFPR---GKYPLILGHEIVGTVEEVGEGVERFKPG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  99 DRVALEPGISCWRCNLCREGRYNLCPEMKFFATpPVHGSLANQVVHPADLCFKLPENVSLEEGA--MCePLSVGVHACRR 176
Cdd:cd08259  80 DRVILYYYIPCGKCEYCLSGEENLCRNRAEYGE-EVDGGFAEYVKVPERSLVKLPDNVSDESAAlaAC-VVGTAVHALKR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 177 AEVGPETNVLVMGAG---PIGLVTMLAARAfsvPRIVIVDVDENRLAVAKQLGADEIVQVTTNLEDVgseveqiqKAMGs 253
Cdd:cd08259 158 AGVKKGDTVLVTGAGggvGIHAIQLAKALG---ARVIAVTRSPEKLKILKELGADYVIDGSKFSEDV--------KKLG- 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 254 NIDVTFDCAGfNKTMSTALAATRCGGKVCLVGMGHG-IMTVPLTPAAAREVDVVGVFRY-KNTWPLCLEFLTSGKIdvKP 331
Cdd:cd08259 226 GADVVIELVG-SPTIEESLRSLNKGGRLVLIGNVTPdPAPLRPGLLILKEIRIIGSISAtKADVEEALKLVKEGKI--KP 302
                       330       340
                ....*....|....*....|....*
gi 15242240 332 LITHRFGFSQkeVEDAFETSARGSN 356
Cdd:cd08259 303 VIDRVVSLED--INEALEDLKSGKV 325
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
29-354 1.91e-41

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: 149.06  E-value: 1.91e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  29 LKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRcadfVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGIS 108
Cdd:cd08281  21 LVIEEVELDPPGPGEVLVKIAAAGLCHSDLSVINGDR----PRPLPMALGHEAAGVVVEVGEGVTDLEVGDHVVLVFVPS 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 109 CWRCNLCREGRYNLCP----------------EMKFFATPPVH----GSLANQVVHPADLCFKLPENVSLEEGAM--CEP 166
Cdd:cd08281  97 CGHCRPCAEGRPALCEpgaaangagtllsggrRLRLRGGEINHhlgvSAFAEYAVVSRRSVVKIDKDVPLEIAALfgCAV 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 167 LSvGVHAC-RRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVgseVE 245
Cdd:cd08281 177 LT-GVGAVvNTAGVRPGQSVAVVGLGGVGLSALLGAVAAGASQVVAVDLNEDKLALARELGATATVNAGD--PNA---VE 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 246 QIQKAMGSNIDVTFDCAGFNKTMSTALAATRCGGKVCLVGMGH--GIMTVPLTPAAAREVDVVG-----------VFRYK 312
Cdd:cd08281 251 QVRELTGGGVDYAFEMAGSVPALETAYEITRRGGTTVTAGLPDpeARLSVPALSLVAEERTLKGsymgscvprrdIPRYL 330
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 15242240 313 NTWplcleflTSGKIDVKPLITHRFGFSqkEVEDAFETSARG 354
Cdd:cd08281 331 ALY-------LSGRLPVDKLLTHRLPLD--EINEGFDRLAAG 363
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
41-336 2.51e-41

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 148.06  E-value: 2.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   41 PHDVRVRMKAVGICGSDV--------HYLktmrcadfvvkePMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRC 112
Cdd:PRK10309  25 QDDVLVKVASSGLCGSDIprifkngaHYY------------PITLGHEFSGYVEAVGSGVDDLHPGDAVACVPLLPCFTC 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  113 NLCREGRYNLCPEMKFFATPPVHGSLANQVVHPADLcFKLPENVSLEEGAMCEPLSVGVHACRRAEVGPETNVLVMGAGP 192
Cdd:PRK10309  93 PECLRGFYSLCAKYDFIGSRRDGGNAEYIVVKRKNL-FALPTDMPIEDGAFIEPITVGLHAFHLAQGCEGKNVIIIGAGT 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  193 IGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADeivQVTTNLEDVGSEVEQIQKAMGSNiDVTFDCAGFNKTMSTAL 272
Cdd:PRK10309 172 IGLLAIQCAVALGAKSVTAIDINSEKLALAKSLGAM---QTFNSREMSAPQIQSVLRELRFD-QLILETAGVPQTVELAI 247
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242240  273 AATRCGGKVCLVGMGHGIMTVPLTPAAA---REVDVVGVF-RYKNTWP-----LCLEFLTSGKIDVKPLITHR 336
Cdd:PRK10309 248 EIAGPRAQLALVGTLHHDLHLTSATFGKilrKELTVIGSWmNYSSPWPgqeweTASRLLTERKLSLEPLIAHR 320
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
37-361 2.87e-40

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: 146.12  E-value: 2.87e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  37 PSVGPHDVRVRMKAVGICGSDVHYLKTMRCADF----VVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRC 112
Cdd:cd08265  47 PNLKPDEILIRVKACGICGSDIHLYETDKDGYIlypgLTEFPVVIGHEFSGVVEKTGKNVKNFEKGDPVTAEEMMWCGMC 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 113 NLCREGRYNLCPEMKFFATpPVHGSLANQVVHPADLCFKL-------PENVSLEEGAMCEPLSVGVHAC--RRAEVGPET 183
Cdd:cd08265 127 RACRSGSPNHCKNLKELGF-SADGAFAEYIAVNARYAWEInelreiySEDKAFEAGALVEPTSVAYNGLfiRGGGFRPGA 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 184 NVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTNLED-VGSEVEQIQKAMGSNIDVtfDCA 262
Cdd:cd08265 206 YVVVYGAGPIGLAAIALAKAAGASKVIAFEISEERRNLAKEMGADYVFNPTKMRDClSGEKVMEVTKGWGADIQV--EAA 283
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 263 G-FNKTMSTALAATRCGGKVclVGMGHGIMTVPLTPAA--AREVDVVGVFRYKN--TWPLCLEFLTSGKIDVKPLITHRF 337
Cdd:cd08265 284 GaPPATIPQMEKSIAINGKI--VYIGRAATTVPLHLEVlqVRRAQIVGAQGHSGhgIFPSVIKLMASGKIDMTKIITARF 361
                       330       340
                ....*....|....*....|....*
gi 15242240 338 GFSqkEVEDAFE-TSARGSNAIKVM 361
Cdd:cd08265 362 PLE--GIMEAIKaASERTDGKITIL 384
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
42-151 8.11e-39

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: 133.89  E-value: 8.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240    42 HDVRVRMKAVGICGSDVHYLKTMrcaDFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCREGRYN 121
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGG---NPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYN 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 15242240   122 LCPEMKFFATpPVHGSLANQVVHPADLCFK 151
Cdd:pfam08240  78 LCPNGRFLGY-DRDGGFAEYVVVPERNLVP 106
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
28-354 9.33e-39

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: 140.92  E-value: 9.33e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  28 TLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHylkTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRValepGI 107
Cdd:cd08245  11 PLEPEEVPVPEPGPGEVLIKIEACGVCHTDLH---AAEGDWGGSKYPLVPGHEIVGEVVEVGAGVEGRKVGDRV----GV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 108 -----SCWRCNLCREGRYNLCPEMKFfaTPPVH-GSLANQVVHPADLCFKLPENVSLEEGA--MCEPLSVgVHACRRAEV 179
Cdd:cd08245  84 gwlvgSCGRCEYCRRGLENLCQKAVN--TGYTTqGGYAEYMVADAEYTVLLPDGLPLAQAAplLCAGITV-YSALRDAGP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 180 GPETNVLVMGAGPIGLVTMLAARAFSVPRIVIvDVDENRLAVAKQLGADEIVQVTTNLedvgseveQIQKAMGSnIDVTF 259
Cdd:cd08245 161 RPGERVAVLGIGGLGHLAVQYARAMGFETVAI-TRSPDKRELARKLGADEVVDSGAEL--------DEQAAAGG-ADVIL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 260 DCAGFNKTMSTALAATRCGGKVCLVGMGHG-IMTVPLTPAAAREVDVVGVfrYKNTWPLCLEFLT-SGKIDVKPlITHRF 337
Cdd:cd08245 231 VTVVSGAAAEAALGGLRRGGRIVLVGLPESpPFSPDIFPLIMKRQSIAGS--THGGRADLQEALDfAAEGKVKP-MIETF 307
                       330
                ....*....|....*..
gi 15242240 338 GFSQkeVEDAFETSARG 354
Cdd:cd08245 308 PLDQ--ANEAYERMEKG 322
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
20-354 1.06e-38

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: 140.75  E-value: 1.06e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  20 AAWLV--GINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKtmrcADF--VVKEPMVIGHECAGIIEEVGEEVKHL 95
Cdd:cd08297   3 AAVVEefGEKPYEVKDVPVPEPGPGEVLVKLEASGVCHTDLHAAL----GDWpvKPKLPLIGGHEGAGVVVAVGPGVSGL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  96 VVGDRValepGI-----SCWRCNLCREGRYNLCPEMKfFATPPVHGSLANQVVHPADLCFKLPENVSLEEGA--MCEPLS 168
Cdd:cd08297  79 KVGDRV----GVkwlydACGKCEYCRTGDETLCPNQK-NSGYTVDGTFAEYAIADARYVTPIPDGLSFEQAAplLCAGVT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 169 VgVHACRRAEVGPETNVLVMGAGpiGLVTMLA---ARAFSVpRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVGSEVE 245
Cdd:cd08297 154 V-YKALKKAGLKPGDWVVISGAG--GGLGHLGvqyAKAMGL-RVIAIDVGDEKLELAKELGADAFVDFKK--SDDVEAVK 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 246 QIQKAMGSniDVTFDCAGFNKTMSTALAATRCGGKVCLVGM-GHGIMTVPLTPAAAREVDVVGVFRYKNTW-PLCLEFLT 323
Cdd:cd08297 228 ELTGGGGA--HAVVVTAVSAAAYEQALDYLRPGGTLVCVGLpPGGFIPLDPFDLVLRGITIVGSLVGTRQDlQEALEFAA 305
                       330       340       350
                ....*....|....*....|....*....|.
gi 15242240 324 SGKidVKPLIThRFGFSQkeVEDAFETSARG 354
Cdd:cd08297 306 RGK--VKPHIQ-VVPLED--LNEVFEKMEEG 331
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
19-354 1.65e-38

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: 139.90  E-value: 1.65e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  19 MAAWLV----GINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMrcADFVVKEPMVIGHECAGIIEEVGEEVKH 94
Cdd:COG0604   1 MKAIVItefgGPEVLELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRGL--YPLPPGLPFIPGSDAAGVVVAVGEGVTG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  95 LVVGDRVALEPGiscwrcnlcregrynlcpemkffatppvHGSLANQVVHPADLCFKLPENVSLEEGAMCePLsVGVHA- 173
Cdd:COG0604  79 FKVGDRVAGLGR----------------------------GGGYAEYVVVPADQLVPLPDGLSFEEAAAL-PL-AGLTAw 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 174 ---CRRAEVGPETNVLVMGA-GPIGL--VTMLAARAFSVprIVIVDVDENRlAVAKQLGADEIVQVTTnlEDVGSEVEQI 247
Cdd:COG0604 129 qalFDRGRLKPGETVLVHGAaGGVGSaaVQLAKALGARV--IATASSPEKA-ELLRALGADHVIDYRE--EDFAERVRAL 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 248 QKAMGsnIDVTFDCAGfNKTMSTALAATRCGGKVCLVG-MGHGIMTVPLTPAAAREVDVVGVF-------RYKNTWPLCL 319
Cdd:COG0604 204 TGGRG--VDVVLDTVG-GDTLARSLRALAPGGRLVSIGaASGAPPPLDLAPLLLKGLTLTGFTlfardpaERRAALAELA 280
                       330       340       350
                ....*....|....*....|....*....|....*
gi 15242240 320 EFLTSGKIdvKPLITHRFGFSqkEVEDAFETSARG 354
Cdd:COG0604 281 RLLAAGKL--RPVIDRVFPLE--EAAEAHRLLESG 311
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
40-360 3.86e-37

