NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19111912|ref|NP_595120|]
View 

hexitol dehydrogenase [Schizosaccharomyces pombe]

Protein Classification

NAD(P)-dependent alcohol dehydrogenase( domain architecture ID 10143035)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 7-355 1.17e-164

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: 463.50  E-value: 1.17e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   7 AFVLRKKMDTAIEDRPGQTLTDdHQVKVAIKATGICGSDVHYWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPG 86
Cdd:cd05285   1 AAVLHGPGDLRLEERPIPEPGP-GEVLVRVRAVGICGSDVHYYKHGRIGDFVVKEPMVLGHESAGTVVAVGSGVTHLKVG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  87 DPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATPPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRGN 166
Cdd:cd05285  80 DRVAIEPGVPCRTCEFCKSGRYNLCPDMRFAATPPVDGTLCRYVNHPADFCHKLPDNVSLEEGALVEPLSVGVHACRRAG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 167 LKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYVGAKPFTPiaakENESLPDYAQRYKQAIIEKyg 246
Cdd:cd05285 160 VRPGDTVLVFGAGPIGLLTAAVAKAFGATKVVVTDIDPSRLEFAKELGATHTVNV----RTEDTPESAEKIAELLGGK-- 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 247 EFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAHgCYKQSLFLVSNGLVDVKPL 326
Cdd:cd05285 234 GPDVVIECTGAESCIQTAIYATRPGGTVVLVGMGKPEVTLPLSAASLREIDIRGVFRYAN-TYPTAIELLASGKVDVKPL 312

                       330       340
                ....*....|....*....|....*....
gi 19111912 327 ITHRFAFKDALKAYETVASGEEGVLKVII 355
Cdd:cd05285 313 ITHRFPLEDAVEAFETAAKGKKGVIKVVI 341
 
Name Accession Description Interval E-value
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 7-355 1.17e-164

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: 463.50  E-value: 1.17e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   7 AFVLRKKMDTAIEDRPGQTLTDdHQVKVAIKATGICGSDVHYWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPG 86
Cdd:cd05285   1 AAVLHGPGDLRLEERPIPEPGP-GEVLVRVRAVGICGSDVHYYKHGRIGDFVVKEPMVLGHESAGTVVAVGSGVTHLKVG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  87 DPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATPPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRGN 166
Cdd:cd05285  80 DRVAIEPGVPCRTCEFCKSGRYNLCPDMRFAATPPVDGTLCRYVNHPADFCHKLPDNVSLEEGALVEPLSVGVHACRRAG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 167 LKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYVGAKPFTPiaakENESLPDYAQRYKQAIIEKyg 246
Cdd:cd05285 160 VRPGDTVLVFGAGPIGLLTAAVAKAFGATKVVVTDIDPSRLEFAKELGATHTVNV----RTEDTPESAEKIAELLGGK-- 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 247 EFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAHgCYKQSLFLVSNGLVDVKPL 326
Cdd:cd05285 234 GPDVVIECTGAESCIQTAIYATRPGGTVVLVGMGKPEVTLPLSAASLREIDIRGVFRYAN-TYPTAIELLASGKVDVKPL 312

                       330       340
                ....*....|....*....|....*....
gi 19111912 327 ITHRFAFKDALKAYETVASGEEGVLKVII 355
Cdd:cd05285 313 ITHRFPLEDAVEAFETAAKGKKGVIKVVI 341
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 6-355 7.81e-100

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: 298.59  E-value: 7.81e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLtDDHQVKVAIKATGICGSDVHYWKEGgigDFILKKPMILGHESAGVVVEVGKGVSSLKP 85
Cdd:COG1063   2 KALVLHGPGDLRLEEVPDPEP-GPGEVLVRVTAVGICGSDLHIYRGG---YPFVRPPLVLGHEFVGEVVEVGEGVTGLKV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  86 GDPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATPPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRG 165
Cdd:COG1063  78 GDRVVVEPNIPCGECRYCRRGRYNLCENLQFLGIAGRDGGFAEYVRVPAANLVKVPDGLSDEAAALVEPLAVALHAVERA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 166 NLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYvGAKpfTPIAAKEnESLPDYAqrykQAIIEKY 245
Cdd:COG1063 158 GVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELAREL-GAD--AVVNPRE-EDLVEAV----RELTGGR 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 246 GeFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAHGCYKQSLFLVSNGLVDVKP 325
Cdd:COG1063 230 G-ADVVIEAVGAPAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDLEP 308

                       330       340       350
                ....*....|....*....|....*....|
gi 19111912 326 LITHRFAFKDALKAYETVASGEEGVLKVII 355
Cdd:COG1063 309 LITHRFPLDDAPEAFEAAADRADGAIKVVL 338
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 29-346 1.85e-88

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 270.50  E-value: 1.85e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   29 DHQVKVAIKATGICGSDVHYWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRY 108
Cdd:PLN02702  41 PHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGSEVKHLVVGDRVALEPGISCWRCNLCKEGRY 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  109 NLCPHMEFAATPPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAV 188
Cdd:PLN02702 121 NLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRANIGPETNVLVMGAGPIGLVTMLA 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  189 AKAYGAIDIVAVDASPSRVEFAqKYVGAKPFTPIAAKENEsLPDYAQRYKQAIIekyGEFDFAVDATGVGICIHTAVLAL 268
Cdd:PLN02702 201 ARAFGAPRIVIVDVDDERLSVA-KQLGADEIVLVSTNIED-VESEVEEIQKAMG---GGIDVSFDCVGFNKTMSTALEAT 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  269 KRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAHgCYKQSLFLVSNGLVDVKPLITHRFAF--KDALKAYETVASG 346
Cdd:PLN02702 276 RAGGKVCLVGMGHNEMTVPLTPAAAREVDVVGVFRYRN-TWPLCLEFLRSGKIDVKPLITHRFGFsqKEVEEAFETSARG 354
tdh TIGR00692
L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme ...
 28-355 7.64e-38

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: 138.45  E-value: 7.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912    28 DDHQVKVAIKATGICGSDVHYWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGR 107
Cdd:TIGR00692  22 GPGEVLIKVLATSICGTDVHIYNWDEWAQSRIKPPQVVGHEVAGEVVGIGPGVEGIKVGDYVSVETHIVCGKCYACRRGQ 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   108 YNLCPHMEFAATPPyDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRGNLkCGSRVLVMGCGTVGLLMMA 187
Cdd:TIGR00692 102 YHVCQNTKIFGVDT-DGCFAEYAVVPAQNIWKNPKSIPPEYATIQEPLGNAVHTVLAGPI-SGKSVLVTGAGPIGLMAIA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   188 VAKAYGAIDIVAVDASPSRVEFAQKyVGAkpfTPIAAKENESLPDYAqrykQAIIEKYGeFDFAVDATGVGICIHTAVLA 267
Cdd:TIGR00692 180 VAKASGAYPVIVSDPNEYRLELAKK-MGA---TYVVNPFKEDVVKEV----ADLTDGEG-VDVFLEMSGAPKALEQGLQA 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   268 LKRGGTFVQAG--NGKPVIDFpINHIINYEINVLGSF-RYAHGCYKQSLFLVSNGLVDVKPLITHRFAFKDALKAYETVA 344
Cdd:TIGR00692 251 VTPGGRVSLLGlpPGKVTIDF-TNKVIFKGLTIYGITgRHMFETWYTVSRLIQSGKLDLDPIITHKFKFDKFEKGFELMR 329

                         330
                  ....*....|.
gi 19111912   345 SGEEGvlKVII 355
Cdd:TIGR00692 330 SGQTG--KVIL 338
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 30-139 2.76e-28

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: 106.15  E-value: 2.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912    30 HQVKVAIKATGICGSDVHYWKEGgigDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRYN 109
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGG---NPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYN 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 19111912   110 LCPHMEFAATpPYDGTLRTYYITTEDFCTK 139
Cdd:pfam08240  78 LCPNGRFLGY-DRDGGFAEYVVVPERNLVP 106
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 124-213 4.35e-04

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 41.60  E-value: 4.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912    124 GTLRTYYITTEDFCTKLPKQISVEEGAlfepmSV------AVHAM-TRGNLKCGSRVLV-MGCGTVGLLMMAVAKAYGAi 195
Cdd:smart00829  56 GAFATRVVTDARLVVPIPDGWSFEEAA-----TVpvvfltAYYALvDLARLRPGESVLIhAAAGGVGQAAIQLARHLGA- 129

                           90
                   ....*....|....*...
gi 19111912    196 DIVAVDASPSRVEFAQKY 213
Cdd:smart00829 130 EVFATAGSPEKRDFLRAL 147
 
Name Accession Description Interval E-value
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 7-355 1.17e-164

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: 463.50  E-value: 1.17e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   7 AFVLRKKMDTAIEDRPGQTLTDdHQVKVAIKATGICGSDVHYWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPG 86
Cdd:cd05285   1 AAVLHGPGDLRLEERPIPEPGP-GEVLVRVRAVGICGSDVHYYKHGRIGDFVVKEPMVLGHESAGTVVAVGSGVTHLKVG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  87 DPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATPPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRGN 166
Cdd:cd05285  80 DRVAIEPGVPCRTCEFCKSGRYNLCPDMRFAATPPVDGTLCRYVNHPADFCHKLPDNVSLEEGALVEPLSVGVHACRRAG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 167 LKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYVGAKPFTPiaakENESLPDYAQRYKQAIIEKyg 246
Cdd:cd05285 160 VRPGDTVLVFGAGPIGLLTAAVAKAFGATKVVVTDIDPSRLEFAKELGATHTVNV----RTEDTPESAEKIAELLGGK-- 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 247 EFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAHgCYKQSLFLVSNGLVDVKPL 326
Cdd:cd05285 234 GPDVVIECTGAESCIQTAIYATRPGGTVVLVGMGKPEVTLPLSAASLREIDIRGVFRYAN-TYPTAIELLASGKVDVKPL 312

                       330       340
                ....*....|....*....|....*....
gi 19111912 327 ITHRFAFKDALKAYETVASGEEGVLKVII 355
Cdd:cd05285 313 ITHRFPLEDAVEAFETAAKGKKGVIKVVI 341
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 6-355 7.81e-100

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: 298.59  E-value: 7.81e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLtDDHQVKVAIKATGICGSDVHYWKEGgigDFILKKPMILGHESAGVVVEVGKGVSSLKP 85
Cdd:COG1063   2 KALVLHGPGDLRLEEVPDPEP-GPGEVLVRVTAVGICGSDLHIYRGG---YPFVRPPLVLGHEFVGEVVEVGEGVTGLKV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  86 GDPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATPPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRG 165
Cdd:COG1063  78 GDRVVVEPNIPCGECRYCRRGRYNLCENLQFLGIAGRDGGFAEYVRVPAANLVKVPDGLSDEAAALVEPLAVALHAVERA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 166 NLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYvGAKpfTPIAAKEnESLPDYAqrykQAIIEKY 245
Cdd:COG1063 158 GVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELAREL-GAD--AVVNPRE-EDLVEAV----RELTGGR 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 246 GeFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAHGCYKQSLFLVSNGLVDVKP 325
Cdd:COG1063 230 G-ADVVIEAVGAPAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDLEP 308

                       330       340       350
                ....*....|....*....|....*....|
gi 19111912 326 LITHRFAFKDALKAYETVASGEEGVLKVII 355
Cdd:COG1063 309 LITHRFPLDDAPEAFEAAADRADGAIKVVL 338
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 29-346 1.85e-88

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 270.50  E-value: 1.85e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   29 DHQVKVAIKATGICGSDVHYWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRY 108
Cdd:PLN02702  41 PHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGSEVKHLVVGDRVALEPGISCWRCNLCKEGRY 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  109 NLCPHMEFAATPPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAV 188
Cdd:PLN02702 121 NLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRANIGPETNVLVMGAGPIGLVTMLA 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  189 AKAYGAIDIVAVDASPSRVEFAqKYVGAKPFTPIAAKENEsLPDYAQRYKQAIIekyGEFDFAVDATGVGICIHTAVLAL 268
Cdd:PLN02702 201 ARAFGAPRIVIVDVDDERLSVA-KQLGADEIVLVSTNIED-VESEVEEIQKAMG---GGIDVSFDCVGFNKTMSTALEAT 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  269 KRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAHgCYKQSLFLVSNGLVDVKPLITHRFAF--KDALKAYETVASG 346
Cdd:PLN02702 276 RAGGKVCLVGMGHNEMTVPLTPAAAREVDVVGVFRYRN-TWPLCLEFLRSGKIDVKPLITHRFGFsqKEVEEAFETSARG 354
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 9-344 4.48e-86

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: 263.71  E-value: 4.48e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   9 VLRKKMDTAIEDRPGQTLTDdHQVKVAIKATGICGSDVHYWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDP 88
Cdd:cd08232   2 VIHAAGDLRVEERPAPEPGP-GEVRVRVAAGGICGSDLHYYQHGGFGTVRLREPMVLGHEVSGVVEAVGPGVTGLAPGQR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  89 VAVEPGCVCRLCDYCRSGRYNLCPHMEF---AATPPY-DGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTR 164
Cdd:cd08232  81 VAVNPSRPCGTCDYCRAGRPNLCLNMRFlgsAMRFPHvQGGFREYLVVDASQCVPLPDGLSLRRAALAEPLAVALHAVNR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 165 GNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKyVGAKPFTPIAakeneslPDYAQRYKQAIiek 244
Cdd:cd08232 161 AGDLAGKRVLVTGAGPIGALVVAAARRAGAAEIVATDLADAPLAVARA-MGADETVNLA-------RDPLAAYAADK--- 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 245 yGEFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYaHGCYKQSLFLVSNGLVDVK 324
Cdd:cd08232 230 -GDFDVVFEASGAPAALASALRVVRPGGTVVQVGMLGGPVPLPLNALVAKELDLRGSFRF-DDEFAEAVRLLAAGRIDVR 307

                       330       340
                ....*....|....*....|
gi 19111912 325 PLITHRFAFKDALKAYETVA 344
Cdd:cd08232 308 PLITAVFPLEEAAEAFALAA 327
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 6-355 9.33e-71

(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: 224.73  E-value: 9.33e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLTDdHQVKVAIKATGICGSDVHYWKEGGIgdFI----------LKKPMILGHESAGVVVE 75
Cdd:cd08233   2 KAARYHGRKDIRVEEVPEPPVKP-GEVKIKVAWCGICGSDLHEYLDGPI--FIpteghphltgETAPVTLGHEFSGVVVE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  76 VGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATPPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPM 155
Cdd:cd08233  79 VGSGVTGFKVGDRVVVEPTIKCGTCGACKRGLYNLCDSLGFIGLGGGGGGFAEYVVVPAYHVHKLPDNVPLEEAALVEPL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 156 SVAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYVGAKPFTPIAAKENESLPDYAQ 235
Cdd:cd08233 159 AVAWHAVRRSGFKPGDTALVLGAGPIGLLTILALKAAGASKIIVSEPSEARRELAEELGATIVLDPTEVDVVAEVRKLTG 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 236 RykqaiiekyGEFDFAVDATGVGICIHTAVLALKRGGTFVQ-AGNGKPvIDFPINHIINYEINVLGSFRYAHGCYKQSLF 314
Cdd:cd08233 239 G---------GGVDVSFDCAGVQATLDTAIDALRPRGTAVNvAIWEKP-ISFNPNDLVLKEKTLTGSICYTREDFEEVID 308

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 19111912 315 LVSNGLVDVKPLITHRFAFKDAL-KAYETVASGEEGVLKVII 355
Cdd:cd08233 309 LLASGKIDAEPLITSRIPLEDIVeKGFEELINDKEQHVKILV 350
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 6-355 5.40e-67

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: 214.31  E-value: 5.40e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLTDDHqVKVAIKATGICGSDVHYWKeggiGDFILKKPMILGHESAGVVVEVGKGVSSLKP 85
Cdd:cd08234   2 KALVYEGPGELEVEEVPVPEPGPDE-VLIKVAACGICGTDLHIYE----GEFGAAPPLVPGHEFAGVVVAVGSKVTGFKV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  86 GDPVAVEPGCVCRLCDYCRSGRYNLCPHME---------FA--ATPPydgtlrtyyittEDFCTKLPKQISVEEGALFEP 154
Cdd:cd08234  77 GDRVAVDPNIYCGECFYCRRGRPNLCENLTavgvtrnggFAeyVVVP------------AKQVYKIPDNLSFEEAALAEP 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 155 MSVAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYVGAKPFTPIAAKENEslpdya 234
Cdd:cd08234 145 LSCAVHGLDLLGIKPGDSVLVFGAGPIGLLLAQLLKLNGASRVTVAEPNEEKLELAKKLGATETVDPSREDPEA------ 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 235 qrykQAIIEKYGeFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKP--VIDFPINHIINYEINVLGSFRYAHgCYKQS 312
Cdd:cd08234 219 ----QKEDNPYG-FDVVIEATGVPKTLEQAIEYARRGGTVLVFGVYAPdaRVSISPFEIFQKELTIIGSFINPY-TFPRA 292

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 19111912 313 LFLVSNGLVDVKPLITHRFAFKDALKAYETVASGeeGVLKVII 355
Cdd:cd08234 293 IALLESGKIDVKGLVSHRLPLEEVPEALEGMRSG--GALKVVV 333
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 6-355 2.85e-65

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: 210.16  E-value: 2.85e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLTDDhQVKVAIKATGICGSDVHYWKEGGIgdfiLKKPMILGHESAGVVVEVGKGVSSLKP 85
Cdd:cd08236   2 KALVLTGPGDLRYEDIPKPEPGPG-EVLVKVKACGICGSDIPRYLGTGA----YHPPLVLGHEFSGTVEEVGSGVDDLAV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  86 GDPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATPpYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRG 165
Cdd:cd08236  77 GDRVAVNPLLPCGKCEYCKKGEYSLCSNYDYIGSR-RDGAFAEYVSVPARNLIKIPDHVDYEEAAMIEPAAVALHAVRLA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 166 NLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYVGAKPFTPiaAKENESLPdyaqrykQAIIEKY 245
Cdd:cd08236 156 GITLGDTVVVIGAGTIGLLAIQWLKILGAKRVIAVDIDDEKLAVARELGADDTINP--KEEDVEKV-------RELTEGR 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 246 GeFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKP---VIDFPINHIINYEINVLGSFRY-----AHGCYKQSLFLVS 317
Cdd:cd08236 227 G-ADLVIEAAGSPATIEQALALARPGGKVVLVGIPYGdvtLSEEAFEKILRKELTIQGSWNSysapfPGDEWRTALDLLA 305

                       330       340       350
                ....*....|....*....|....*....|....*...
gi 19111912 318 NGLVDVKPLITHRFAFKDALKAYETVASGEEGVLKVII 355
Cdd:cd08236 306 SGKIKVEPLITHRLPLEDGPAAFERLADREEFSGKVLL 343
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 6-355 2.00e-62

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: 202.83  E-value: 2.00e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLTDDhQVKVAIKATGICGSDVHYWKEGGigdFILKKPMILGHESAGVVVEVGKGVSSLKP 85
Cdd:cd08235   2 KAAVLHGPNDVRLEEVPVPEPGPG-EVLVKVRACGICGTDVKKIRGGH---TDLKPPRILGHEIAGEIVEVGDGVTGFKV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  86 GDPVAVEPGCVCRLCDYCRSGRYNLCPHMEfAATPPYDGTLRTYY-----ITTEDFCTKLPKQISVEEGALFEPMSVAVH 160
Cdd:cd08235  78 GDRVFVAPHVPCGECHYCLRGNENMCPNYK-KFGNLYDGGFAEYVrvpawAVKRGGVLKLPDNVSFEEAALVEPLACCIN 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 161 AMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKyVGAKpfTPIAAKEneslPDYAQRYKqA 240
Cdd:cd08235 157 AQRKAGIKPGDTVLVIGAGPIGLLHAMLAKASGARKVIVSDLNEFRLEFAKK-LGAD--YTIDAAE----EDLVEKVR-E 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 241 IIEKYGeFDFAVDATGVGICIHTAVLALKRGGTF----VQAGNGKPVIDFpiNHIINYEINVLGSFRYAHGCYKQSLFLV 316
Cdd:cd08235 229 LTDGRG-ADVVIVATGSPEAQAQALELVRKGGRIlffgGLPKGSTVNIDP--NLIHYREITITGSYAASPEDYKEALELI 305

                       330       340       350
                ....*....|....*....|....*....|....*....
gi 19111912 317 SNGLVDVKPLITHRFAFKDALKAYETVASGEEgvLKVII 355
Cdd:cd08235 306 ASGKIDVKDLITHRFPLEDIEEAFELAADGKS--LKIVI 342
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 6-347 1.05e-60

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 198.03  E-value: 1.05e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRK-KMDTAIEDRPGQTLtDDHQVKVAIKATGICGSDVHYWkEGGIGDFILkkPMILGHESAGVVVEVGKGVSSLK 84
Cdd:COG1064   2 KAAVLTEpGGPLELEEVPRPEP-GPGEVLVKVEACGVCHSDLHVA-EGEWPVPKL--PLVPGHEIVGRVVAVGPGVTGFK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  85 PGDPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATpPYDGTLRTYYITTEDFCTKLPKQISVEEGA-LFEPMSVAVHAMT 163
Cdd:COG1064  78 VGDRVGVGWVDSCGTCEYCRSGRENLCENGRFTGY-TTDGGYAEYVVVPARFLVKLPDGLDPAEAApLLCAGITAYRALR 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 164 RGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAiDIVAVDASPSRVEFAQKYvGAKPFtpIAAKEneslPDYAQRykqaiIE 243
Cdd:COG1064 157 RAGVGPGDRVAVIGAGGLGHLAVQIAKALGA-EVIAVDRSPEKLELAREL-GADHV--VNSSD----EDPVEA-----VR 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 244 KYGEFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAHGCYKQSLFLVSNGLVDV 323
Cdd:COG1064 224 ELTGADVVIDTVGAPATVNAALALLRRGGRLVLVGLPGGPIPLPPFDLILKERSIRGSLIGTRADLQEMLDLAAEGKIKP 303