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: 137.47  E-value: 3.86e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  40 GPHDVRVRMKAVGICGSDVHYLKTMRCADFvvkePMVIGHECAGIIEEVGEEVKHLVVGDRVaLEPGIS-CWRCNLCREG 118
Cdd:cd08277  26 KANEVRIKMLATSVCHTDILAIEGFKATLF----PVILGHEGAGIVESVGEGVTNLKPGDKV-IPLFIGqCGECSNCRSG 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 119 RYNLCPEMKFFATP--------------PVH-----GSLANQVVHPADLCFKLPENVSLEEGAMcepLSVGVH-----AC 174
Cdd:cd08277 101 KTNLCQKYRANESGlmpdgtsrftckgkKIYhflgtSTFSQYTVVDENYVAKIDPAAPLEHVCL---LGCGFStgygaAW 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 175 RRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVqvttNLEDVGSEVEQ-IQKAMGS 253
Cdd:cd08277 178 NTAKVEPGSTVAVFGLGAVGLSAIMGAKIAGASRIIGVDINEDKFEKAKEFGATDFI----NPKDSDKPVSEvIREMTGG 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 254 NIDVTFDCAGFNKTMSTALAATRCG-GKVCLVGMGHGIM--TVPLTPAAAREVD--VVGVFRYKNTWPLCLEFLTSGKID 328
Cdd:cd08277 254 GVDYSFECTGNADLMNEALESTKLGwGVSVVVGVPPGAElsIRPFQLILGRTWKgsFFGGFKSRSDVPKLVSKYMNKKFD 333
                       330       340       350
                ....*....|....*....|....*....|..
gi 15242240 329 VKPLITHRFGFsqKEVEDAFETSARGsNAIKV 360
Cdd:cd08277 334 LDELITHVLPF--EEINKGFDLMKSG-ECIRT 362
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
29-307 3.98e-37

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: 136.47  E-value: 3.98e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  29 LKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLktmRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRValepGI- 107
Cdd:cd05283  12 LEPFTFERRPLGPDDVDIKITYCGVCHSDLHTL---RNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDRV----GVg 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 108 ----SCWRCNLCREGRYNLCPEMKFFATPPV------HGSLANQVVHPADLCFKLPENVSLEEGA--MC------EPLsv 169
Cdd:cd05283  85 cqvdSCGTCEQCKSGEEQYCPKGVVTYNGKYpdgtitQGGYADHIVVDERFVFKIPEGLDSAAAAplLCagitvySPL-- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 170 gvhacRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVpRIVIVDVDENRLAVAKQLGADEIVqvttnledVGSEVEQIQK 249
Cdd:cd05283 163 -----KRNGVGPGKRVGVVGIGGLGHLAVKFAKALGA-EVTAFSRSPSKKEDALKLGADEFI--------ATKDPEAMKK 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15242240 250 AMGSnIDVTFDCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVG 307
Cdd:cd05283 229 AAGS-LDLIIDTVSASHDLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGRKSVAG 285
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
20-361 1.55e-36

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: 135.13  E-value: 1.55e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  20 AAWLVGINTLKIQPFLLPSV-GPHDVRVRMKAVGICGSDVHYLKTMRCADfvvkEPMVIGHECAGIIEEVGEEVKHLVVG 98
Cdd:cd08287   3 ATVIHGPGDIRVEEVPDPVIeEPTDAVIRVVATCVCGSDLWPYRGVSPTR----APAPIGHEFVGVVEEVGSEVTSVKPG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  99 DRVALEPGISCWRCNLCREGRYNLCPEMKFFaTPPVHGSLANQVVHP-AD-LCFKLPENVSLEEG------AMCEPLSVG 170
Cdd:cd08287  79 DFVIAPFAISDGTCPFCRAGFTTSCVHGGFW-GAFVDGGQGEYVRVPlADgTLVKVPGSPSDDEDllpsllALSDVMGTG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 171 VHACRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVqvttnlEDVGSE-VEQIqK 249
Cdd:cd08287 158 HHAAVSAGVRPGSTVVVVGDGAVGLCAVLAAKRLGAERIIAMSRHEDRQALAREFGATDIV------AERGEEaVARV-R 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 250 AM--GSNIDVTFDCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVG----VFRYKntwPLCLEFLT 323
Cdd:cd08287 231 ELtgGVGADAVLECVGTQESMEQAIAIARPGGRVGYVGVPHGGVELDVRELFFRNVGLAGgpapVRRYL---PELLDDVL 307
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 15242240 324 SGKIDVKPLITHRFGFSqkEVEDAFET-SARgsNAIKVM 361
Cdd:cd08287 308 AGRINPGRVFDLTLPLD--EVAEGYRAmDER--RAIKVL 342
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
60-362 1.69e-36

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: 133.16  E-value: 1.69e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  60 YLKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVAlepgiscwrcnlcregrynlcpemkffatppVHGSLA 139
Cdd:cd08255   7 ALEGLSTGTEKLPLPLPPGYSSVGRVVEVGSGVTGFKPGDRVF-------------------------------CFGPHA 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 140 NQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRL 219
Cdd:cd08255  56 ERVVVPANLLVPLPDGLPPERAALTALAATALNGVRDAEPRLGERVAVVGLGLVGLLAAQLAKAAGAREVVGVDPDAARR 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 220 AVAKQLGADEIVQVTTNLEDVGSEVeqiqkamgsniDVTFDCAGFNKTMSTALAATRCGGKVCLVGMGhGIMTVPLT-PA 298
Cdd:cd08255 136 ELAEALGPADPVAADTADEIGGRGA-----------DVVIEASGSPSALETALRLLRDRGRVVLVGWY-GLKPLLLGeEF 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 299 AAREVDVV-----GVFRYknTWP----------LCLEFLTSGKIDvkPLITHRFGFSqkEVEDAFET-SARGSNAIKVMF 362
Cdd:cd08255 204 HFKRLPIRssqvyGIGRY--DRPrrwtearnleEALDLLAEGRLE--ALITHRVPFE--DAPEAYRLlFEDPPECLKVVL 277
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
41-285 4.80e-36

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: 134.64  E-value: 4.80e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  41 PHDVRVRMKAVGICGSDVHylktMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCREGRY 120
Cdd:cd08282  25 PTDAIVRITTTAICGSDLH----MYRGRTGAEPGLVLGHEAMGEVEEVGSAVESLKVGDRVVVPFNVACGRCRNCKRGLT 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 121 NLCPEM---------KFFATPPVHGSLANQVVHP-ADL-CFKLPENVSLEEGAMCEPLS----VGVHACRRAEVGPETNV 185
Cdd:cd08282 101 GVCLTVnpgraggayGYVDMGPYGGGQAEYLRVPyADFnLLKLPDRDGAKEKDDYLMLSdifpTGWHGLELAGVQPGDTV 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 186 LVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGAdeivqVTTNLEDvGSEVEQIQKAMGSNIDVTFDCAGF- 264
Cdd:cd08282 181 AVFGAGPVGLMAAYSAILRGASRVYVVDHVPERLDLAESIGA-----IPIDFSD-GDPVEQILGLEPGGVDRAVDCVGYe 254
                       250       260       270
                ....*....|....*....|....*....|.
gi 15242240 265 ----------NKTMSTALAATRCGGKVCLVG 285
Cdd:cd08282 255 ardrggeaqpNLVLNQLIRVTRPGGGIGIVG 285
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
25-349 6.76e-36

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: 133.54  E-value: 6.76e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  25 GINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADfvVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALE 104
Cdd:cd08266  11 GPEVLEYGDLPEPEPGPDEVLVRVKAAALNHLDLWVRRGMPGIK--LPLPHILGSDGAGVVEAVGPGVTNVKPGQRVVIY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 105 PGISCWRCNLCREGRYNLCPEMKFFATpPVHGSLANQVVHPADLCFKLPENVSLEEGAmCEPLSVGV--HACR-RAEVGP 181
Cdd:cd08266  89 PGISCGRCEYCLAGRENLCAQYGILGE-HVDGGYAEYVAVPARNLLPIPDNLSFEEAA-AAPLTFLTawHMLVtRARLRP 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 182 ETNVLVMGAGP-IGLVTMLAARAFSVprIVIVDV-DENRLAVAKQLGADEIVQVTTnlEDVGSEVEQIQKAMGsnIDVTF 259
Cdd:cd08266 167 GETVLVHGAGSgVGSAAIQIAKLFGA--TVIATAgSEDKLERAKELGADYVIDYRK--EDFVREVRELTGKRG--VDVVV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 260 DCAGfNKTMSTALAATRCGGKVCLVGMGHGIMT-VPLTPAAAREVDVVGVF-----RYKNTwplcLEFLTSGKIdvKPLI 333
Cdd:cd08266 241 EHVG-AATWEKSLKSLARGGRLVTCGATTGYEApIDLRHVFWRQLSILGSTmgtkaELDEA----LRLVFRGKL--KPVI 313
                       330
                ....*....|....*.
gi 15242240 334 THRFGFSqkEVEDAFE 349
Cdd:cd08266 314 DSVFPLE--EAAEAHR 327
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
42-349 6.72e-31

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: 120.50  E-value: 6.72e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  42 HDVRVRMKAVGICGSDVHYLKTMrcadFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCREGRYN 121
Cdd:cd08299  33 HEVRIKIVATGICRSDDHVVSGK----LVTPFPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFVPQCGKCRACLNPESN 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 122 LCPEMKFFAT---------------PPVHGSLANQ------VVHPADLCfKLPENVSLEEGAM--CEpLSVGV-HACRRA 177
Cdd:cd08299 109 LCLKNDLGKPqglmqdgtsrftckgKPIHHFLGTStfseytVVDEIAVA-KIDAAAPLEKVCLigCG-FSTGYgAAVNTA 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 178 EVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVqvttNLEDVGSEVEQ-IQKAMGSNID 256
Cdd:cd08299 187 KVTPGSTCAVFGLGGVGLSAIMGCKAAGASRIIAVDINKDKFAKAKELGATECI----NPQDYKKPIQEvLTEMTDGGVD 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 257 VTFDCAGFNKTMSTALAATRCGGKVC-LVGMGHGIMTVPLTPA---AAREVD--VVGVFRYKNTWP-LCLEFLtSGKIDV 329
Cdd:cd08299 263 FSFEVIGRLDTMKAALASCHEGYGVSvIVGVPPSSQNLSINPMlllTGRTWKgaVFGGWKSKDSVPkLVADYM-AKKFNL 341
                       330       340
                ....*....|....*....|
gi 15242240 330 KPLITHRFGFSQkeVEDAFE 349
Cdd:cd08299 342 DPLITHTLPFEK--INEGFD 359
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
19-288 1.02e-28

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: 113.82  E-value: 1.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  19 MAAWL------VGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKtmrcADFVV-KEPMVIGHECAGIIEEVGEE 91
Cdd:cd08298   1 MKAMVlekpgpIEENPLRLTEVPVPEPGPGEVLIKVEACGVCRTDLHIVE----GDLPPpKLPLIPGHEIVGRVEAVGPG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  92 VKHLVVGDRVALEP-GISCWRCNLCREGRYNLCPEMKFFATpPVHGSLANQVVHPADLCFKLPENVSLEEGA--MCEPLs 168
Cdd:cd08298  77 VTRFSVGDRVGVPWlGSTCGECRYCRSGRENLCDNARFTGY-TVDGGYAEYMVADERFAYPIPEDYDDEEAAplLCAGI- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 169 VGVHACRRAEVGPETNVLVMGAGPIG-LVTMLAARAFSvpRIVIVDVDENRLAVAKQLGADeivqvttnleDVGSEVEQI 247
Cdd:cd08298 155 IGYRALKLAGLKPGQRLGLYGFGASAhLALQIARYQGA--EVFAFTRSGEHQELARELGAD----------WAGDSDDLP 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15242240 248 QKAMGSNIDvtFDCAGfnKTMSTALAATRCGGKVCLVGMGH 288
Cdd:cd08298 223 PEPLDAAII--FAPVG--ALVPAALRAVKKGGRVVLAGIHM 259
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
37-361 3.39e-28