                       330       340
                ....*....|....*....|....
gi 19111912 324 kplITHRFAFKDALKAYETVASGE 347
Cdd:COG1064 304 ---EVETIPLEEANEALERLRAGK 324
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 9-355 2.45e-60

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 197.60  E-value: 2.45e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912    9 VLRKKMDTAIEDRpgQTLTDDHQVKVAIKATGICGSDVHYWKEGGIGDFILKKPMILGHEsaGVVVEVGKGVSSLKPGDP 88
Cdd:PRK09880   9 VVAGKKDVAVTEQ--EIEWNNNGTLVQITRGGICGSDLHYYQEGKVGNFVIKAPMVLGHE--VIGKIVHSDSSGLKEGQT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   89 VAVEPGCVCRLCDYCRSGRYNLCPHMEFAA----TPPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTR 164
Cdd:PRK09880  85 VAINPSKPCGHCKYCLSHNENQCTTMRFFGsamyFPHVDGGFTRYKVVDTAQCIPYPEKADEKVMAFAEPLAVAIHAAHQ 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  165 -GNLKcGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKyVGAkpfTPIAAKENESLPDYAQrykqaiiE 243
Cdd:PRK09880 165 aGDLQ-GKRVFVSGVGPIGCLIVAAVKTLGAAEIVCADVSPRSLSLARE-MGA---DKLVNPQNDDLDHYKA-------E 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  244 KyGEFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAhGCYKQSLFLVSNGLVDV 323
Cdd:PRK09880 233 K-GYFDVSFEVSGHPSSINTCLEVTRAKGVMVQVGMGGAPPEFPMMTLIVKEISLKGSFRFT-EEFNTAVSWLANGVINP 310

                        330       340       350
                 ....*....|....*....|....*....|..
gi 19111912  324 KPLITHRFAFKDALKAYETvASGEEGVLKVII 355
Cdd:PRK09880 311 LPLLSAEYPFTDLEEALIF-AGDKTQAAKVQL 341
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 31-313 4.83e-57

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: 186.76  E-value: 4.83e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  31 QVKVAIKATGICGSDVHYWKEGGIGDfiLKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSgrynl 110
Cdd:cd05188   1 EVLVRVEAAGLCGTDLHIRRGGYPPP--PKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNLGCGTCELCRE----- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 111 CPHMEFAATPPYDGTLRTYYITTEDFCTKLPKQISVEEGALF-EPMSVAVHAM-TRGNLKCGSRVLVMGCGTVGLLMMAV 188
Cdd:cd05188  74 LCPGGGILGEGLDGGFAEYVVVPADNLVPLPDGLSLEEAALLpEPLATAYHALrRAGVLKPGDTVLVLGAGGVGLLAAQL 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 189 AKAYGAiDIVAVDASPSRVEFAQKYVGAKPFtpiaakeNESLPDYAQRykqAIIEKYGEFDFAVDATGVGICIHTAVLAL 268
Cdd:cd05188 154 AKAAGA-RVIVTDRSDEKLELAKELGADHVI-------DYKEEDLEEE---LRLTGGGGADVVIDAVGGPETLAQALRLL 222

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 19111912 269 KRGGTFVQAGN-GKPVIDFPINHIINYEINVLGSFRYAHGCYKQSL 313
Cdd:cd05188 223 RPGGRIVVVGGtSGGPPLDDLRRLLFKELTIIGSTGGTREDFEEAL 268
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 6-355 2.68e-56

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: 187.01  E-value: 2.68e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLTDDhQVKVAIKATGICGSDVHYWkeGGIGDFiLKKPMILGHESAGVVVEVGKGVSSLKP 85
Cdd:cd08261   2 KALVCEKPGRLEVVDIPEPVPGAG-EVLVRVKRVGICGSDLHIY--HGRNPF-ASYPRILGHELSGEVVEVGEGVAGLKV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  86 GDPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATPPyDGTLRTYYITTEDfCTKLPKQISVEEGALFEPMSVAVHAMTRG 165
Cdd:cd08261  78 GDRVVVDPYISCGECYACRKGRPNCCENLQVLGVHR-DGGFAEYIVVPAD-ALLVPEGLSLDQAALVEPLAIGAHAVRRA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 166 NLKCGSRVLVMGCGTVGLLMMAVAKAYGAiDIVAVDASPSRVEFAQKYVGAKPFTPIAAKENESLPDYAQrykqaiieky 245
Cdd:cd08261 156 GVTAGDTVLVVGAGPIGLGVIQVAKARGA-RVIVVDIDDERLEFARELGADDTINVGDEDVAARLRELTD---------- 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 246 GE-FDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAHGCYKQSLFLVSNGLVDVK 324
Cdd:cd08261 225 GEgADVVIDATGNPASMEEAVELVAHGGRVVLVGLSKGPVTFPDPEFHKKELTILGSRNATREDFPDVIDLLESGKVDPE 304

                       330       340       350
                ....*....|....*....|....*....|.
gi 19111912 325 PLITHRFAFKDALKAYETVASGEEGVLKVII 355
Cdd:cd08261 305 ALITHRFPFEDVPEAFDLWEAPPGGVIKVLI 335
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 31-347 4.18e-49

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: 168.19  E-value: 4.18e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  31 QVKVAIKATGICGSDVHYWKEGGIgdFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRYNL 110
Cdd:cd08254  28 EVLVKVKAAGVCHSDLHILDGGVP--TLTKLPLTLGHEIAGTVVEVGAGVTNFKVGDRVAVPAVIPCGACALCRRGRGNL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 111 CPHMEFAATpPYDGTLRTYYITTEDFCTKLPKQISVEEGALfepMSVAV----HAM-TRGNLKCGSRVLVMGCGTVGLLM 185
Cdd:cd08254 106 CLNQGMPGL-GIDGGFAEYIVVPARALVPVPDGVPFAQAAV---ATDAVltpyHAVvRAGEVKPGETVLVIGLGGLGLNA 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 186 MAVAKAYGAiDIVAVDASPSRVEFAQKYvGAKPFTpiaakenESLPDYAQRYKQAiiEKYGEFDFAVDATGVGICIHTAV 265
Cdd:cd08254 182 VQIAKAMGA-AVIAVDIKEEKLELAKEL-GADEVL-------NSLDDSPKDKKAA--GLGGGFDVIFDFVGTQPTFEDAQ 250

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 266 LALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAHGCYKQSLFLVSNGLVDvkpLITHRFAFKDALKAYETVAS 345
Cdd:cd08254 251 KAVKPGGRIVVVGLGRDKLTVDLSDLIARELRIIGSFGGTPEDLPEVLDLIAKGKLD---PQVETRPLDEIPEVLERLHK 327


                ..
gi 19111912 346 GE 347
Cdd:cd08254 328 GK 329
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 22-355 8.36e-45

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: 157.01  E-value: 8.36e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  22 PGQTLTD-------DHQVKVAIKATGICGSDVH-----YWKEGGIgdfilKKPMILGHESAGVVVEVGKGVSSLKPGDPV 89
Cdd:cd05281  11 PGAELVEvpvpkpgPGEVLIKVLAASICGTDVHiyewdEWAQSRI-----KPPLIFGHEFAGEVVEVGEGVTRVKVGDYV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  90 AVEPGCVCRLCDYCRSGRYNLCPHMEFAATpPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRGNLKc 169
Cdd:cd05281  86 SAETHIVCGKCYQCRTGNYHVCQNTKILGV-DTDGCFAEYVVVPEENLWKNDKDIPPEIASIQEPLGNAVHTVLAGDVS- 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 170 GSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKyVGAkpfTPIAAKENESLPDyaqryKQAIIEKYGeFD 249
Cdd:cd05281 164 GKSVLITGCGPIGLMAIAVAKAAGASLVIASDPNPYRLELAKK-MGA---DVVINPREEDVVE-----VKSVTDGTG-VD 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 250 FAVDATGVGICIHTAVLALKRGGTFVQAG-NGKPV-IDFPiNHIINYEINVLG-SFRYAHGCYKQSLFLVSNGLVDVKPL 326
Cdd:cd05281 234 VVLEMSGNPKAIEQGLKALTPGGRVSILGlPPGPVdIDLN-NLVIFKGLTVQGiTGRKMFETWYQVSALLKSGKVDLSPV 312

                       330       340
                ....*....|....*....|....*....
gi 19111912 327 ITHRFAFKDALKAYETVASGEEGvlKVII 355
Cdd:cd05281 313 ITHKLPLEDFEEAFELMRSGKCG--KVVL 339
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 29-319 2.93e-44

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: 154.40  E-value: 2.93e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  29 DHQVKVAIKATGICGSDVHYWKegGIGDFIlKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEP-GCVCRLCDYCRSGR 107
Cdd:cd08258  26 PGEVLIKVAAAGICGSDLHIYK--GDYDPV-ETPVVLGHEFSGTIVEVGPDVEGWKVGDRVVSETtFSTCGRCPYCRRGD 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 108 YNLCPHMEFAATpPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAM-TRGNLKCGSRVLVMGCGTVGLLMM 186
Cdd:cd08258 103 YNLCPHRKGIGT-QADGGFAEYVLVPEESLHELPENLSLEAAALTEPLAVAVHAVaERSGIRPGDTVVVFGPGPIGLLAA 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 187 AVAKAYGA-IDIVAVDASPSRVEFAQKyVGakpftpiAAKENESLPDYAQRYKQaIIEKYGeFDFAVDATGVGICIHTAV 265
Cdd:cd08258 182 QVAKLQGAtVVVVGTEKDEVRLDVAKE-LG-------ADAVNGGEEDLAELVNE-ITDGDG-ADVVIECSGAVPALEQAL 251

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19111912 266 LALKRGGTFVQAGNGKPV---IDFPInhIINYEINVLGSFRYAHGCYKQSLFLVSNG 319
Cdd:cd08258 252 ELLRKGGRIVQVGIFGPLaasIDVER--IIQKELSVIGSRSSTPASWETALRLLASG 306
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 6-355 4.33e-43

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: 152.43  E-value: 4.33e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLTDDHQVKVAIKATGICGSDVHYWKEGGIGDfilKKPMILGHESAGVVVEVGKGVSSLKP 85
Cdd:cd05278   2 KALVYLGPGKIGLEEVPDPKIQGPHDAIVRVTATSICGSDLHIYRGGVPGA---KHGMILGHEFVGEVVEVGSDVKRLKP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  86 GDPVAVepGCV--CRLCDYCRSGRYNLCPHMEFAATPPY--DGTLRTYYITTE-DF-CTKLPKQISvEEGALFEP--MSV 157
Cdd:cd05278  79 GDRVSV--PCItfCGRCRFCRRGYHAHCENGLWGWKLGNriDGGQAEYVRVPYaDMnLAKIPDGLP-DEDALMLSdiLPT 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 158 AVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYVGAKPFTPiaakENESLPDYAqry 237
Cdd:cd05278 156 GFHGAELAGIKPGSTVAVIGAGPVGLCAVAGARLLGAARIIAVDSNPERLDLAKEAGATDIINP----KNGDIVEQI--- 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 238 kQAIIEKYGeFDFAVDATGVGICIHTAVLALKRGGTFVQAG-NGKPVIDFPI------NHIInyeinvlgSFRYAHG-CY 309
Cdd:cd05278 229 -LELTGGRG-VDCVIEAVGFEETFEQAVKVVRPGGTIANVGvYGKPDPLPLLgewfgkNLTF--------KTGLVPVrAR 298

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 19111912 310 KQSLF-LVSNGLVDVKPLITHRFAFKDALKAYETVASGEEGVLKVII 355
Cdd:cd05278 299 MPELLdLIEEGKIDPSKLITHRFPLDDILKAYRLFDNKPDGCIKVVI 345
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 31-356 1.94e-41

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: 147.85  E-value: 1.94e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  31 QVKVAIKATGICGSDVHYWKEGGIGdfILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRYNL 110
Cdd:cd08239  26 EVLLRVKASGLCGSDLHYYYHGHRA--PAYQGVIPGHEPAGVVVAVGPGVTHFRVGDRVMVYHYVGCGACRNCRRGWMQL 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 111 CPHMEFAATPPYDGTLRTYYITTEDFCTKLPKQISVEEGALF-EPMSVAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVA 189
Cdd:cd08239 104 CTSKRAAYGWNRDGGHAEYMLVPEKTLIPLPDDLSFADGALLlCGIGTAYHALRRVGVSGRDTVLVVGAGPVGLGALMLA 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 190 KAYGAIDIVAVDASPSRVEFAQKYvGAkpfTPIAAKENESLpdyaqrykQAIIEKYGE--FDFAVDATGVGICIHTAVLA 267
Cdd:cd08239 184 RALGAEDVIGVDPSPERLELAKAL-GA---DFVINSGQDDV--------QEIRELTSGagADVAIECSGNTAARRLALEA 251

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 268 LKRGGTFVQAG-NGKPVIDfPINHIINYEINVLGSFRYAHGCYKQSLFLVSNGLVDVKPLITHRFAFKDALKAYETVASG 346
Cdd:cd08239 252 VRPWGRLVLVGeGGELTIE-VSNDLIRKQRTLIGSWYFSVPDMEECAEFLARHKLEVDRLVTHRFGLDQAPEAYALFAQG 330

                       330
                ....*....|
gi 19111912 347 EEGvlKVIIG 356
Cdd:cd08239 331 ESG--KVVFV 338
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 22-354 1.09e-39

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 143.43  E-value: 1.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   22 PGQTLTD-------DHQVKVAIKATGICGSDVHYWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPG 94
Cdd:PRK05396  11 PGLWLTDvpvpepgPNDVLIKVKKTAICGTDVHIYNWDEWAQKTIPVPMVVGHEFVGEVVEVGSEVTGFKVGDRVSGEGH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   95 CVCRLCDYCRSGRYNLCPHME---------FAatppydgtlrTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRG 165
Cdd:PRK05396  91 IVCGHCRNCRAGRRHLCRNTKgvgvnrpgaFA----------EYLVIPAFNVWKIPDDIPDDLAAIFDPFGNAVHTALSF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  166 NLkCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKyVGAkpfTPIAAKENESLPDYAQRYKqaiiEKY 245
Cdd:PRK05396 161 DL-VGEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELARK-MGA---TRAVNVAKEDLRDVMAELG----MTE 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  246 GeFDFAVDATGVGICIHTAVLALKRGGTFvqAGNGKPVIDFPI--NHIINYEINVlgsfryaHGCYKQSLF--------L 315
Cdd:PRK05396 232 G-FDVGLEMSGAPSAFRQMLDNMNHGGRI--AMLGIPPGDMAIdwNKVIFKGLTI-------KGIYGREMFetwykmsaL 301

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 19111912  316 VSNGLvDVKPLITHRFAFKDALKAYETVASGEEGvlKVI 354
Cdd:PRK05396 302 LQSGL-DLSPIITHRFPIDDFQKGFEAMRSGQSG--KVI 337
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 28-341 5.17e-39

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: 141.59  E-value: 5.17e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  28 DDHQVKVAIKATGICGSDVHYWKegGIGDFIlKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGR 107
Cdd:cd08260  24 PPDGVVVEVEACGVCRSDWHGWQ--GHDPDV-TLPHVPGHEFAGVVVEVGEDVSRWRVGDRVTVPFVLGCGTCPYCRAGD 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 108 YNLCPHMefaaTPP---YDGTLRTYY-ITTEDF-CTKLPKQISVEEGAL----FepmSVAVHAMT-RGNLKCGSRVLVMG 177
Cdd:cd08260 101 SNVCEHQ----VQPgftHPGSFAEYVaVPRADVnLVRLPDDVDFVTAAGlgcrF---ATAFRALVhQARVKPGEWVAVHG 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 178 CGTVGLLMMAVAKAYGAiDIVAVDASPSRVEFAQKyVGAKpfTPIAAKENESLPdyaqrykQAIIEKY-GEFDFAVDATG 256
Cdd:cd08260 174 CGGVGLSAVMIASALGA-RVIAVDIDDDKLELARE-LGAV--ATVNASEVEDVA-------AAVRDLTgGGAHVSVDALG 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 257 VGICIHTAVLALKRGGTFVQAG---NGKPVIDFPINHIINYEINVLGSFRYAHGCYKQSLFLVSNGLVDVKPLITHRFAF 333
Cdd:cd08260 243 IPETCRNSVASLRKRGRHVQVGltlGEEAGVALPMDRVVARELEIVGSHGMPAHRYDAMLALIASGKLDPEPLVGRTISL 322


                ....*...
gi 19111912 334 KDALKAYE 341
Cdd:cd08260 323 DEAPDALA 330
tdh TIGR00692
L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme ...
 28-355 7.64e-38

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: 138.45  E-value: 7.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912    28 DDHQVKVAIKATGICGSDVHYWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGR 107
Cdd:TIGR00692  22 GPGEVLIKVLATSICGTDVHIYNWDEWAQSRIKPPQVVGHEVAGEVVGIGPGVEGIKVGDYVSVETHIVCGKCYACRRGQ 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   108 YNLCPHMEFAATPPyDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRGNLkCGSRVLVMGCGTVGLLMMA 187
Cdd:TIGR00692 102 YHVCQNTKIFGVDT-DGCFAEYAVVPAQNIWKNPKSIPPEYATIQEPLGNAVHTVLAGPI-SGKSVLVTGAGPIGLMAIA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   188 VAKAYGAIDIVAVDASPSRVEFAQKyVGAkpfTPIAAKENESLPDYAqrykQAIIEKYGeFDFAVDATGVGICIHTAVLA 267
Cdd:TIGR00692 180 VAKASGAYPVIVSDPNEYRLELAKK-MGA---TYVVNPFKEDVVKEV----ADLTDGEG-VDVFLEMSGAPKALEQGLQA 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   268 LKRGGTFVQAG--NGKPVIDFpINHIINYEINVLGSF-RYAHGCYKQSLFLVSNGLVDVKPLITHRFAFKDALKAYETVA 344
Cdd:TIGR00692 251 VTPGGRVSLLGlpPGKVTIDF-TNKVIFKGLTIYGITgRHMFETWYTVSRLIQSGKLDLDPIITHKFKFDKFEKGFELMR 329

                         330
                  ....*....|.
gi 19111912   345 SGEEGvlKVII 355
Cdd:TIGR00692 330 SGQTG--KVIL 338
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
29-355 2.23e-37

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 137.52  E-value: 2.23e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  29 DHQVKVAIKATGICGSDVHYWKeggiGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRY 108
Cdd:COG1062  16 PGEVLVRIVAAGLCHSDLHVRD----GDLPVPLPAVLGHEGAGVVEEVGPGVTGVAPGDHVVLSFIPSCGHCRYCASGRP 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 109 NLCphMEFAAT----PPYDGTLR-------------------TYYITTEDFCTKLPKQISVEEGALFepmSVAVhaMT-- 163
Cdd:COG1062  92 ALC--EAGAALngkgTLPDGTSRlssadgepvghffgqssfaEYAVVPERSVVKVDKDVPLELAALL---GCGV--QTga 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 164 -----RGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYvGAKPFtpIAAKENEslpdyAQRYK 238
Cdd:COG1062 165 gavlnTAKVRPGDTVAVFGLGGVGLSAVQGARIAGASRIIAVDPVPEKLELAREL-GATHT--VNPADED-----AVEAV 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 239 QAIIEkyGEFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPV--IDFPINHIINYEINVLGSfrYAHGCYKQSLF-- 314
Cdd:COG1062 237 RELTG--GGVDYAFETTGNPAVIRQALEALRKGGTVVVVGLAPPGaeISLDPFQLLLTGRTIRGS--YFGGAVPRRDIpr 312

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 19111912 315 ---LVSNGLVDVKPLITHRFAFKDALKAYETVASGEegVLKVII 355
Cdd:COG1062 313 lvdLYRAGRLPLDELITRRYPLDEINEAFDDLRSGE--VIRPVI 354
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 6-355 3.62e-37

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: 137.67  E-value: 3.62e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLTDDHQVKVAIKATGICGSDVHYWkEGGIGDfiLKKPMILGHESAGVVVEVGKGVSSLKP 85
Cdd:cd08283   2 KALVWHGKGDVRVEEVPDPKIEDPTDAIVRVTATAICGSDLHLY-HGYIPG--MKKGDILGHEFMGVVEEVGPEVRNLKV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  86 GDPVAVEPGCVCRLCDYCRSGRYNLC----PHMEFAA---------------TPPYDGT----LRTYYittEDF-CTKLP 141
Cdd:cd08283  79 GDRVVVPFTIACGECFYCKRGLYSQCdntnPSAEMAKlyghagagifgyshlTGGYAGGqaeyVRVPF---ADVgPFKIP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 142 KQISVEEgALF--EPMSVAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYVGAkpf 219
Cdd:cd08283 156 DDLSDEK-ALFlsDILPTGYHAAELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLGA--- 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 220 TPIAAKENESLPDyaqrykqAIIEKYGEF--DFAVDATGV---------------------GICIHTAVLALKRGGTFVQ 276
Cdd:cd08283 232 ETINFEEVDDVVE-------ALRELTGGRgpDVCIDAVGMeahgsplhkaeqallkletdrPDALREAIQAVRKGGTVSI 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 277 AGN-GKPVIDFPINHIINYEINVLGSfRYAHGCYKQSLF-LVSNGLVDVKPLITHRFAFKDALKAYETVASGEEGVLKVI 354
Cdd:cd08283 305 IGVyGGTVNKFPIGAAMNKGLTLRMG-QTHVQRYLPRLLeLIESGELDPSFIITHRLPLEDAPEAYKIFDKKEDGCIKVV 383