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 112.44  E-value: 3.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   37 PSVGPHDVRVRMKAVGICGSDvhyLKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCR 116
Cdd:PRK13771  21 PKPGKDEVVIKVNYAGLCYRD---LLQLQGFYPRMKYPVILGHEVVGTVEEVGENVKGFKPGDRVASLLYAPDGTCEYCR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  117 EGRYNLCPEMKFFATpPVHGSLANQVVHPADLCFKLPENVSlEEGAMCEP--LSVGVHACRRAEVGPETNVLVMGA-GPI 193
Cdd:PRK13771  98 SGEEAYCKNRLGYGE-ELDGFFAEYAKVKVTSLVKVPPNVS-DEGAVIVPcvTGMVYRGLRRAGVKKGETVLVTGAgGGV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  194 GLVTMLAARAFSVpRIVIVDVDENRLAVAKQLgADEIVQVTTNLEDVgseveqiqKAMGsNIDVTFDCAGfNKTMSTALA 273
Cdd:PRK13771 176 GIHAIQVAKALGA-KVIAVTSSESKAKIVSKY-ADYVIVGSKFSEEV--------KKIG-GADIVIETVG-TPTLEESLR 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  274 ATRCGGKVCLVGM--GHGIMTVPLTPAAAREVDVVGVFR-YKNTWPLCLEFLTSGKIdvKPLITHRFGFSqkEVEDAFET 350
Cdd:PRK13771 244 SLNMGGKIIQIGNvdPSPTYSLRLGYIILKDIEIIGHISaTKRDVEEALKLVAEGKI--KPVIGAEVSLS--EIDKALEE 319
                        330
                 ....*....|.
gi 15242240  351 SARGSNAIKVM 361
Cdd:PRK13771 320 LKDKSRIGKIL 330
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
19-354 5.05e-28

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: 111.50  E-value: 5.05e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  19 MAAWLV----GINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKH 94
Cdd:cd05289   1 MKAVRIheygGPEVLELADVPTPEPGPGEVLVKVHAAGVNPVDLKIREGLLKAAFPLTLPLIPGHDVAGVVVAVGPGVTG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  95 LVVGDRValepgiscwrcnlcregrynlcpemkfFATPPVH--GSLANQVVHPADLCFKLPENVSLEEGAMCePLSV--- 169
Cdd:cd05289  81 FKVGDEV---------------------------FGMTPFTrgGAYAEYVVVPADELALKPANLSFEEAAAL-PLAGlta 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 170 --GVHacRRAEVGPETNVLVMGA-GPIGLVTMLAARAFSVprIVIVDVDENRLAVAKQLGADEIVQVTTNLEDVGSEVEq 246
Cdd:cd05289 133 wqALF--ELGGLKAGQTVLIHGAaGGVGSFAVQLAKARGA--RVIATASAANADFLRSLGADEVIDYTKGDFERAAAPG- 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 247 iqkamgsNIDVTFDCAGFnKTMSTALAATRCGGKVClvgmghGIMTVPLTPAAAREVDVVGVFRYKNTWPLCLEFLT--- 323
Cdd:cd05289 208 -------GVDAVLDTVGG-ETLARSLALVKPGGRLV------SIAGPPPAEQAAKRRGVRAGFVFVEPDGEQLAELAelv 273
                       330       340       350
                ....*....|....*....|....*....|..
gi 15242240 324 -SGKIdvKPLITHRFGFSqkEVEDAFETSARG 354
Cdd:cd05289 274 eAGKL--RPVVDRVFPLE--DAAEAHERLESG 301
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
41-361 6.74e-28

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: 111.44  E-value: 6.74e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  41 PHDVRVRMKAVGICGSDVhyLKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRValepgiscwrcnlcregry 120
Cdd:cd08241  27 PGEVRIRVEAAGVNFPDL--LMIQGKYQVKPPLPFVPGSEVAGVVEAVGEGVTGFKVGDRV------------------- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 121 nlcpemkfFATPPvHGSLANQVVHPADLCFKLPENVSLEEGAmCEPLSVGV--HAC-RRAEVGPETNVLVMGA-GPIGLV 196
Cdd:cd08241  86 --------VALTG-QGGFAEEVVVPAAAVFPLPDGLSFEEAA-ALPVTYGTayHALvRRARLQPGETVLVLGAaGGVGLA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 197 TMLAARAFSVPRIVIVDVDEnRLAVAKQLGADEIVQVTTnlEDVGSEVEQIQKAMGsnIDVTFDCAGfnktMSTALAATR 276
Cdd:cd08241 156 AVQLAKALGARVIAAASSEE-KLALARALGADHVIDYRD--PDLRERVKALTGGRG--VDVVYDPVG----GDVFEASLR 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 277 C---GGKVCLVGMGHG-IMTVPLTPAAAREVDVVGVF----------RYKNTWPLCLEFLTSGKIdvKPLITHRFGFSQk 342
Cdd:cd08241 227 SlawGGRLLVIGFASGeIPQIPANLLLLKNISVVGVYwgayarrepeLLRANLAELFDLLAEGKI--RPHVSAVFPLEQ- 303
                       330
                ....*....|....*....
gi 15242240 343 eVEDAFETSARGSNAIKVM 361
Cdd:cd08241 304 -AAEALRALADRKATGKVV 321
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
42-349 1.55e-27

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: 111.17  E-value: 1.55e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  42 HDVRVRMKAVGICGSDVHylkTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCREGRYN 121
Cdd:cd08300  28 GEVRIKILATGVCHTDAY---TLSGADPEGLFPVILGHEGAGIVESVGEGVTSVKPGDHVIPLYTPECGECKFCKSGKTN 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 122 LCPEMKFF----------------ATPPVH----GSLAN-QVVHPADLCfKLPENVSLEEGAMcepLSVGVH-----ACR 175
Cdd:cd08300 105 LCQKIRATqgkglmpdgtsrfsckGKPIYHfmgtSTFSEyTVVAEISVA-KINPEAPLDKVCL---LGCGVTtgygaVLN 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 176 RAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADE----------IVQVTTNLEDVGseve 245
Cdd:cd08300 181 TAKVEPGSTVAVFGLGAVGLAVIQGAKAAGASRIIGIDINPDKFELAKKFGATDcvnpkdhdkpIQQVLVEMTDGG---- 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 246 qiqkamgsnIDVTFDCAGFNKTMSTALAATRCG-GKVCLVGM---GHGIMTVPLTPAAAREV--DVVGVFRYKNTWPLCL 319
Cdd:cd08300 257 ---------VDYTFECIGNVKVMRAALEACHKGwGTSVIIGVaaaGQEISTRPFQLVTGRVWkgTAFGGWKSRSQVPKLV 327
                       330       340       350
                ....*....|....*....|....*....|
gi 15242240 320 EFLTSGKIDVKPLITHRFGFsqKEVEDAFE 349
Cdd:cd08300 328 EDYMKGKIKVDEFITHTMPL--DEINEAFD 355
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
37-341 2.00e-26

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: 107.28  E-value: 2.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  37 PSVGPHDVRVRMKAVGICGSDVhYLKTMRCADfVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRValepgiscWRCNLCR 116
Cdd:cd08253  23 PTPGPGEVLVRVHASGVNPVDT-YIRAGAYPG-LPPLPYVPGSDGAGVVEAVGEGVDGLKVGDRV--------WLTNLGW 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 117 EGRynlcpemkffatppvHGSLANQVVHPADLCFKLPENVSLEEGAmceplSVGVHAC-------RRAEVGPETNVLVMG 189
Cdd:cd08253  93 GRR---------------QGTAAEYVVVPADQLVPLPDGVSFEQGA-----ALGIPALtayralfHRAGAKAGETVLVHG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 190 -AGPIGLVTMLAARAFSVpRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVgseVEQIQKAMGSN-IDVTFDCAgFNKT 267
Cdd:cd08253 153 gSGAVGHAAVQLARWAGA-RVIATASSAEGAELVRQAGADAVFNYRA--EDL---ADRILAATAGQgVDVIIEVL-ANVN 225
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15242240 268 MSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRYKNT---WPLCLEFLTSGKID--VKPLITHRFGFSQ 341
Cdd:cd08253 226 LAKDLDVLAPGGRIVVYGSGGLRGTIPINPLMAKEASIRGVLLYTATpeeRAAAAEAIAAGLADgaLRPVIAREYPLEE 304
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
41-349 4.65e-26

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: 107.00  E-value: 4.65e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  41 PHDVRVRMKAVGICGSDVHYLK-TMRCADFvvkePMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCREGR 119
Cdd:cd08301  27 AMEVRIKILHTSLCHTDVYFWEaKGQTPLF----PRILGHEAAGIVESVGEGVTDLKPGDHVLPVFTGECKECRHCKSEK 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 120 YNLCPEMKF--------------FAT--PPVHGSLANQ------VVHPADLCfKLPENVSLEEGAMcepLSVGVH----- 172
Cdd:cd08301 103 SNMCDLLRIntdrgvmindgksrFSIngKPIYHFVGTStfseytVVHVGCVA-KINPEAPLDKVCL---LSCGVStglga 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 173 ACRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVqvttNLEDVGSEVEQIQKAM- 251
Cdd:cd08301 179 AWNVAKVKKGSTVAIFGLGAVGLAVAEGARIRGASRIIGVDLNPSKFEQAKKFGVTEFV----NPKDHDKPVQEVIAEMt 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 252 GSNIDVTFDCAGFNKTMSTALAATRCG-GKVCLVGMGHGIMTVPLTPA---AAREV--DVVGVFRYKNTWPLCLEFLTSG 325
Cdd:cd08301 255 GGGVDYSFECTGNIDAMISAFECVHDGwGVTVLLGVPHKDAVFSTHPMnllNGRTLkgTLFGGYKPKTDLPNLVEKYMKK 334
                       330       340
                ....*....|....*....|....
gi 15242240 326 KIDVKPLITHRFGFSqkEVEDAFE 349
Cdd:cd08301 335 ELELEKFITHELPFS--EINKAFD 356
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
25-341 2.11e-25

Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. 2-haloacrylate reductase, a member of this subgroup, catalyzes the NADPH-dependent reduction of a carbon-carbon double bond in organohalogen compounds. Although similar to QOR, Burkholderia 2-haloacrylate reductase does not act on the quinones 1,4-benzoquinone and 1,4-naphthoquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176189 [Multi-domain]  Cd Length: 320  Bit Score: 104.44  E-value: 2.11e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  25 GINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYlktmRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVAle 104
Cdd:cd05286  10 GPEVLEYEDVPVPEPGPGEVLVRNTAIGVNFIDTYF----RSGLYPLPLPFVLGVEGAGVVEAVGPGVTGFKVGDRVA-- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 105 pgiscwrcnlcregrynlcpemkfFATPPvhGSLANQVVHPADLCFKLPENVSLEEGA--MCEPLSVGVHACRRAEVGPE 182
Cdd:cd05286  84 ------------------------YAGPP--GAYAEYRVVPASRLVKLPDGISDETAAalLLQGLTAHYLLRETYPVKPG 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 183 TNVLVMG-AGPIG--LVTMLAARAFSVprIVIVDVDEnRLAVAKQLGADEIVQVTTnlEDVGSEVEQIQKAMGsnIDVTF 259
Cdd:cd05286 138 DTVLVHAaAGGVGllLTQWAKALGATV--IGTVSSEE-KAELARAAGADHVINYRD--EDFVERVREITGGRG--VDVVY 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 260 DCAGfNKTMSTALAATRCGGKVCLVGMGHGIMT-VPLTPAAAREVDVVG--VFRYKNT---WPLC----LEFLTSGKIDV 329
Cdd:cd05286 211 DGVG-KDTFEGSLDSLRPRGTLVSFGNASGPVPpFDLLRLSKGSLFLTRpsLFHYIATreeLLARaaelFDAVASGKLKV 289
                       330
                ....*....|..
gi 15242240 330 KplITHRFGFSQ 341
Cdd:cd05286 290 E--IGKRYPLAD 299
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
36-293 5.84e-25