                .
gi 19111912 355 I 355
Cdd:cd08283 384 L 384
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
 30-355 9.86e-37

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: 135.61  E-value: 9.86e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  30 HQVKVAIKATGICGSDVH-------YWKEGGIGDFIlKKPMILGHESAGVVVEVGKGVSS--LKPGDPVAVEPGCVCRLC 100
Cdd:cd08256  25 GEILVKVEACGICAGDIKcyhgapsFWGDENQPPYV-KPPMIPGHEFVGRVVELGEGAEErgVKVGDRVISEQIVPCWNC 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 101 DYCRSGRYNLC-PHMEFAATPPYDGTLRTYYITTED-FCTKLPKQISVEEGALFEPMSVAVHAMTRGNLKCGSRVLVMGC 178
Cdd:cd08256 104 RFCNRGQYWMCqKHDLYGFQNNVNGGMAEYMRFPKEaIVHKVPDDIPPEDAILIEPLACALHAVDRANIKFDDVVVLAGA 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 179 GTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYvGAKPFTPIAAKE--NESLpdyaqrykqAIIEKYGeFDFAVDATG 256
Cdd:cd08256 184 GPLGLGMIGAARLKNPKKLIVLDLKDERLALARKF-GADVVLNPPEVDvvEKIK---------ELTGGYG-CDIYIEATG 252

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 257 VGICIHTAVLALKRGGTFVQ-AGNGKPV-IDFPinhIIN--YEINVLGSfRYAHGCYKQSLFLVSNGLVDVKPLITHRFA 332
Cdd:cd08256 253 HPSAVEQGLNMIRKLGRFVEfSVFGDPVtVDWS---IIGdrKELDVLGS-HLGPYCYPIAIDLIASGRLPTDGIVTHQFP 328

                       330       340
                ....*....|....*....|...
gi 19111912 333 FKDALKAYETVASGEEGvLKVII 355
Cdd:cd08256 329 LEDFEEAFELMARGDDS-IKVVL 350
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 6-347 2.19e-36

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


Pssm-ID: 176220 [Multi-domain]  Cd Length: 332  Bit Score: 134.37  E-value: 2.19e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRK-KMDTAIEDRPGQTLTDDhQVKVAIKATGICGSDVHYWKeggiGDF-ILKKPMILGHESAGVVVEVGKGVSSL 83
Cdd:cd08259   2 KAAILHKpNKPLQIEEVPDPEPGPG-EVLIKVKAAGVCYRDLLFWK----GFFpRGKYPLILGHEIVGTVEEVGEGVERF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  84 KPGDPVAVEPGCVCRLCDYCRSGRYNLCPH-MEFAATppYDGTLRTYYITTEDFCTKLPKQISVEEGALFE-PMSVAVHA 161
Cdd:cd08259  77 KPGDRVILYYYIPCGKCEYCLSGEENLCRNrAEYGEE--VDGGFAEYVKVPERSLVKLPDNVSDESAALAAcVVGTAVHA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 162 MTRGNLKCGSRVLVMGC-GTVGLLMMAVAKAYGAiDIVAVDASPSRVEFAQKyVGAKPFTPIAAKENEslpdyaqrykqa 240
Cdd:cd08259 155 LKRAGVKKGDTVLVTGAgGGVGIHAIQLAKALGA-RVIAVTRSPEKLKILKE-LGADYVIDGSKFSED------------ 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 241 iIEKYGEFDFAVDAtgVGI-CIHTAVLALKRGGTFVQAGNGKP-VIDFPINHIINYEINVLGSFRYAHGCYKQSLFLVSN 318
Cdd:cd08259 221 -VKKLGGADVVIEL--VGSpTIEESLRSLNKGGRLVLIGNVTPdPAPLRPGLLILKEIRIIGSISATKADVEEALKLVKE 297

                       330       340
                ....*....|....*....|....*....
gi 19111912 319 GLvdVKPLITHRFAFKDALKAYETVASGE 347
Cdd:cd08259 298 GK--IKPVIDRVVSLEDINEALEDLKSGK 324
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 6-355 4.42e-34

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: 128.52  E-value: 4.42e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLTDDHQVKVAIKATGICGSDVHYWKeggiGDFILKKP-MILGHESAGVVVEVGKGVSSLK 84
Cdd:cd08286   2 KALVYHGPGKISWEDRPKPTIQEPTDAIVKMLKTTICGTDLHILK----GDVPTVTPgRILGHEGVGVVEEVGSAVTNFK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  85 PGDPVAVEPGCVCRLCDYCRSGRYNLCP-------HM------EFAATPPYDGTLRtyyittedfctKLPKQISVEEGAL 151
Cdd:cd08286  78 VGDRVLISCISSCGTCGYCRKGLYSHCEsggwilgNLidgtqaEYVRIPHADNSLY-----------KLPEGVDEEAAVM 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 152 FEPMSVAVH--AMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYvGAkpftpiAAKENES 229
Cdd:cd08286 147 LSDILPTGYecGVLNGKVKPGDTVAIVGAGPVGLAALLTAQLYSPSKIIMVDLDDNRLEVAKKL-GA------THTVNSA 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 230 LPDYAQRYKqAIIEKYGeFDFAVDATGVGICIHTAVLALKRGGTFVQAG-NGKPViDFPINHIINYEINVLGSFRYAHgC 308
Cdd:cd08286 220 KGDAIEQVL-ELTDGRG-VDVVIEAVGIPATFELCQELVAPGGHIANVGvHGKPV-DLHLEKLWIKNITITTGLVDTN-T 295

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 19111912 309 YKQSLFLVSNGLVDVKPLITHRFAFKDALKAYETV-ASGEEGVLKVII 355
Cdd:cd08286 296 TPMLLKLVSSGKLDPSKLVTHRFKLSEIEKAYDTFsAAAKHKALKVII 343
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 29-355 5.68e-34

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: 128.43  E-value: 5.68e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  29 DHQVKVAIKATGICGSDVHYWKeggiGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRY 108
Cdd:cd08279  25 PGEVLVRIAAAGLCHSDLHVVT----GDLPAPLPAVLGHEGAGVVEEVGPGVTGVKPGDHVVLSWIPACGTCRYCSRGQP 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 109 NLCP-HMEFAATPPYDGTLRT------------------YYITTEDFCTKLPKQISVEEGALfepMSVAVhaMT------ 163
Cdd:cd08279 101 NLCDlGAGILGGQLPDGTRRFtadgepvgamcglgtfaeYTVVPEASVVKIDDDIPLDRAAL---LGCGV--TTgvgavv 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 164 -RGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYvGAKPFtpIAAKENEslpdyAQRYKQAII 242
Cdd:cd08279 176 nTARVRPGDTVAVIGCGGVGLNAIQGARIAGASRIIAVDPVPEKLELARRF-GATHT--VNASEDD-----AVEAVRDLT 247

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 243 EKYGeFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKP--VIDFPINHIINYEINVLGSF-----------RYAHgcy 309
Cdd:cd08279 248 DGRG-ADYAFEAVGRAATIRQALAMTRKGGTAVVVGMGPPgeTVSLPALELFLSEKRLQGSLygsanprrdipRLLD--- 323

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 19111912 310 kqslfLVSNGLVDVKPLITHRFAFKDALKAYETVASGEegVLKVII 355
Cdd:cd08279 324 -----LYRAGRLKLDELVTRRYSLDEINEAFADMLAGE--NARGVI 362
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
6-344 1.13e-33

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 127.64  E-value: 1.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912    6 KAFVLRKKMDTAIEDRPGQTLTDDHQVKVAIKATGICGSDV--------HYWkeggigdfilkkPMILGHESAGVVVEVG 77
Cdd:PRK10309   2 KSVVNDTDGIVRVAESPIPEIKHQDDVLVKVASSGLCGSDIprifkngaHYY------------PITLGHEFSGYVEAVG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   78 KGVSSLKPGDPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATPPyDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSV 157
Cdd:PRK10309  70 SGVDDLHPGDAVACVPLLPCFTCPECLRGFYSLCAKYDFIGSRR-DGGNAEYIVVKRKNLFALPTDMPIEDGAFIEPITV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  158 AVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYVGAKPFTP--IAAKENESLPDyAQ 235
Cdd:PRK10309 149 GLHAFHLAQGCEGKNVIIIGAGTIGLLAIQCAVALGAKSVTAIDINSEKLALAKSLGAMQTFNSreMSAPQIQSVLR-EL 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  236 RYKQAIIEKYG---EFDFAVDATGVGICIhTAVLALKRGGTFVQAGNGKpvidfpinhIINYEINVLGSFRYAHGC---- 308
Cdd:PRK10309 228 RFDQLILETAGvpqTVELAIEIAGPRAQL-ALVGTLHHDLHLTSATFGK---------ILRKELTVIGSWMNYSSPwpgq 297

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 19111912  309 -YKQSLFLVSNGLVDVKPLITHRFAFKDALKAYETVA 344
Cdd:PRK10309 298 eWETASRLLTERKLSLEPLIAHRGSFESFAQAVRDLA 334
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 31-355 7.64e-33

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: 125.45  E-value: 7.64e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  31 QVKVAIKATGICGSDVHYWKeggiGDF-ILKKPMILGHES-----AGVVVEVGKGVSS-LKPGDPVAVEPGCVCRLCDYC 103
Cdd:cd08231  27 AVLVRVRLAGVCGSDVHTVA----GRRpRVPLPIILGHEGvgrvvALGGGVTTDVAGEpLKVGDRVTWSVGAPCGRCYRC 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 104 RSGRYNLCP------HMEFAATPPYDGTLRTYYI---TTEDFctKLPKQISVEEGAL-FEPMSVAVHAMTR-GNLKCGSR 172
Cdd:cd08231 103 LVGDPTKCEnrkkygHEASCDDPHLSGGYAEHIYlppGTAIV--RVPDNVPDEVAAPaNCALATVLAALDRaGPVGAGDT 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 173 VLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYvGAkpfTPIAAKENESLPDyAQRYKQAIIEKYGeFDFAV 252
Cdd:cd08231 181 VVVQGAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAREF-GA---DATIDIDELPDPQ-RRAIVRDITGGRG-ADVVI 254

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 253 DATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPIN--HIINYEINVLGSFRYAHGCYKQSL-FLVSN-GLVDVKPLIT 328
Cdd:cd08231 255 EASGHPAAVPEGLELLRRGGTYVLVGSVAPAGTVPLDpeRIVRKNLTIIGVHNYDPSHLYRAVrFLERTqDRFPFAELVT 334

                       330       340
                ....*....|....*....|....*..
gi 19111912 329 HRFAFKDALKAYETVASGEegVLKVII 355
Cdd:cd08231 335 HRYPLEDINEALELAESGT--ALKVVI 359
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 18-353 1.04e-32

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: 125.71  E-value: 1.04e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  18 IEDRPGQTLTDDhQVKVAIKATGICGSDVHYW---KEG-----GIGDFilkkPMILGHESAGVVVEVGKGVSSLKPGDPV 89
Cdd:cd08265  41 VEDVPVPNLKPD-EILIRVKACGICGSDIHLYetdKDGyilypGLTEF----PVVIGHEFSGVVEKTGKNVKNFEKGDPV 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  90 AVEPGCVCRLCDYCRSGRYNLCPH---MEFAAtppyDGTLRTYYITTEDFCTKLPKQISV-------EEGALFEPMSVAV 159
Cdd:cd08265 116 TAEEMMWCGMCRACRSGSPNHCKNlkeLGFSA----DGAFAEYIAVNARYAWEINELREIysedkafEAGALVEPTSVAY 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 160 HAM-TR-GNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKyVGAK-PFTPIaaKENESLPdyaqr 236
Cdd:cd08265 192 NGLfIRgGGFRPGAYVVVYGAGPIGLAAIALAKAAGASKVIAFEISEERRNLAKE-MGADyVFNPT--KMRDCLS----- 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 237 yKQAIIEKYGEF--DFAVDATGVG---ICIHTAVLALKrgGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYA-HGCYK 310
Cdd:cd08265 264 -GEKVMEVTKGWgaDIQVEAAGAPpatIPQMEKSIAIN--GKIVYIGRAATTVPLHLEVLQVRRAQIVGAQGHSgHGIFP 340

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 19111912 311 QSLFLVSNGLVDVKPLITHRFAFKDALKAYETVASGEEGVLKV 353
Cdd:cd08265 341 SVIKLMASGKIDMTKIITARFPLEGIMEAIKAASERTDGKITI 383
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 54-355 4.11e-32

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: 121.61  E-value: 4.11e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  54 IGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVepgcvcrlcdycrsgrynLCPHmefaatppydgtlRTYYITT 133
Cdd:cd08255  13 TGTEKLPLPLPPGYSSVGRVVEVGSGVTGFKPGDRVFC------------------FGPH-------------AERVVVP 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 134 EDFCTKLPKQISVEEGALFEPMSVAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKY 213
Cdd:cd08255  62 ANLLVPLPDGLPPERAALTALAATALNGVRDAEPRLGERVAVVGLGLVGLLAAQLAKAAGAREVVGVDPDAARRELAEAL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 214 VGAKPFTPIAAKENEslpdyaqrykqaiiekYGEFDFAVDATGVGICIHTAVLALKRGGT-----FVQAGNGKPVIDFPI 288
Cdd:cd08255 142 GPADPVAADTADEIG----------------GRGADVVIEASGSPSALETALRLLRDRGRvvlvgWYGLKPLLLGEEFHF 205

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19111912 289 NH--IINYEINVLGSFRYAHGCYKQSLFLVSNGLVD---VKPLITHRFAFKDALKAYETVASGEEGVLKVII 355
Cdd:cd08255 206 KRlpIRSSQVYGIGRYDRPRRWTEARNLEEALDLLAegrLEALITHRVPFEDAPEAYRLLFEDPPECLKVVL 277
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 6-355 7.56e-32

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: 122.37  E-value: 7.56e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLTDDHQVKVAIKATGICGSDVHYWKeggiGDFILKKPMILGHESAGVVVEVGKGVSSLKP 85
Cdd:cd08284   2 KAVVFKGPGDVRVEEVPIPQIQDPTDAIVKVTAAAICGSDLHIYR----GHIPSTPGFVLGHEFVGEVVEVGPEVRTLKV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  86 GDPVAVEPGCVCRLCDYCRSGRYNLCP----------------HMEFAATPPYDGTLRtyyittedfctKLPKQISVEEG 149
Cdd:cd08284  78 GDRVVSPFTIACGECFYCRRGQSGRCAkgglfgyagspnldgaQAEYVRVPFADGTLL-----------KLPDGLSDEAA 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 150 ALF-EPMSVAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKyVGAKPFTPIAAkene 228
Cdd:cd08284 147 LLLgDILPTGYFGAKRAQVRPGDTVAVIGCGPVGLCAVLSAQVLGAARVFAVDPVPERLERAAA-LGAEPINFEDA---- 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 229 slpdyaqRYKQAIIEKYGE--FDFAVDATGVGICIHTAVLALKRGGTFVQAG-NGKPVIDFPINHIINYEINvlgsFRYA 305
Cdd:cd08284 222 -------EPVERVREATEGrgADVVLEAVGGAAALDLAFDLVRPGGVISSVGvHTAEEFPFPGLDAYNKNLT----LRFG 290

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19111912 306 hGCYKQSLF-----LVSNGLVDVKPLITHRFAFKDALKAYETVASGEegVLKVII 355
Cdd:cd08284 291 -RCPVRSLFpellpLLESGRLDLEFLIDHRMPLEEAPEAYRLFDKRK--VLKVVL 342
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 29-302 2.81e-31

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: 120.68  E-value: 2.81e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  29 DHQVKVAIKATGICGSDVHY----WKEGgigdfilKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVepGCV---CRLCD 101
Cdd:cd05283  24 PDDVDIKITYCGVCHSDLHTlrneWGPT-------KYPLVPGHEIVGIVVAVGSKVTKFKVGDRVGV--GCQvdsCGTCE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 102 YCRSGRYNLCPHMEFAATPPY-DGTLR-----TYYITTEDFCTKLPKQISVEEGAlfePMSVA---VHA-MTRGNLKCGS 171
Cdd:cd05283  95 QCKSGEEQYCPKGVVTYNGKYpDGTITqggyaDHIVVDERFVFKIPEGLDSAAAA---PLLCAgitVYSpLKRNGVGPGK 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 172 RVLVMGCGtvGLLMMAV--AKAYGAiDIVAVDASPSRVEFAQKYvGAKPFtpIAAKENESLPDYAqrykqaiiekyGEFD 249
Cdd:cd05283 172 RVGVVGIG--GLGHLAVkfAKALGA-EVTAFSRSPSKKEDALKL-GADEF--IATKDPEAMKKAA-----------GSLD 234

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 19111912 250 FAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSF 302
Cdd:cd05283 235 LIIDTVSASHDLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGRKSVAGSL 287
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 17-347 3.98e-31

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: 120.36  E-value: 3.98e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  17 AIEDRPGQTLTDDhQVKVAIKATGICGSDVHYWK--EGGIGDFILkkPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPG 94
Cdd:cd05284  14 RLEDVPVPEPGPG-QVLVRVGGAGVCHSDLHVIDgvWGGILPYKL--PFTLGHENAGWVEEVGSGVDGLKEGDPVVVHPP 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  95 CVCRLCDYCRSGRYNLCPHmefAATPP--YDGTLRTYYITTEDFCTKLPKQISVEEGAlfePMS----VAVHAMTRGN-- 166
Cdd:cd05284  91 WGCGTCRYCRRGEENYCEN---ARFPGigTDGGFAEYLLVPSRRLVKLPRGLDPVEAA---PLAdaglTAYHAVKKALpy 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 167 LKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYvGAKPFTPIAAKENESLpdyaqrykqAIIEKYG 246
Cdd:cd05284 165 LDPGSTVVVIGVGGLGHIAVQILRALTPATVIAVDRSEEALKLAERL-GADHVLNASDDVVEEV---------RELTGGR 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 247 EFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPViDFPINHIINYEINVLGSFryaHGCYK---QSLFLVSNGLvdV 323
Cdd:cd05284 235 GADAVIDFVGSDETLALAAKLLAKGGRYVIVGYGGHG-RLPTSDLVPTEISVIGSL---WGTRAelvEVVALAESGK--V 308

                       330       340
                ....*....|....*....|....
gi 19111912 324 KPLIThRFAFKDALKAYETVASGE 347
Cdd:cd05284 309 KVEIT-KFPLEDANEALDRLREGR 331
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 17-355 1.17e-30

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: 119.85  E-value: 1.17e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  17 AIEDRPGQTltddHQVKVAIKATGICGSDVHYWKeggiGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCV 96
Cdd:cd05279  17 EIEVAPPKA----GEVRIKVVATGVCHTDLHVID----GKLPTPLPVILGHEGAGIVESIGPGVTTLKPGDKVIPLFGPQ 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  97 CRLCDYCRSGRYNLCphMEFAATPP----YDGTLR------------------TYYITTEDFCTKLPKQISVEEGALFE- 153
Cdd:cd05279  89 CGKCKQCLNPRPNLC--SKSRGTNGrglmSDGTSRftckgkpihhflgtstfaEYTVVSEISLAKIDPDAPLEKVCLIGc 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 154 PMSVAVHAMTR-GNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAqKYVGakpftpiaAKENESLPD 232
Cdd:cd05279 167 GFSTGYGAAVNtAKVTPGSTCAVFGLGGVGLSVIMGCKAAGASRIIAVDINKDKFEKA-KQLG--------ATECINPRD 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 233 YAQRYKQAIIE-KYGEFDFAVDATGVGICIHTAVLAL-KRGGTFVQAGNGkpvidfPINHIINYEINVLGSFRYAHGCY- 309
Cdd:cd05279 238 QDKPIVEVLTEmTDGGVDYAFEVIGSADTLKQALDATrLGGGTSVVVGVP------PSGTEATLDPNDLLTGRTIKGTVf 311

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19111912 310 ------KQSLFLVS---NGLVDVKPLITHRFAFKDALKAYETVASGEegVLKVII 355
Cdd:cd05279 312 ggwkskDSVPKLVAlyrQKKFPLDELITHVLPFEEINDGFDLMRSGE--SIRTIL 364
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 6-341 2.60e-30