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 103.58  E-value: 5.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   36 LPSVGPHDVRVRMKAVGICGSDVHylktMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGI-SCWRCNL 114
Cdd:PRK09422  20 LRPLKHGEALVKMEYCGVCHTDLH----VANGDFGDKTGRILGHEGIGIVKEVGPGVTSLKVGDRVSIAWFFeGCGHCEY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  115 CREGRYNLCPEMKfFATPPVHGSLANQVVHPADLCFKLPENvsLEEGAMCEPLSVGV---HACRRAEVGPETNVLVMGAG 191
Cdd:PRK09422  96 CTTGRETLCRSVK-NAGYTVDGGMAEQCIVTADYAVKVPEG--LDPAQASSITCAGVttyKAIKVSGIKPGQWIAIYGAG 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  192 PIG-LVTMLAARAFSVpRIVIVDVDENRLAVAKQLGADeivqVTTNLEDVGSEVEQIQKAMGS--NIDVT-FDCAGFNKt 267
Cdd:PRK09422 173 GLGnLALQYAKNVFNA-KVIAVDINDDKLALAKEVGAD----LTINSKRVEDVAKIIQEKTGGahAAVVTaVAKAAFNQ- 246
                        250       260
                 ....*....|....*....|....*.
gi 15242240  268 mstALAATRCGGKVCLVGMGHGIMTV 293
Cdd:PRK09422 247 ---AVDAVRAGGRVVAVGLPPESMDL 269
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
20-311 9.03e-24

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


Pssm-ID: 176211 [Multi-domain]  Cd Length: 339  Bit Score: 100.35  E-value: 9.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  20 AAWLVGINT--LKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKtmrcADFVVKEPMVIGHECAGIIEEVGEEVKHLVV 97
Cdd:cd08249   3 AAVLTGPGGglLVVVDVPVPKPGPDEVLVKVKAVALNPVDWKHQD----YGFIPSYPAILGCDFAGTVVEVGSGVTRFKV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  98 GDRVALepgiscwrcnLCREGRYNlcpemkffatPPVHGSLANQVVHPADLCFKLPENVSLEEGA------------MCE 165
Cdd:cd08249  79 GDRVAG----------FVHGGNPN----------DPRNGAFQEYVVADADLTAKIPDNISFEEAAtlpvglvtaalaLFQ 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 166 PLSVGVHACRRAEVGPETNVLVMGAG-PIGLVTMLAARAFSVPriVIVDVDENRLAVAKQLGADEIVqvttnleD--VGS 242
Cdd:cd08249 139 KLGLPLPPPKPSPASKGKPVLIWGGSsSVGTLAIQLAKLAGYK--VITTASPKNFDLVKSLGADAVF-------DyhDPD 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15242240 243 EVEQIQKAMGSNIDVTFDCAGFNKTMSTALAATRCGGKVCLVGMghgiMTVPLTPAAAREVDVVGVFRY 311
Cdd:cd08249 210 VVEDIRAATGGKLRYALDCISTPESAQLCAEALGRSGGGKLVSL----LPVPEETEPRKGVKVKFVLGY 274
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
36-349 1.76e-23

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: 99.24  E-value: 1.76e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  36 LPSVGPHDVRVRMKAVGICGSDVHylkTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALE-PGISCWRCNL 114
Cdd:cd08296  20 VPLPGPGEVLIKVEACGVCHSDAF---VKEGAMPGLSYPRVPGHEVVGRIDAVGEGVSRWKVGDRVGVGwHGGHCGTCDA 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 115 CREGRYNLCPEMKFfatPPVH--GSLANQVVHPADLCFKLPENVSLEEGA--MCEPLSVgVHACRRAEVGPETNVLVMGA 190
Cdd:cd08296  97 CRRGDFVHCENGKV---TGVTrdGGYAEYMLAPAEALARIPDDLDAAEAAplLCAGVTT-FNALRNSGAKPGDLVAVQGI 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 191 GPIG-LVTMLAARA-FsvpRIVIVDVDENRLAVAKQLGADEIVQvtTNLEDVGSEVeqiqKAMGSnIDVTFDCAGFNKTM 268
Cdd:cd08296 173 GGLGhLAVQYAAKMgF---RTVAISRGSDKADLARKLGAHHYID--TSKEDVAEAL----QELGG-AKLILATAPNAKAI 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 269 STALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGvfrykntWPL--------CLEFltSGKIDVKPLItHRFGFS 340
Cdd:cd08296 243 SALVGGLAPRGKLLILGAAGEPVAVSPLQLIMGRKSIHG-------WPSgtaldsedTLKF--SALHGVRPMV-ETFPLE 312

                ....*....
gi 15242240 341 QkeVEDAFE 349
Cdd:cd08296 313 K--ANEAYD 319
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
19-360 2.27e-23

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


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 99.15  E-value: 2.27e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  19 MAAWLV----GINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADfvVKEPMVIGHECAGIIEEVGEEVKH 94
Cdd:cd08276   1 MKAWRLsgggGLDNLKLVEEPVPEPGPGEVLVRVHAVSLNYRDLLILNGRYPPP--VKDPLIPLSDGAGEVVAVGEGVTR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  95 LVVGDRVAlepgiscwrCNLCREGRYNLCPEMKFFAT--PPVHGSLANQVVHPADLCFKLPENVSLEEGAmCEPLSvGVH 172
Cdd:cd08276  79 FKVGDRVV---------PTFFPNWLDGPPTAEDEASAlgGPIDGVLAEYVVLPEEGLVRAPDHLSFEEAA-TLPCA-GLT 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 173 A----CRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVpRIVIVDVDENRLAVAKQLGADEIVQVTTNLeDVGSEVEQIQ 248
Cdd:cd08276 148 AwnalFGLGPLKPGDTVLVQGTGGVSLFALQFAKAAGA-RVIATSSSDEKLERAKALGADHVINYRTTP-DWGEEVLKLT 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 249 KAMGsnIDVTFDCAGfNKTMSTALAATRCGGKVCLVG-MGHGIMTVPLTPAAAREVDVVGV-------FRYKNTwplCLE 320
Cdd:cd08276 226 GGRG--VDHVVEVGG-PGTLAQSIKAVAPGGVISLIGfLSGFEAPVLLLPLLTKGATLRGIavgsraqFEAMNR---AIE 299
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 15242240 321 fltsgKIDVKPLITHRFGFsqKEVEDAFETSARGSNAIKV 360
Cdd:cd08276 300 -----AHRIRPVIDRVFPF--EEAKEAYRYLESGSHFGKV 332
PLN02740 PLN02740
Alcohol dehydrogenase-like
32-354 2.99e-23

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 99.49  E-value: 2.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   32 QPFLLPSV-----GPHDVRVRMKAVGICGSDVHYLKTMRCADfvVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPG 106
Cdd:PLN02740  21 EPLVMEEIrvdppQKMEVRIKILYTSICHTDLSAWKGENEAQ--RAYPRILGHEAAGIVESVGEGVEDLKAGDHVIPIFN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  107 ISCWRCNLCREGRYNLCPEM---------------KFFAT----PPVH----GSLANQVVHPADLCFKLPENVSLEEgaM 163
Cdd:PLN02740  99 GECGDCRYCKRDKTNLCETYrvdpfksvmvndgktRFSTKgdgqPIYHflntSTFTEYTVLDSACVVKIDPNAPLKK--M 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  164 CEpLSVGVH-----ACRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVqvttNLE 238
Cdd:PLN02740 177 SL-LSCGVStgvgaAWNTANVQAGSSVAIFGLGAVGLAVAEGARARGASKIIGVDINPEKFEKGKEMGITDFI----NPK 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  239 DVGSEV-EQIQKAMGSNIDVTFDCAGFNKTMSTALAATRCG-GKVCLVGMGHGIMTVPLTPAA---AREV--DVVGVFRY 311
Cdd:PLN02740 252 DSDKPVhERIREMTGGGVDYSFECAGNVEVLREAFLSTHDGwGLTVLLGIHPTPKMLPLHPMElfdGRSItgSVFGDFKG 331
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 15242240  312 KNTWPLCLEFLTSGKIDVKPLITHRFGFSqkEVEDAFETSARG 354
Cdd:PLN02740 332 KSQLPNLAKQCMQGVVNLDGFITHELPFE--KINEAFQLLEDG 372
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
36-355 4.21e-23

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


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 98.06  E-value: 4.21e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  36 LPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRValepgiscwrcnlc 115
Cdd:cd08267  21 IPTPKPGEVLVKVHAASVNPVDWKLRRGPPKLLLGRPFPPIPGMDFAGEVVAVGSGVTRFKVGDEV-------------- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 116 regrYNLCPEMKFfatppvhGSLANQVVHPADLCFKLPENVSLEEGAmCEPLSvGVHAC----RRAEVGPETNVLVMGA- 190
Cdd:cd08267  87 ----FGRLPPKGG-------GALAEYVVAPESGLAKKPEGVSFEEAA-ALPVA-GLTALqalrDAGKVKPGQRVLINGAs 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 191 GPIGLVTMLAARAFsVPRIVIVDVDENrLAVAKQLGADEIVQVTTnlEDVGSEVEQIQKamgsnIDVTFDCAGFNK-TMS 269
Cdd:cd08267 154 GGVGTFAVQIAKAL-GAHVTGVCSTRN-AELVRSLGADEVIDYTT--EDFVALTAGGEK-----YDVIFDAVGNSPfSLY 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 270 TALAATRCGGKVCLVGMGHGIMTVPLTPAAARevdvVGVFRYKNTWPLC------LEFLT----SGKidVKPLITHRFGF 339
Cdd:cd08267 225 RASLALKPGGRYVSVGGGPSGLLLVLLLLPLT----LGGGGRRLKFFLAkpnaedLEQLAelveEGK--LKPVIDSVYPL 298
                       330
                ....*....|....*.
gi 15242240 340 SqkEVEDAFETSARGS 355
Cdd:cd08267 299 E--DAPEAYRRLKSGR 312
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
19-240 1.19e-22

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: 97.04  E-value: 1.19e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  19 MAAWLV---GINTLKIQPFLLPSVGPHDVRVRMKAVGIcgSDVHYlktmRCADFVVKEPM--VIGHECAGIIEEVGEEVK 93
Cdd:cd08264   1 MKALVFeksGIENLKVEDVKDPKPGPGEVLIRVKMAGV--NPVDY----NVINAVKVKPMphIPGAEFAGVVEEVGDHVK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  94 HLVVGDRVALEPGISCWRCNLCREGRYNLCPEMKFFATpPVHGSLANQVVHPADLCFKLPENVSLEEGAmcePLSVGV-- 171
Cdd:cd08264  75 GVKKGDRVVVYNRVFDGTCDMCLSGNEMLCRNGGIIGV-VSNGGYAEYIVVPEKNLFKIPDSISDELAA---SLPVAAlt 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242240 172 --HACRRAEVGPETNVLVMGA-GPIGLVTMLAARAFSVPRIVIvdvdeNRLAVAKQLGADEIVQVTTNLEDV 240
Cdd:cd08264 151 ayHALKTAGLGPGETVVVFGAsGNTGIFAVQLAKMMGAEVIAV-----SRKDWLKEFGADEVVDYDEVEEKV 217
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
192-324 1.37e-22