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 118.22  E-value: 2.60e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912    6 KAFVLRK-KMDTAIEDRPGQTLTDDhQVKVAIKATGICGSDVHYWKeggiGDFI-LKKPMILGHESAGVVVEVGKGVSSL 83
Cdd:PRK13771   2 KAVILPGfKQGYRIEEVPDPKPGKD-EVVIKVNYAGLCYRDLLQLQ----GFYPrMKYPVILGHEVVGTVEEVGENVKGF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   84 KPGDPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATpPYDGTLRTYYITTEDFCTKLPKQISvEEGALFEP--MSVAVHA 161
Cdd:PRK13771  77 KPGDRVASLLYAPDGTCEYCRSGEEAYCKNRLGYGE-ELDGFFAEYAKVKVTSLVKVPPNVS-DEGAVIVPcvTGMVYRG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  162 MTRGNLKCGSRVLVMGC-GTVGLLMMAVAKAYGAiDIVAVDASPSRVEFAQKY-----VGAKpftpiaakeneslpdYAQ 235
Cdd:PRK13771 155 LRRAGVKKGETVLVTGAgGGVGIHAIQVAKALGA-KVIAVTSSESKAKIVSKYadyviVGSK---------------FSE 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  236 RYKqaiieKYGEFDFAVDATGvGICIHTAVLALKRGGTFVQAGNGKP--VIDFPINHIINYEINVLGSFRYAHGCYKQSL 313
Cdd:PRK13771 219 EVK-----KIGGADIVIETVG-TPTLEESLRSLNMGGKIIQIGNVDPspTYSLRLGYIILKDIEIIGHISATKRDVEEAL 292

                        330       340
                 ....*....|....*....|....*...
gi 19111912  314 FLVSNGlvDVKPLITHRFAFKDALKAYE 341
Cdd:PRK13771 293 KLVAEG--KIKPVIGAEVSLSEIDKALE 318
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 6-355 2.09e-29

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: 115.87  E-value: 2.09e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMdTAIEDRPGQTLTDDhQVKVAIKATGICGSDVHYWKE--------GGIGDFILKKPMILGHE-SAGVVVEV 76
Cdd:cd08262   2 RAAVFRDGP-LVVRDVPDPEPGPG-QVLVKVLACGICGSDLHATAHpeamvddaGGPSLMDLGADIVLGHEfCGEVVDYG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  77 GKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRYNLCPhmefaatppydGTLRTYYITTEDFCTKLPKQISVEEGALFEPMS 156
Cdd:cd08262  80 PGTERKLKVGTRVTSLPLLLCGQGASCGIGLSPEAP-----------GGYAEYMLLSEALLLRVPDGLSMEDAALTEPLA 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 157 VAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKyVGAKPFtpIAAKEnESLPDYAQR 236
Cdd:cd08262 149 VGLHAVRRARLTPGEVALVIGCGPIGLAVIAALKARGVGPIVASDFSPERRALALA-MGADIV--VDPAA-DSPFAAWAA 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 237 YKQAIIEKYGEFDF-AVDATGVgicIHTAVLALKRGGTFVQAGnGKPVIDfpinHI-----INYEINVLGSFRYAHGCYK 310
Cdd:cd08262 225 ELARAGGPKPAVIFeCVGAPGL---IQQIIEGAPPGGRIVVVG-VCMESD----NIepalaIRKELTLQFSLGYTPEEFA 296

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 19111912 311 QSLFLVSNGLVDVKPLITHRFAFKDALKAYETVASGEEGVlKVII 355
Cdd:cd08262 297 DALDALAEGKVDVAPMVTGTVGLDGVPDAFEALRDPEHHC-KILV 340
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 14-355 2.81e-29

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: 115.93  E-value: 2.81e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  14 MDTAIEDRPGQTLTDDH---------QVKVAIKATGICGSDVHYWKeggiGDFILKKPMILGHESAGVVV---EVGKGVS 81
Cdd:cd08263   1 MKAAVLKGPNPPLTIEEipvprpkegEILIRVAACGVCHSDLHVLK----GELPFPPPFVLGHEISGEVVevgPNVENPY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  82 SLKPGDPVAVEPGCVCRLCDYCRSGRYNLCPhmEFAA-----TPPYDGTLR------------------TYYITTEDFCT 138
Cdd:cd08263  77 GLSVGDRVVGSFIMPCGKCRYCARGKENLCE--DFFAynrlkGTLYDGTTRlfrldggpvymysmgglaEYAVVPATALA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 139 KLPKQISVEEGAlfePMSVAV----HAMTR-GNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAqKY 213
Cdd:cd08263 155 PLPESLDYTESA---VLGCAGftayGALKHaADVRPGETVAVIGVGGVGSSAIQLAKAFGASPIIAVDVRDEKLAKA-KE 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 214 VGAKpFTPIAAKEneslpDYAQRYKQAIIEkyGEFDFAVDATGVGICIHTAVLALKRGGTFVQAG--NGKPVIDFPINHI 291
Cdd:cd08263 231 LGAT-HTVNAAKE-----DAVAAIREITGG--RGVDVVVEALGKPETFKLALDVVRDGGRAVVVGlaPGGATAEIPITRL 302

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19111912 292 INYEINVLGSFRYAHgcyKQSL----FLVSNGLVDVKPLITHRFAFKDALKAYETVASGEEGVLKVII 355
Cdd:cd08263 303 VRRGIKIIGSYGARP---RQDLpelvGLAASGKLDPEALVTHKYKLEEINEAYENLRKGLIHGRAIVE 367
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 29-355 6.53e-29

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: 113.99  E-value: 6.53e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  29 DHQVKVAIKATGICGSDVHYWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGcvcrlcdycrsgry 108
Cdd:cd08269  19 PGQVLVRVEGCGVCGSDLPAFNQGRPWFVYPAEPGGPGHEGWGRVVALGPGVRGLAVGDRVAGLSG-------------- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 109 nlcphmefaatppydGTLRTYYITTEDFCTKLPKQISVEEGALfEPMSVAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAV 188
Cdd:cd08269  85 ---------------GAFAEYDLADADHAVPLPSLLDGQAFPG-EPLGCALNVFRRGWIRAGKTVAVIGAGFIGLLFLQL 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 189 AKAYGAIDIVAVDASPSRVEFAQKYVGAKPFTPIAakeneslpdyaqrykQAIIEKYGE------FDFAVDATGVGICIH 262
Cdd:cd08269 149 AAAAGARRVIAIDRRPARLALARELGATEVVTDDS---------------EAIVERVREltggagADVVIEAVGHQWPLD 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 263 TAVLALKRGGTFVQAG--NGKPVidfPIN-HIINY-EINVLGSFRYAHGCYKQSLF----LVSNGLVDVKPLITHRFAFK 334
Cdd:cd08269 214 LAGELVAERGRLVIFGyhQDGPR---PVPfQTWNWkGIDLINAVERDPRIGLEGMReavkLIADGRLDLGSLLTHEFPLE 290

                       330       340
                ....*....|....*....|.
gi 19111912 335 DALKAYETVASGEEGVLKVII 355
Cdd:cd08269 291 ELGDAFEAARRRPDGFIKGVI 311
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 30-139 2.76e-28

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: 106.15  E-value: 2.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912    30 HQVKVAIKATGICGSDVHYWKEGgigDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRYN 109
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGG---NPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYN 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 19111912   110 LCPHMEFAATpPYDGTLRTYYITTEDFCTK 139
Cdd:pfam08240  78 LCPNGRFLGY-DRDGGFAEYVVVPERNLVP 106
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 31-347 4.08e-28

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: 112.86  E-value: 4.08e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  31 QVKVAIKATGICGSDVHYWKeggiGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPV--AVEPGCVCrlCDYCRSGRY 108
Cdd:cd08281  35 EVLVKIAAAGLCHSDLSVIN----GDRPRPLPMALGHEAAGVVVEVGEGVTDLEVGDHVvlVFVPSCGH--CRPCAEGRP 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 109 NLCphmEFAATPPYDGTLRT-----------------------YYITTEDFCTKLPKQISVEEGALF--EPMSVAVHAMT 163
Cdd:cd08281 109 ALC---EPGAAANGAGTLLSggrrlrlrggeinhhlgvsafaeYAVVSRRSVVKIDKDVPLEIAALFgcAVLTGVGAVVN 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 164 RGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAqKYVGAkpftpiAAKENESLPDYAQRYKQAiie 243
Cdd:cd08281 186 TAGVRPGQSVAVVGLGGVGLSALLGAVAAGASQVVAVDLNEDKLALA-RELGA------TATVNAGDPNAVEQVREL--- 255

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 244 KYGEFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPINH--IINYEINVLGSfrYAHGCYKQS-----LFLV 316
Cdd:cd08281 256 TGGGVDYAFEMAGSVPALETAYEITRRGGTTVTAGLPDPEARLSVPAlsLVAEERTLKGS--YMGSCVPRRdipryLALY 333

                       330       340       350
                ....*....|....*....|....*....|.
gi 19111912 317 SNGLVDVKPLITHRFAFKDALKAYETVASGE 347
Cdd:cd08281 334 LSGRLPVDKLLTHRLPLDEINEGFDRLAAGE 364
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 6-347 7.02e-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: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 111.47  E-value: 7.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDT--AIEDRPGQTLTDdHQVKVAIKATGICGSDVHYWKeggiGDF--ILKKPMILGHESAGVVVEVGKGVS 81
Cdd:cd08297   2 KAAVVEEFGEKpyEVKDVPVPEPGP-GEVLVKLEASGVCHTDLHAAL----GDWpvKPKLPLIGGHEGAGVVVAVGPGVS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  82 SLKPGDPVAVEP-GCVCRLCDYCRSGRYNLCPHMEFAAtppY--DGTLRTYYITTEDFCTKLPKQISVEEGAlfePM--- 155
Cdd:cd08297  77 GLKVGDRVGVKWlYDACGKCEYCRTGDETLCPNQKNSG---YtvDGTFAEYAIADARYVTPIPDGLSFEQAA---PLlca 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 156 -SVAVHAMTRGNLKCGSRVLVMGCGTvGLLMMAV--AKAYGAiDIVAVDASPSRVEFAQKyVGAKPFtpIAAKENESLpd 232
Cdd:cd08297 151 gVTVYKALKKAGLKPGDWVVISGAGG-GLGHLGVqyAKAMGL-RVIAIDVGDEKLELAKE-LGADAF--VDFKKSDDV-- 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 233 yaqrykQAIIEKYGEF--DFAVDATGVGICIHTAVLALKRGGTFVQAG-NGKPVIDFPINHIINYEINVLGSFryaHGCY 309
Cdd:cd08297 224 ------EAVKELTGGGgaHAVVVTAVSAAAYEQALDYLRPGGTLVCVGlPPGGFIPLDPFDLVLRGITIVGSL---VGTR 294

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 19111912 310 KQS---LFLVSNGLvdVKPLIThRFAFKDALKAYETVASGE 347
Cdd:cd08297 295 QDLqeaLEFAARGK--VKPHIQ-VVPLEDLNEVFEKMEEGK 332
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 6-355 1.90e-26