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 91.90  E-value: 1.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   192 PIGLVTMLAARAFSVpRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVgseVEQIQKAMGSN-IDVTFDCAGFNKTMST 270
Cdd:pfam00107   1 GVGLAAIQLAKAAGA-KVIAVDGSEEKLELAKELGADHVINPKE--TDL---VEEIKELTGGKgVDVVFDCVGSPATLEQ 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15242240   271 ALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRYK-NTWPLCLEFLTS 324
Cdd:pfam00107  75 ALKLLRPGGRVVVVGLPGGPLPLPLAPLLLKELTILGSFLGSpEEFPEALDLLAS 129
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
29-301 1.10e-21

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: 94.20  E-value: 1.10e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  29 LKIQPFLLPSVGPHDVRVRMKAVGICGSDV----HYLKTMRcadfvvKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALE 104
Cdd:cd08268  15 LRIEELPVPAPGAGEVLIRVEAIGLNRADAmfrrGAYIEPP------PLPARLGYEAAGVVEAVGAGVTGFAVGDRVSVI 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 105 PgiscwrcnlcregrynlcpemkfFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHAC--RRAEVGPE 182
Cdd:cd08268  89 P-----------------------AADLGQYGTYAEYALVPAAAVVKLPDGLSFVEAAALWMQYLTAYGAlvELAGLRPG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 183 TNVLVMGA-GPIGLVTMLAARAFSVPRIVIVDVDENRlAVAKQLGADEIVQvtTNLEDVGSEVEQIqkAMGSNIDVTFDC 261
Cdd:cd08268 146 DSVLITAAsSSVGLAAIQIANAAGATVIATTRTSEKR-DALLALGAAHVIV--TDEEDLVAEVLRI--TGGKGVDVVFDP 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15242240 262 AGfNKTMSTALAATRCGGKVCLVG-MGHGIMTVPLTPAAAR 301
Cdd:cd08268 221 VG-GPQFAKLADALAPGGTLVVYGaLSGEPTPFPLKAALKK 260
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
37-305 4.03e-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: 4.03e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  37 PSVGPHDVRVRMKAVGICGSDVH-----YLKTMRCADFvvkepMVIGHECAGIIEEVGEEvKHLVVGDRVALEPGISCWR 111
Cdd:cd08230  21 PEPTPGEVLVRTLEVGVCGTDREivageYGTAPPGEDF-----LVLGHEALGVVEEVGDG-SGLSPGDLVVPTVRRPPGK 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 112 CNLCREGRYNLCPEMKFF--ATPPVHGSLANQVVHPADLCFKLPENVSlEEGAMCEPLSVGVHA-------CRRAEVGPE 182
Cdd:cd08230  95 CLNCRIGRPDFCETGEYTerGIKGLHGFMREYFVDDPEYLVKVPPSLA-DVGVLLEPLSVVEKAieqaeavQKRLPTWNP 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 183 TNVLVMGAGPIGLVT--MLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTNLEDVGSEVEqiqkamgsnIDVTFD 260
Cdd:cd08230 174 RRALVLGAGPIGLLAalLLRLRGFEVYVLNRRDPPDPKADIVEELGATYVNSSKTPVAEVKLVGE---------FDLIIE 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15242240 261 CAGFNKTMSTALAATRCGGKVCLVGmghgimtvplTPAAAREVDV 305
Cdd:cd08230 245 ATGVPPLAFEALPALAPNGVVILFG----------VPGGGREFEV 279
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
37-360 5.15e-20

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 89.54  E-value: 5.15e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  37 PSVGPHDVRVRMKAVGicgsdVHYLKTM---RCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGIscwrcn 113
Cdd:cd08272  23 PQPGPGQVLVRVHASG-----VNPLDTKirrGGAAARPPLPAILGCDVAGVVEAVGEGVTRFRVGDEVYGCAGG------ 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 114 lcregrynlcpemkfFATPPvhGSLANQVVHPADLCFKLPENVSLEEGAmCEPLsVGVHA----CRRAEVGPETNVLVM- 188
Cdd:cd08272  92 ---------------LGGLQ--GSLAEYAVVDARLLALKPANLSMREAA-ALPL-VGITAweglVDRAAVQAGQTVLIHg 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 189 GAGPIGLVTMLAARAFSVprIVIVDVDENRLAVAKQLGADEIVQVTTNLedvgseVEQIQKAMGSN-IDVTFDCAGfNKT 267
Cdd:cd08272 153 GAGGVGHVAVQLAKAAGA--RVYATASSEKAAFARSLGADPIIYYRETV------VEYVAEHTGGRgFDVVFDTVG-GET 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 268 MSTALAATRC-GGKVCLVGMGhgimTVPLTPAAAREVDVVGVF----------RYKNTWPL--CLEFLTSGKIdvKPLI- 333
Cdd:cd08272 224 LDASFEAVALyGRVVSILGGA----THDLAPLSFRNATYSGVFtllplltgegRAHHGEILreAARLVERGQL--RPLLd 297
                       330       340
                ....*....|....*....|....*..
gi 15242240 334 THRFGFSqkEVEDAFETSARGSNAIKV 360
Cdd:cd08272 298 PRTFPLE--EAAAAHARLESGSARGKI 322
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
19-361 3.58e-19

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: 87.11  E-value: 3.58e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  19 MAAWLV----GINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDV-----HYlktmrcadfvvkePM------VIGHECAG 83
Cdd:cd05276   1 MKAIVIkepgGPEVLELGEVPKPAPGPGEVLIRVAAAGVNRADLlqrqgLY-------------PPppgasdILGLEVAG 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  84 IIEEVGEEVKHLVVGDRV-ALEPGiscwrcnlcreGRYnlcpemkffatppvhgslANQVVHPADLCFKLPENVSLEEGA 162
Cdd:cd05276  68 VVVAVGPGVTGWKVGDRVcALLAG-----------GGY------------------AEYVVVPAGQLLPVPEGLSLVEAA 118
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 163 -MCEPLSVGVHA-CRRAEVGPETNVLVM-GAGPIGLVTMLAARAFSVPRIVIVDVDEnRLAVAKQLGADeiVQVTTNLED 239
Cdd:cd05276 119 aLPEVFFTAWQNlFQLGGLKAGETVLIHgGASGVGTAAIQLAKALGARVIATAGSEE-KLEACRALGAD--VAINYRTED 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 240 VgseVEQIQKAMGSN-IDVTFDCAG---FNKTMStALAAtrcGGKVCLVGMGHGIMT-VPLTPAAAREVDVVG-VFR--- 310
Cdd:cd05276 196 F---AEEVKEATGGRgVDVILDMVGgdyLARNLR-ALAP---DGRLVLIGLLGGAKAeLDLAPLLRKRLTLTGsTLRsrs 268
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242240 311 --YK---------NTWPLclefLTSGKIdvKPLITHRFGFSqkEVEDAFETSARGSNAIKVM 361
Cdd:cd05276 269 leEKaalaaafreHVWPL----FASGRI--RPVIDKVFPLE--EAAEAHRRMESNEHIGKIV 322
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
40-297 9.47e-19

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 86.47  E-value: 9.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   40 GPHDVRVRMKAVGICGSDVHYLKTmrcaDF-VVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALepGI---SCWRCNLC 115
Cdd:PLN02586  36 GDEDVTVKILYCGVCHSDLHTIKN----EWgFTRYPIVPGHEIVGIVTKLGKNVKKFKEGDRVGV--GVivgSCKSCESC 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  116 REGRYNLCPEMKFFATPPVH------GSLANQVVHPADLCFKLPENVSLEEGA--MCEPLSVGVHACRRAEVGPETNVLV 187
Cdd:PLN02586 110 DQDLENYCPKMIFTYNSIGHdgtknyGGYSDMIVVDQHFVLRFPDNLPLDAGAplLCAGITVYSPMKYYGMTEPGKHLGV 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  188 MGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVqvttnledVGSEVEQIQKAMGSnIDVTFDCAGFNKT 267
Cdd:PLN02586 190 AGLGGLGHVAVKIGKAFGLKVTVISSSSNKEDEAINRLGADSFL--------VSTDPEKMKAAIGT-MDYIIDTVSAVHA 260
                        250       260       270
                 ....*....|....*....|....*....|
gi 15242240  268 MSTALAATRCGGKVCLVGMGHGIMTVPLTP 297
Cdd:PLN02586 261 LGPLLGLLKVNGKLITLGLPEKPLELPIFP 290
sorbose_phosphate_red cd08238
L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, ...
16-225 3.98e-18

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: 84.80  E-value: 3.98e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  16 EENMAAWLVGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKT----MRCADFVVKEPMVIGHECAGIIEEVGEE 91
Cdd:cd08238   1 MKTKAWRMYGKGDLRLEKFELPEIADDEILVRVISDSLCFSTWKLALQgsdhKKVPNDLAKEPVILGHEFAGTILKVGKK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  92 VKH-LVVGDRVALEPgiscwrcNLCREGRYNlCPEMKFfatpPVHGSLANQVVHPADL----CFKLPENVSLEEGAMCEP 166
Cdd:cd08238  81 WQGkYKPGQRFVIQP-------ALILPDGPS-CPGYSY----TYPGGLATYHIIPNEVmeqdCLLIYEGDGYAEASLVEP 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242240 167 LS--VG-VHACRRAEVGPETN----------VLVMGAGPIGLvtMLAARAFSVP----RIVIVDVDENRLAVAKQL 225
Cdd:cd08238 149 LScvIGaYTANYHLQPGEYRHrmgikpggntAILGGAGPMGL--MAIDYAIHGPigpsLLVVTDVNDERLARAQRL 222
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
25-263 5.64e-18

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


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 83.79  E-value: 5.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  25 GINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDV-----HYLKTMRCadfvvkePMVIGHECAGIIEEVGEEVKHLVVGD 99
Cdd:cd08275  10 GLDKLKVEKEALPEPSSGEVRVRVEACGLNFADLmarqgLYDSAPKP-------PFVPGFECAGTVEAVGEGVKDFKVGD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 100 RVALepgiscwrcnLCREGRYnlcpemkffatppvhgslANQVVHPADLCFKLPENVSLEEGAMCepLSVGVHA----CR 175
Cdd:cd08275  83 RVMG----------LTRFGGY------------------AEVVNVPADQVFPLPDGMSFEEAAAF--PVNYLTAyyalFE 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 176 RAEVGPETNVLV-MGAGPIGLvtMLAARAFSVPRIVIV-DVDENRLAVAKQLGADE-IVQVTTNLedvgseVEQIQKAMG 252
Cdd:cd08275 133 LGNLRPGQSVLVhSAAGGVGL--AAGQLCKTVPNVTVVgTASASKHEALKENGVTHvIDYRTQDY------VEEVKKISP 204
                       250
                ....*....|.
gi 15242240 253 SNIDVTFDCAG 263
Cdd:cd08275 205 EGVDIVLDALG 215
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
28-362 1.43e-17

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: 82.33  E-value: 1.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  28 TLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLkTMRCADFVVKePMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGI 107
Cdd:cd05282  13 VLELVSLPIPPPGPGEVLVRMLAAPINPSDLITI-SGAYGSRPPL-PAVPGNEGVGVVVEVGSGVSGLLVGQRVLPLGGE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 108 SCWRcnlcregrynlcpemkffatppvhgslaNQVVHPADLCFKLPENVSLEEGAMC--EPLSVGVHACRRAEVGPETNV 185
Cdd:cd05282  91 GTWQ----------------------------EYVVAPADDLIPVPDSISDEQAAMLyiNPLTAWLMLTEYLKLPPGDWV 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 186 LVMGAGP-IG--LVTMLAARAFSVPRIVIVDVDENRLavaKQLGADEIvqVTTNLEDVGSEVEQIQKAMGsnIDVTFDCA 262
Cdd:cd05282 143 IQNAANSaVGrmLIQLAKLLGFKTINVVRRDEQVEEL---KALGADEV--IDSSPEDLAQRVKEATGGAG--ARLALDAV 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 263 GFNKTmSTALAATRCGGKVCLVG-MGHGIMTVPLTPAAAREVDVVGVF-------RYKNTWPLCLEFLT----SGKIdvK 330
Cdd:cd05282 216 GGESA-TRLARSLRPGGTLVNYGlLSGEPVPFPRSVFIFKDITVRGFWlrqwlhsATKEAKQETFAEVIklveAGVL--T 292
                       330       340       350
                ....*....|....*....|....*....|..
gi 15242240 331 PLITHRFGFSqkEVEDAFETSARGSNAIKVMF 362
Cdd:cd05282 293 TPVGAKFPLE--DFEEAVAAAEQPGRGGKVLL 322
quinone_pig3 TIGR02824
putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative ...
29-361 4.65e-17

putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative quinone oxidoreductases that belong to the broader superfamily (modeled by Pfam pfam00107) of zinc-dependent alcohol (of medium chain length) dehydrogenases and quinone oxiooreductases. The alignment shows no motif of conserved Cys residues as are found in zinc-binding members of the superfamily, and members are likely to be quinone oxidoreductases instead. A member of this family in Homo sapiens, PIG3, is induced by p53 but is otherwise uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274316 [Multi-domain]  Cd Length: 325  Bit Score: 80.77  E-value: 4.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240    29 LKIQPFLLPSVGPHDVRVRMKAVGICGSDVhyLKTMRcadfvvKEPM------VIGHECAGIIEEVGEEVKHLVVGDRVa 102
Cdd:TIGR02824  15 LVLVEVPLPVPKAGEVLIRVAAAGVNRPDL--LQRAG------KYPPppgasdILGLEVAGEVVAVGEGVSRWKVGDRV- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   103 lepgiscwrCNLCREGRYnlcpemkffatppvhgslANQVVHPADLCFKLPENVSLEEGAMCeP---LSVGVHACRRAEV 179
Cdd:TIGR02824  86 ---------CALVAGGGY------------------AEYVAVPAGQVLPVPEGLSLVEAAAL-PetfFTVWSNLFQRGGL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   180 GPETNVLVM-GAGPIGLVTMLAARAFSVPRIVIVDVDEnRLAVAKQLGADEIVQVTTnlEDVGSEVEQIQKAMGsnIDVT 258
Cdd:TIGR02824 138 KAGETVLIHgGASGIGTTAIQLAKAFGARVFTTAGSDE-KCAACEALGADIAINYRE--EDFVEVVKAETGGKG--VDVI 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   259 FDCAG---FNKTMStALAAtrcGGKVCLVGMGHG-IMTVPLTPAAAREVDVVGV----------------FRyKNTWPLc 318
Cdd:TIGR02824 213 LDIVGgsyLNRNIK-ALAL---DGRIVQIGFQGGrKAELDLGPLLAKRLTITGStlrarpvaekaaiaaeLR-EHVWPL- 286
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 15242240   319 lefLTSGKIdvKPLITHRFGFSQkeVEDAFETSARGSNAIKVM 361
Cdd:TIGR02824 287 ---LASGRV--RPVIDKVFPLED--AAQAHALMESGDHIGKIV 322
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
38-359 3.54e-16

Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member of the medium chain dehydrogenase/ reductase (MDR) family. Riticulons are endoplasmic reticulum associated proteins involved in membrane trafficking and neuroendocrine secretion. The MDR/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 78.80  E-value: 3.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  38 SVGPHDVRVRmkavgiCGSDVHYLKTMRCADFVVKE----PMVIGHECAGIIEEVGEEVKHLVVGDRVALepgiscwrcn 113
Cdd:cd08248  40 SVNPIDVLMR------SGYGRTLLNKKRKPQSCKYSgiefPLTLGRDCSGVVVDIGSGVKSFEIGDEVWG---------- 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 114 lcregrynlcpemkffATPPVH-GSLANQVVHPADLCFKLPENVSLEEGAmceplSVGVHAC-------RRAEVGPET-- 183
Cdd:cd08248 104 ----------------AVPPWSqGTHAEYVVVPENEVSKKPKNLSHEEAA-----SLPYAGLtawsalvNVGGLNPKNaa 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 184 --NVLVMGA-GPIGLVTMLAARAFSVprIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVGSEVEQIQKamgsnIDVTFD 260
Cdd:cd08248 163 gkRVLILGGsGGVGTFAIQLLKAWGA--HVTTTCSTDAIPLVKSLGADDVIDYNN--EDFEEELTERGK-----FDVILD 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 261 CAGFNKTMSTALAATRCGGKVCLVG--MG----HGIMTVPLTPAAAREVDVVGVFRYKNT--W------PLCLEFLT--- 323
Cdd:cd08248 234 TVGGDTEKWALKLLKKGGTYVTLVSplLKntdkLGLVGGMLKSAVDLLKKNVKSLLKGSHyrWgffspsGSALDELAklv 313
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 15242240 324 -SGKIdvKPLITHRFGFSqkEVEDAFE----TSARGSNAIK 359
Cdd:cd08248 314 eDGKI--KPVIDKVFPFE--EVPEAYEkvesGHARGKTVIK 350
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
42-243 4.37e-16

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: 77.61  E-value: 4.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  42 HDVRVRMKAVGICGSDVhylktMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVAlepGIScwrcnlcregryn 121
Cdd:cd05195   1 DEVEVEVKAAGLNFRDV-----LVALGLLPGDETPLGLECSGIVTRVGSGVTGLKVGDRVM---GLA------------- 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 122 lcpemkffatppvHGSLANQVVHPADLCFKLPENVSLEEGAmceplSVGVHAC-------RRAEVGPETNVLVM-GAGPI 193
Cdd:cd05195  60 -------------PGAFATHVRVDARLVVKIPDSLSFEEAA-----TLPVAYLtayyalvDLARLQKGESVLIHaAAGGV 121
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15242240 194 GlvtmLAArafsvprivivdvdenrLAVAKQLGADeiVQVTtnledVGSE 243
Cdd:cd05195 122 G----QAA-----------------IQLAQHLGAE--VFAT-----VGSE 143
PLN02827 PLN02827
Alcohol dehydrogenase-like
40-349 1.33e-15

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 77.25  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   40 GPHDVRVRMKAVGICGSDVHYLKTMrcADFvvkePMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCREGR 119
Cdd:PLN02827  36 QPLEIRIKVVSTSLCRSDLSAWESQ--ALF----PRIFGHEASGIVESIGEGVTEFEKGDHVLTVFTGECGSCRHCISGK 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  120 YNLCPEM----------------KFFATPPVH----GSLANQVVHPADLCFKLPENVSLEEGAMcepLSVGVHA-----C 174
Cdd:PLN02827 110 SNMCQVLglerkgvmhsdqktrfSIKGKPVYHycavSSFSEYTVVHSGCAVKVDPLAPLHKICL---LSCGVAAglgaaW 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  175 RRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVqvttNLEDVGSEVEQIQKAM-GS 253
Cdd:PLN02827 187 NVADVSKGSSVVIFGLGTVGLSVAQGAKLRGASQIIGVDINPEKAEKAKTFGVTDFI----NPNDLSEPIQQVIKRMtGG 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  254 NIDVTFDCAGFNKTMSTALAAtrcggkvCLVGMGhgiMTVPL-TPAAAREVD---------------VVGVFRYKNTWPL 317
Cdd:PLN02827 263 GADYSFECVGDTGIATTALQS-------CSDGWG---LTVTLgVPKAKPEVSahyglflsgrtlkgsLFGGWKPKSDLPS 332
                        330       340       350
                 ....*....|....*....|....*....|..
gi 15242240  318 CLEFLTSGKIDVKPLITHRFGFSqkEVEDAFE 349
Cdd:PLN02827 333 LVDKYMNKEIMIDEFITHNLSFD--EINKAFE 362
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
34-285 1.75e-15

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 76.76  E-value: 1.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   34 FLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADfvvKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALepGISCWRCN 113
Cdd:PLN02514  27 YTLRKTGPEDVVIKVIYCGICHTDLHQIKNDLGMS---NYPMVPGHEVVGEVVEVGSDVSKFTVGDIVGV--GVIVGCCG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  114 LCREGRYNL---CPEMKFFAT------PPVHGSLANQVVHPADLCFKLPENVSLEEGA--MCEPLSVGVHACRRAEVGPE 182
Cdd:PLN02514 102 ECSPCKSDLeqyCNKRIWSYNdvytdgKPTQGGFASAMVVDQKFVVKIPEGMAPEQAAplLCAGVTVYSPLSHFGLKQSG 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  183 TNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVqvttnledVGSEVEQIQKAmGSNIDVTFDCA 262
Cdd:PLN02514 182 LRGGILGLGGVGHMGVKIAKAMGHHVTVISSSDKKREEALEHLGADDYL--------VSSDAAEMQEA-ADSLDYIIDTV 252
                        250       260
                 ....*....|....*....|...
gi 15242240  263 GFNKTMSTALAATRCGGKVCLVG 285
Cdd:PLN02514 253 PVFHPLEPYLSLLKLDGKLILMG 275
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
19-285 7.07e-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: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 68.46  E-value: 7.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  19 MAAWLV----GINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADfvvKEPMVIGHECAGIIEEVGEEVKH 94
Cdd:cd08271   1 MKAWVLpkpgAALQLTLEEIEIPGPGAGEVLVKVHAAGLNPVDWKVIAWGPPAW---SYPHVPGVDGAGVVVAVGAKVTG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  95 LVVGDRVAlepgiscWRCNLCRegrynlcpemkffatppvHGSLANQVVHPADLCFKLPENVSLEEGAM--CEPLSVGVH 172
Cdd:cd08271  78 WKVGDRVA-------YHASLAR------------------GGSFAEYTVVDARAVLPLPDSLSFEEAAAlpCAGLTAYQA 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 173 ACRRAEVGPETNVLVMGA-GPIGLVTM-LAARAFSVpriVIVDVDENRLAVAKQLGADEIVQVTTnlEDVGSEVEQIQKA 250
Cdd:cd08271 133 LFKKLRIEAGRTILITGGaGGVGSFAVqLAKRAGLR---VITTCSKRNFEYVKSLGADHVIDYND--EDVCERIKEITGG 207
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15242240 251 MGsnIDVTFDCAGfnKTMSTALAAT--RCGGKVCLVG 285
Cdd:cd08271 208 RG--VDAVLDTVG--GETAAALAPTlaFNGHLVCIQG 240
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
46-162 1.01e-12

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 67.80  E-value: 1.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240     46 VRMKAVGICGSDVhyLKTMRcadfVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVAlepGIscwrcnlcregrynlcpe 125
Cdd:smart00829   1 IEVRAAGLNFRDV--LIALG----LYPGEAVLGGECAGVVTRVGPGVTGLAVGDRVM---GL------------------ 53
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 15242240    126 mkffatppVHGSLANQVVHPADLCFKLPENVSLEEGA 162
Cdd:smart00829  54 --------APGAFATRVVTDARLVVPIPDGWSFEEAA 82
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
37-309 2.13e-12

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: 67.01  E-value: 2.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  37 PSVGPHDVRVRMKAVGicgsdVHYLKTM----RCADFVVKE-PMVIGHECAGIIEEVGEEVKHLVVGDRVALEpgiscwr 111
Cdd:cd08244  23 PVPGPGQVRIAVAAAG-----VHFVDTQlrsgWGPGPFPPElPYVPGGEVAGVVDAVGPGVDPAWLGRRVVAH------- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 112 cnlcregrynlcpemkffaTPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCepLSVGVHAC---RRAEVGPETNVLVM 188
Cdd:cd08244  91 -------------------TGRAGGGYAELAVADVDSLHPVPDGLDLEAAVAV--VHDGRTALgllDLATLTPGDVVLVT 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 189 GA-GPIG-LVTMLAARAFSvpRIVIVDVDENRLAVAKQLGADEIVQVTtnLEDVGSEVEqiQKAMGSNIDVTFDCAGfNK 266
Cdd:cd08244 150 AAaGGLGsLLVQLAKAAGA--TVVGAAGGPAKTALVRALGADVAVDYT--RPDWPDQVR--EALGGGGVTVVLDGVG-GA 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15242240 267 TMSTALAATRCGGKVCLVGMGHGIMT-VPLTPAAAREVDVVGVF 309
Cdd:cd08244 223 IGRAALALLAPGGRFLTYGWASGEWTaLDEDDARRRGVTVVGLL 266
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
40-297 6.29e-12

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 66.20  E-value: 6.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   40 GPHDVRVRMKAVGICGSDVHYLKTMRCadfVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGI-SCWRCNLCREG 118
Cdd:PLN02178  30 GENDVTVKILFCGVCHSDLHTIKNHWG---FSRYPIIPGHEIVGIATKVGKNVTKFKEGDRVGVGVIIgSCQSCESCNQD 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  119 RYNLCPEMKFFATPPVHGSLANQ------VVHPADLCFKLPENVSLEEGA--MCEPLSVgVHACRRAEVGPET--NVLVM 188
Cdd:PLN02178 107 LENYCPKVVFTYNSRSSDGTRNQggysdvIVVDHRFVLSIPDGLPSDSGAplLCAGITV-YSPMKYYGMTKESgkRLGVN 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  189 GAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVqvttnledVGSEVEQIQKAMGSnIDVTFDCAGFNKTM 268
Cdd:PLN02178 186 GLGGLGHIAVKIGKAFGLRVTVISRSSEKEREAIDRLGADSFL--------VTTDSQKMKEAVGT-MDFIIDTVSAEHAL 256
                        250       260
                 ....*....|....*....|....*....
gi 15242240  269 STALAATRCGGKVCLVGMGHGIMTVPLTP 297
Cdd:PLN02178 257 LPLFSLLKVSGKLVALGLPEKPLDLPIFP 285
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
37-227 2.13e-11

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


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 64.75  E-value: 2.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  37 PSVGPHDVRVRMKAVGICGSDVHYLKTM------RCADFVVKEPM-VIGHECAGIIEEVGEEVKHLVVGDRVALEPGISC 109
Cdd:cd08246  38 PELGPGEVLVAVMAAGVNYNNVWAALGEpvstfaARQRRGRDEPYhIGGSDASGIVWAVGEGVKNWKVGDEVVVHCSVWD 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 110 WRCNLCREGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAmCEPLsVGVHACRR------AEVGPET 183
Cdd:cd08246 118 GNDPERAGGDPMFDPSQRIWGYETNYGSFAQFALVQATQLMPKPKHLSWEEAA-AYML-VGATAYRMlfgwnpNTVKPGD 195
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15242240 184 NVLVMGA-GPIG-LVTMLAARAFSVPriVIVDVDENRLAVAKQLGA 227
Cdd:cd08246 196 NVLIWGAsGGLGsMAIQLARAAGANP--VAVVSSEEKAEYCRALGA 239
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
25-355 3.59e-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: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 63.44  E-value: 3.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  25 GINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVhylkTMR--CADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVA 102
Cdd:cd08273  11 GPEVLKVVEADLPEPAAGEVVVKVEASGVSFADV----QMRrgLYPDQPPLPFTPGYDLVGRVDALGSGVTGFEVGDRVA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 103 lepgiscwrcnlcregrynlcpemkffATPPVhGSLANQVVHPADLCFKLPENVSLEEgAMCEPLsVGVHAC----RRAE 178
Cdd:cd08273  87 ---------------------------ALTRV-GGNAEYINLDAKYLVPVPEGVDAAE-AVCLVL-NYVTAYqmlhRAAK 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 179 VGPETNVLVMGA-GPIGLVTMLAARAFSVPriVIVDVDENRLAVAKQLGADEIVQVTtnledvgSEVEQIQKAMGSnIDV 257
Cdd:cd08273 137 VLTGQRVLIHGAsGGVGQALLELALLAGAE--VYGTASERNHAALRELGATPIDYRT-------KDWLPAMLTPGG-VDV 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 258 TFDCAGFnKTMSTALAATRCGGKVCLVGM-----GHGIMTVPLTPAAA-----------REVDVVGVFRYKNTWP----- 316
Cdd:cd08273 207 VFDGVGG-ESYEESYAALAPGGTLVCYGGnssllQGRRSLAALGSLLArlaklkllptgRRATFYYVWRDRAEDPklfrq 285
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 15242240 317 ---LCLEFLTSGKIdvKPLITHRFGFSqkEVEDAFETSARGS 355
Cdd:cd08273 286 dltELLDLLAKGKI--RPKIAKRLPLS--EVAEAHRLLESGK 323
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
26-263 8.89e-11

2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176251 [Multi-domain]  Cd Length: 324  Bit Score: 62.24  E-value: 8.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  26 INTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMrcADFVVKEPMVIGHECAGIIEEVGEEVKH-LVVGDRVAle 104
Cdd:cd08291  15 VKELSLPEPEVPEPGPGEVLIKVEAAPINPSDLGFLKGQ--YGSTKALPVPPGFEGSGTVVAAGGGPLAqSLIGKRVA-- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 105 pgisCWrcnlcregrynlcpemkffatPPVHGSLANQVVHPADLCFKLPENVSLEEGAMC--EPLSV-GVHACRRAEvGP 181
Cdd:cd08291  91 ----FL---------------------AGSYGTYAEYAVADAQQCLPLPDGVSFEQGASSfvNPLTAlGMLETAREE-GA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 182 ETNVLVMGAGPIGlvTMLA--ARAFSVPRIVIVDVDEnRLAVAKQLGADEIvqVTTNLEDVGSEVEQIQKAMGSNIdvTF 259
Cdd:cd08291 145 KAVVHTAAASALG--RMLVrlCKADGIKVINIVRRKE-QVDLLKKIGAEYV--LNSSDPDFLEDLKELIAKLNATI--FF 217

                ....
gi 15242240 260 DCAG 263
Cdd:cd08291 218 DAVG 221
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
26-308 1.26e-10

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: 61.97  E-value: 1.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  26 INTLKIQPFLLPSVGPHDVRVRMKAVGICGSDvhyLKTMRCADFVVKE-PMVIGHECAGIIEEVGEEVKHLVVGDRVAle 104
Cdd:cd08292  13 ADVLEIGEVPKPTPGAGEVLVRTTLSPIHNHD---LWTIRGTYGYKPElPAIGGSEAVGVVDAVGEGVKGLQVGQRVA-- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 105 pgiscwrcnlcregrynlcpemkFFatpPVHGSLANQVVHPADLCFKLPENVSLEEGAM--CEPLSvGVHACRRAEVGP- 181
Cdd:cd08292  88 -----------------------VA---PVHGTWAEYFVAPADGLVPLPDGISDEVAAQliAMPLS-ALMLLDFLGVKPg 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 182 ETNVLVMGAGPIG-LVTMLA-ARAFSVPRIVivdvdeNRLAVAKQLGADEIVQV-TTNLEDVGSEVEQIqkAMGSNIDVT 258
Cdd:cd08292 141 QWLIQNAAGGAVGkLVAMLAaARGINVINLV------RRDAGVAELRALGIGPVvSTEQPGWQDKVREA--AGGAPISVA 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242240 259 FDCAGfNKTMSTALAATRCGGKVCLVG-MGHGIMTVPLTPAAAREVDVVGV 308
Cdd:cd08292 213 LDSVG-GKLAGELLSLLGEGGTLVSFGsMSGEPMQISSGDLIFKQATVRGF 262
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
28-286 9.00e-10

Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 59.16  E-value: 9.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  28 TLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHylkTMRCADFVVKEPMVIGHECAGIIEEVGEEvkHLVVGDRVALEPGi 107
Cdd:cd08243  14 VLKLREIPIPEPKPGWVLIRVKAFGLNRSEIF---TRQGHSPSVKFPRVLGIEAVGEVEEAPGG--TFTPGQRVATAMG- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 108 scwrcnlcregrynlcpEMKFfatpPVHGSLANQVVHPADLCFKLPENVSLEE-GAMCEPLSVGVHACRRA-EVGPETNV 185
Cdd:cd08243  88 -----------------GMGR----TFDGSYAEYTLVPNEQVYAIDSDLSWAElAALPETYYTAWGSLFRSlGLQPGDTL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 186 LVMGA-GPIGLVTMLAARAFSvPRIVIVDVDENRLAVAKQLGADEIVQvttnleDVGSEVEQIQKAMGSnIDVTFDCAGf 264
Cdd:cd08243 147 LIRGGtSSVGLAALKLAKALG-ATVTATTRSPERAALLKELGADEVVI------DDGAIAEQLRAAPGG-FDKVLELVG- 217
                       250       260
                ....*....|....*....|..
gi 15242240 265 NKTMSTALAATRCGGKVCLVGM 286
Cdd:cd08243 218 TATLKDSLRHLRPGGIVCMTGL 239
ribitol-5-phosphate_DH cd08237
ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of ...
43-263 1.34e-09

ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of the MDR/zinc-dependent alcohol dehydrogenase-like family, oxidizes the phosphate ester of ribitol-5-phosphate to xylulose-5-phosphate of 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-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: 176199 [Multi-domain]  Cd Length: 341  Bit Score: 58.91  E-value: 1.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  43 DVRVRMKAVGICGSDVHYLKTMRCADFVVKE-PMVIGHEcaGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCREgryN 121
Cdd:cd08237  27 WVIVRPTYLSICHADQRYYQGNRSPEALKKKlPMALIHE--GIGVVVSDPTGTYKVGTKVVMVPNTPVEKDEIIPE---N 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 122 LCPEMKFFATPpVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAE---VGPETNVLVMGAGPIGLVTM 198
Cdd:cd08237 102 YLPSSRFRSSG-YDGFMQDYVFLPPDRLVKLPDNVDPEVAAFTELVSVGVHAISRFEqiaHKDRNVIGVWGDGNLGYITA 180
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242240 199 LAAR-AFSVPRIVIVDVDENRLavAKQLGADEIVQVTTNLEDVgseveqiqkamgsNIDVTFDCAG 263
Cdd:cd08237 181 LLLKqIYPESKLVVFGKHQEKL--DLFSFADETYLIDDIPEDL-------------AVDHAFECVG 231
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
25-263 4.29e-09

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 57.35  E-value: 4.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   25 GINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDV-----HYLKTMRCADfvvkepmVIGHECAGIIEEVGEEVKHLVVGD 99
Cdd:PTZ00354  12 GVDVLKIGESPKPAPKRNDVLIKVSAAGVNRADTlqrqgKYPPPPGSSE-------ILGLEVAGYVEDVGSDVKRFKEGD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  100 RV-ALEPGiscwrcnlcregrynlcpemkffatppvhGSLANQVVHPADLCFKLPENVSLEE-GAMCEPLSVGVHACRR- 176
Cdd:PTZ00354  85 RVmALLPG-----------------------------GGYAEYAVAHKGHVMHIPQGYTFEEaAAIPEAFLTAWQLLKKh 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  177 AEVGPETNVLV-MGAGPIGLVTMLAARAFSVPRIVIVDVDEnRLAVAKQLGADEIVQVTTNLedvGSEVEQIQKAMGSNI 255
Cdd:PTZ00354 136 GDVKKGQSVLIhAGASGVGTAAAQLAEKYGAATIITTSSEE-KVDFCKKLAAIILIRYPDEE---GFAPKVKKLTGEKGV 211

                 ....*...
gi 15242240  256 DVTFDCAG 263
Cdd:PTZ00354 212 NLVLDCVG 219
PRK10754 PRK10754
NADPH:quinone reductase;
25-277 8.38e-09

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 56.28  E-value: 8.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   25 GINTLKIQPFLLPSVGPHDVRVRMKAVGIcgsdvHYLKT-MRCADFVVKE-PMVIGHECAGIIEEVGEEVKHLVVGDRVA 102
Cdd:PRK10754  12 GPEVLQAVEFTPADPAENEVQVENKAIGI-----NYIDTyIRSGLYPPPSlPSGLGTEAAGVVSKVGSGVKHIKVGDRVV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  103 lepgiscwrcnlcregrYNLCPemkFFATPPVHGSLANQVVhpadlcfKLPENVSLEEGAMCEPLSVGVHACRRA--EVG 180
Cdd:PRK10754  87 -----------------YAQSA---LGAYSSVHNVPADKAA-------ILPDAISFEQAAASFLKGLTVYYLLRKtyEIK 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  181 P-ETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDEnRLAVAKQLGADEIVQVTTnlEDVGSEVEQIQKamGSNIDVTF 259
Cdd:PRK10754 140 PdEQFLFHAAAGGVGLIACQWAKALGAKLIGTVGSAQ-KAQRAKKAGAWQVINYRE--ENIVERVKEITG--GKKVRVVY 214
                        250
                 ....*....|....*...
gi 15242240  260 DCAGfnktMSTALAATRC 277
Cdd:PRK10754 215 DSVG----KDTWEASLDC 228
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
37-101 4.01e-08

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


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 54.45  E-value: 4.01e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242240  37 PSVGPHDVRVRMKAVGICGSDVhylKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRV 101
Cdd:cd08252  26 PVPGGRDLLVRVEAVSVNPVDT---KVRAGGAPVPGQPKILGWDASGVVEAVGSEVTLFKVGDEV 87
Glu_dehyd_C pfam16912
Glucose dehydrogenase C-terminus;
161-360 1.18e-07

Glucose dehydrogenase C-terminus;


Pssm-ID: 407146 [Multi-domain]  Cd Length: 211  Bit Score: 51.56  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   161 GAMCEPLSVGV----HACR---RAEVGPETnVLVMGAGPIGLVT---MLAARAFSvpRIVIV---DVDENRLAVAKQLGA 227
Cdd:pfam16912   4 GFLVEPLSIVEkaieHAEAsrsRFEWRPRS-ALVLGNGPLGLLAlamLRVQRGFD--RVYCLgrrDRPDPTIDLVEELGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   228 DEIVQVTTNLEDVGSEVEQiqkamgsnIDVTFDCAGFNKTMSTALAATRCGGKVCLVGMGHGiMTVPLTPAAA-REV--- 303
Cdd:pfam16912  81 TYVDSRETPVDEIPAAHEP--------MDLVYEATGYAPHAFEAIDALAPNGVAALLGVPTS-WTFEIDGGALhRELvlh 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242240   304 --DVVG-VFRYKNTWPLCLEFLTSGKIDV-KPLITHRFGFSqkEVEDAFEtsaRGSNAIKV 360
Cdd:pfam16912 152 nkALVGsVNANRRHFEAAADTLAAAPEWFlDALVTGVVPLD--EFEEAFE---DGDDDIKT 207
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
40-257 2.68e-07

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: 51.66  E-value: 2.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  40 GPHDVRVRMKAVGICGSDVHYLK----TMRcadfvvKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGiscwrcnlc 115
Cdd:cd08251   6 GPGEVRIQVRAFSLNFGDLLCVRglypTMP------PYPFTPGFEASGVVRAVGPHVTRLAVGDEVIAGTG--------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 116 regrynlcPEMkffatppvhGSLANQVVHPADLCFKLPENVSLEEGamCEPLSVG---VHACRRAEVGPETNVLVMGA-G 191
Cdd:cd08251  71 --------ESM---------GGHATLVTVPEDQVVRKPASLSFEEA--CALPVVFltvIDAFARAGLAKGEHILIQTAtG 131
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15242240 192 PIGLVTMLAARAFSVpRIVIVDVDENRLAVAKQLGADEIVQVTTnlEDVGSEVEQIQKAMGsnIDV 257
Cdd:cd08251 132 GTGLMAVQLARLKGA-EIYATASSDDKLEYLKQLGVPHVINYVE--EDFEEEIMRLTGGRG--VDV 192
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
30-154 1.77e-06

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: 49.18  E-value: 1.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  30 KIQPFLLPSVGPHDVRVRMKAVGICGSDVHYlktmrCA---DFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALepg 106
Cdd:cd08250  19 SIVDVPVPLPGPGEVLVKNRFVGINASDINF-----TAgryDPGVKPPFDCGFEGVGEVVAVGEGVTDFKVGDAVAT--- 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15242240 107 iscwrcnlcregrynlcpeMKFfatppvhGSLANQVVHPADLCFKLPE 154
Cdd:cd08250  91 -------------------MSF-------GAFAEYQVVPARHAVPVPE 112
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
135-308 6.40e-06

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


Pssm-ID: 274315 [Multi-domain]  Cd Length: 323  Bit Score: 47.55  E-value: 6.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   135 HGSLANQVVHPADLCFKLPENVSLEEG----------AMCeplsvgVHACRRAEVGPETN-VLVMGA----GPIGlVTML 199
Cdd:TIGR02823  94 DGGYSQYARVPADWLVPLPEGLSLREAmalgtagftaALS------VMALERNGLTPEDGpVLVTGAtggvGSLA-VAIL 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240   200 AARAFSVpriVIVDVDENRLAVAKQLGADEIVQVttnledvgSEVEQIQKAMGSNI-DVTFDCAGfNKTMSTALAATRCG 278
Cdd:TIGR02823 167 SKLGYEV---VASTGKAEEEDYLKELGASEVIDR--------EDLSPPGKPLEKERwAGAVDTVG-GHTLANVLAQLKYG 234
                         170       180       190
                  ....*....|....*....|....*....|..
gi 15242240   279 GKVCLVGMGHGiMTVPLT--PAAAREVDVVGV 308
Cdd:TIGR02823 235 GAVAACGLAGG-PDLPTTvlPFILRGVSLLGI 265
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
29-362 2.54e-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: 2.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  29 LKIQPFLLPSVGPHD-VRVRMKAVGICGSDVHYL--KTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRValep 105
Cdd:cd08290  16 LQLESYEIPPPGPPNeVLVKMLAAPINPADINQIqgVYPIKPPTTPEPPAVGGNEGVGEVVKVGSGVKSLKPGDWV---- 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 106 giscwrcnlcregrynlcpemkfFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAMcepLSVGVHACRR-----AEVG 180
Cdd:cd08290  92 -----------------------IPLRPGLGTWRTHAVVPADDLIKVPNDVDPEQAAT---LSVNPCTAYRlledfVKLQ 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 181 PETNVLVMGAGP------IGLVTMLAARAFSVPRivivdvDENRLAVAKQ----LGADEIVQVTTNLEDVGSEVeqIQKA 250
Cdd:cd08290 146 PGDWVIQNGANSavgqavIQLAKLLGIKTINVVR------DRPDLEELKErlkaLGADHVLTEEELRSLLATEL--LKSA 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 251 MGSNIDVTFDCAG--FNKTMSTALAAtrcGGkvCLV---GMGHGIMTVPLTPAAAREVDVVGVFRYKNT-------WPLC 318
Cdd:cd08290 218 PGGRPKLALNCVGgkSATELARLLSP---GG--TMVtygGMSGQPVTVPTSLLIFKDITLRGFWLTRWLkranpeeKEDM 292
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 15242240 319 LEFL----TSGKIdVKPLITHRFGFSQKEVEDAFETSARGSNAIKVMF 362
Cdd:cd08290 293 LEELaeliREGKL-KAPPVEKVTDDPLEEFKDALANALKGGGGGKQVL 339
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
74-285 4.51e-05

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


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 44.98  E-value: 4.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  74 PMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGIscwrcnlcREGRYNLCPEMKFFATpPVHGSLANQVVHPADLCFKLP 153
Cdd:cd08274  78 PRIQGADIVGRVVAVGEGVDTARIGERVLVDPSI--------RDPPEDDPADIDYIGS-ERDGGFAEYTVVPAENAYPVN 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 154 ENVSLEE-GAMCEPLSVGVHACRRAEVGPETNVLVMGA-GPIGLVTM-LAARAFSvprIVIVDVDENRLAVAKQLGADEI 230
Cdd:cd08274 149 SPLSDVElATFPCSYSTAENMLERAGVGAGETVLVTGAsGGVGSALVqLAKRRGA---IVIAVAGAAKEEAVRALGADTV 225
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15242240 231 VQVTTNLedvgseVEQIQKAMGSNIDVTFDCAGfNKTMSTALAATRCGGKVCLVG 285
Cdd:cd08274 226 ILRDAPL------LADAKALGGEPVDVVADVVG-GPLFPDLLRLLRPGGRYVTAG 273
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
74-286 6.55e-05

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


Pssm-ID: 176183 [Multi-domain]  Cd Length: 325  Bit Score: 44.45  E-value: 6.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240  74 PMVIGHECAGIIEEVGeeVKHLVVGDRVAL---EPGISCWrcnlcregrynlcpemkffatppvhGSLANQVVHPADLCF 150
Cdd:cd05280  58 PHTPGIDAAGTVVSSD--DPRFREGDEVLVtgyDLGMNTD-------------------------GGFAEYVRVPADWVV 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 151 KLPENVSLEEgAMCeplsVG---------VHACRRAEVGPE-TNVLVMGA-GPIGL--VTMLAARAFSVpriVIVDVDEN 217
Cdd:cd05280 111 PLPEGLSLRE-AMI----LGtagftaalsVHRLEDNGQTPEdGPVLVTGAtGGVGSiaVAILAKLGYTV---VALTGKEE 182
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 218 RLAVAKQLGADEIVqvttNLEDVGSEVEqiqKAMGSNI-DVTFDCAGfNKTMSTALAATRCGGKVCLVGM 286
Cdd:cd05280 183 QADYLKSLGASEVL----DREDLLDESK---KPLLKARwAGAIDTVG-GDVLANLLKQTKYGGVVASCGN 244
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
145-308 9.39e-04

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


Pssm-ID: 176249 [Multi-domain]  Cd Length: 326  Bit Score: 40.77  E-value: 9.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 145 PADLCFKLPENVSLEEgAM-------CEPLSVgvHACRRAEVGPETN-VLVMGA-GPIG--LVTMLAARAFSVPRIVIVD 213
Cdd:cd08289 105 PAEWVVPLPKGLTLKE-AMilgtagfTAALSI--HRLEENGLTPEQGpVLVTGAtGGVGslAVSILAKLGYEVVASTGKA 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242240 214 VDENRLavaKQLGADEIVqvtTNLEDVGSEVEQIQKAMGSNIdvtFDCAGfNKTMSTALAATRCGGKVCLVGMGHGImTV 293
Cdd:cd08289 182 DAADYL---KKLGAKEVI---PREELQEESIKPLEKQRWAGA---VDPVG-GKTLAYLLSTLQYGGSVAVSGLTGGG-EV 250
                       170
                ....*....|....*..
gi 15242240 294 PLT--PAAAREVDVVGV 308
Cdd:cd08289 251 ETTvfPFILRGVNLLGI 267
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
185-246 2.31e-03

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 37.57  E-value: 2.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15242240   185 VLVMGAGPIGLVTM-LAARAFSVPRIVIVDVDENRL-AVAKQLGADEIVQVTTNLEDVGSEVEQ 246
Cdd:pfam03435   1 VLIIGAGSVGQGVApLLARHFDVDRITVADRTLEKAqALAAKLGGVRFIAVAVDADNYEAVLAA 64
 
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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