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: 107.33  E-value: 1.90e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLTDdHQVKVAIKATGICGSDVHYWKeggiGDFilKKPMILGHEsaGVVVEVGKGVSSLKp 85
Cdd:cd08242   2 KALVLDGGLDLRVEDLPKPEPPP-GEALVRVLLAGICNTDLEIYK----GYY--PFPGVPGHE--FVGIVEEGPEAELV- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  86 GDPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATPPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRG 165
Cdd:cd08242  72 GKRVVGEINIACGRCEYCRRGLYTHCPNRTVLGIVDRDGAFAEYLTLPLENLHVVPDLVPDEQAVFAEPLAAALEILEQV 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 166 NLKCGSRVLVMGCGTVGLLMMAVAKAYGAiDIVAVDASPSRVEFAQKyVGAKPFTPIAAKeneslpdyaqrykqaiiEKY 245
Cdd:cd08242 152 PITPGDKVAVLGDGKLGLLIAQVLALTGP-DVVLVGRHSEKLALARR-LGVETVLPDEAE-----------------SEG 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 246 GEFDFAVDATGVGICIHTAVLALK-RGGTFVQAGNGKPViDFPINHIINYEINVLGS----FRYAhgcykqsLFLVSNGL 320
Cdd:cd08242 213 GGFDVVVEATGSPSGLELALRLVRpRGTVVLKSTYAGPA-SFDLTKAVVNEITLVGSrcgpFAPA-------LRLLRKGL 284

                       330       340       350
                ....*....|....*....|....*....|....*
gi 19111912 321 VDVKPLITHRFAFKDALKAYEtvASGEEGVLKVII 355
Cdd:cd08242 285 VDVDPLITAVYPLEEALEAFE--RAAEPGALKVLL 317
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 6-355 8.32e-26

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: 106.17  E-value: 8.32e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTL-TDDHQVKvaIKATGICGSDVHYWKEGGIGDfilKKPMILGHESAGVVVEVGKGVSSLK 84
Cdd:cd08285   2 KAFAMLGIGKVGWIEKPIPVCgPNDAIVR--PTAVAPCTSDVHTVWGGAPGE---RHGMILGHEAVGVVEEVGSEVKDFK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  85 PGDPVAVEPGCVCRLCDYCRSGRYNLCPHM----EFAATPpyDGTLRTYYITTEDFC--TKLPKQISVEEgALFEP--MS 156
Cdd:cd08285  77 PGDRVIVPAITPDWRSVAAQRGYPSQSGGMlggwKFSNFK--DGVFAEYFHVNDADAnlAPLPDGLTDEQ-AVMLPdmMS 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 157 VAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYvGAkpfTPIAakeneslpDYAqr 236
Cdd:cd08285 154 TGFHGAELANIKLGDTVAVFGIGPVGLMAVAGARLRGAGRIIAVGSRPNRVELAKEY-GA---TDIV--------DYK-- 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 237 yKQAIIEKYGEF------DFAVDATGVGICIHTAVLALKRGGTFVQAG--NGKPVIDFPI--------NHIINYEINVLG 300
Cdd:cd08285 220 -NGDVVEQILKLtggkgvDAVIIAGGGQDTFEQALKVLKPGGTISNVNyyGEDDYLPIPReewgvgmgHKTINGGLCPGG 298

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19111912 301 SFRyahgcYKQSLFLVSNGLVDVKPLITHRF-AFKDALKAYETVASGEEGVLKVII 355
Cdd:cd08285 299 RLR-----MERLASLIEYGRVDPSKLLTHHFfGFDDIEEALMLMKDKPDDLIKPVI 349
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 29-289 4.16e-25

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: 104.50  E-value: 4.16e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  29 DHQVKVAIKATGICGSDVHYwKEGGIGdfiLKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPgCVCRLCDYCRSGRY 108
Cdd:cd08278  27 PDEVLVRIVATGICHTDLVV-RDGGLP---TPLPAVLGHEGAGVVEAVGSAVTGLKPGDHVVLSF-ASCGECANCLSGHP 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 109 NLCPHME---FAATPPyDGTLR--------------------TYYITTEDFCTKLPKQISVEegaLFEPMSVAVhaMTrG 165
Cdd:cd08278 102 AYCENFFplnFSGRRP-DGSTPlslddgtpvhghffgqssfaTYAVVHERNVVKVDKDVPLE---LLAPLGCGI--QT-G 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 166 -----N-LKC--GSRVLVMGCGTVGL-LMMAvAKAYGAIDIVAVDASPSRVEFAQKyVGAkpfT-PIAAKENESLpdyaq 235
Cdd:cd08278 175 agavlNvLKPrpGSSIAVFGAGAVGLaAVMA-AKIAGCTTIIAVDIVDSRLELAKE-LGA---ThVINPKEEDLV----- 244

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19111912 236 rykQAIIEKYGE-FDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPIN 289
Cdd:cd08278 245 ---AAIREITGGgVDYALDTTGVPAVIEQAVDALAPRGTLALVGAPPPGAEVTLD 296
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 29-347 1.31e-24

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: 102.40  E-value: 1.31e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  29 DHQVKVAIKATGICGSDVHYWKEGGIGDfilKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVepGCV---CRLCDYCRS 105
Cdd:cd08245  24 PGEVLIKIEACGVCHTDLHAAEGDWGGS---KYPLVPGHEIVGEVVEVGAGVEGRKVGDRVGV--GWLvgsCGRCEYCRR 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 106 GRYNLCPHMEFAATpPYDGTLRTYYITTEDFCTKLPKQISVEEGAlfePMSVA----VHAMTRGNLKCGSRVLVMGCGTV 181
Cdd:cd08245  99 GLENLCQKAVNTGY-TTQGGYAEYMVADAEYTVLLPDGLPLAQAA---PLLCAgitvYSALRDAGPRPGERVAVLGIGGL 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 182 GLLMMAVAKAYGAiDIVAVDASPSRVEFAQKyVGAKPFtpIAAKENESLPDYAqrykqaiiekyGEFDFAVDATGVGICI 261
Cdd:cd08245 175 GHLAVQYARAMGF-ETVAITRSPDKRELARK-LGADEV--VDSGAELDEQAAA-----------GGADVILVTVVSGAAA 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 262 HTAVLALKRGGTFVQAG-NGKPVIDFPINHIINYEINVLGSfryAHGCYK---QSLFLVSNGlvDVKPlITHRFAFKDAL 337
Cdd:cd08245 240 EAALGGLRRGGRIVLVGlPESPPFSPDIFPLIMKRQSIAGS---THGGRAdlqEALDFAAEG--KVKP-MIETFPLDQAN 313

                       330
                ....*....|
gi 19111912 338 KAYETVASGE 347
Cdd:cd08245 314 EAYERMEKGD 323
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 18-355 1.90e-24

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


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 101.95  E-value: 1.90e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  18 IEDRPGQTLTDDHqVKVAIKATGICGSDVhyWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVC 97
Cdd:cd08266  17 YGDLPEPEPGPDE-VLVRVKAAALNHLDL--WVRRGMPGIKLPLPHILGSDGAGVVEAVGPGVTNVKPGQRVVIYPGISC 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  98 RLCDYCRSGRYNLCPHMEFAATpPYDGTLRTYYITTEDFCTKLPKQISVEEGALFePMS--VAVHA-MTRGNLKCGSRVL 174
Cdd:cd08266  94 GRCEYCLAGRENLCAQYGILGE-HVDGGYAEYVAVPARNLLPIPDNLSFEEAAAA-PLTflTAWHMlVTRARLRPGETVL 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 175 VMGCGT-VGLLMMAVAKAYGAIDIVAVdASPSRVEFAQKyVGAkpftpiaakeneslpDYAQRYKQ--------AIIEKY 245
Cdd:cd08266 172 VHGAGSgVGSAAIQIAKLFGATVIATA-GSEDKLERAKE-LGA---------------DYVIDYRKedfvrevrELTGKR 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 246 GeFDFAVDATGvGICIHTAVLALKRGGTFVQAG---NGKPVIDfpINHIINYEINVLGSFRYAHGCYKQSLFLVSNGlvD 322
Cdd:cd08266 235 G-VDVVVEHVG-AATWEKSLKSLARGGRLVTCGattGYEAPID--LRHVFWRQLSILGSTMGTKAELDEALRLVFRG--K 308

                       330       340       350
                ....*....|....*....|....*....|...
gi 19111912 323 VKPLITHRFAFKDALKAYETVASGeEGVLKVII 355
Cdd:cd08266 309 LKPVIDSVFPLEEAAEAHRRLESR-EQFGKIVL 340
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 6-287 1.48e-21

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: 93.79  E-value: 1.48e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKmdTAIEDRPGQtLTD-------DHQVKVAIKATGICGSDVHYwKEGGIGDfiLKKPMILGHESAGVVVEVGK 78
Cdd:cd08298   2 KAMVLEKP--GPIEENPLR-LTEvpvpepgPGEVLIKVEACGVCRTDLHI-VEGDLPP--PKLPLIPGHEIVGRVEAVGP 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  79 GVSSLKPGDPVAVEP-GCVCRLCDYCRSGRYNLCPHMEFAAtppY--DGTLRTYYITTEDFCTKLPKQISVEEGA-LFEP 154
Cdd:cd08298  76 GVTRFSVGDRVGVPWlGSTCGECRYCRSGRENLCDNARFTG---YtvDGGYAEYMVADERFAYPIPEDYDDEEAApLLCA 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 155 MSVAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAiDIVAVDASPSRVEFAQKyVGAkpftpiaakeneslpDYA 234
Cdd:cd08298 153 GIIGYRALKLAGLKPGQRLGLYGFGASAHLALQIARYQGA-EVFAFTRSGEHQELARE-LGA---------------DWA 215

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 19111912 235 QRYKQaiiEKYGEFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGK-PVIDFP 287
Cdd:cd08298 216 GDSDD---LPPEPLDAAIIFAPVGALVPAALRAVKKGGRVVLAGIHMsDIPAFD 266
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 6-218 9.56e-20

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: 89.19  E-value: 9.56e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLTDDHQVKVAIKATGICGSDVHYWKeggiGDFILKKPMILGHESAGVVVEVGKGVSSLKP 85
Cdd:cd08282   2 KAVVYGGPGNVAVEDVPDPKIEHPTDAIVRITTTAICGSDLHMYR----GRTGAEPGLVLGHEAMGEVEEVGSAVESLKV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  86 GDPVAVEPGCVCRLCDYCRSGRYNLCPHME---------FAATPPYDGT----LRTYYitTEDFCTKLPKQISVEEGALF 152
Cdd:cd08282  78 GDRVVVPFNVACGRCRNCKRGLTGVCLTVNpgraggaygYVDMGPYGGGqaeyLRVPY--ADFNLLKLPDRDGAKEKDDY 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 153 EPMS----VAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKyVGAKP 218
Cdd:cd08282 156 LMLSdifpTGWHGLELAGVQPGDTVAVFGAGPVGLMAAYSAILRGASRVYVVDHVPERLDLAES-IGAIP 224
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 30-355 1.20e-19

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: 88.93  E-value: 1.20e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  30 HQVKVAIKATGICGSDVHYWKEGGIGDFilkkPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRYN 109
Cdd:cd08277  28 NEVRIKMLATSVCHTDILAIEGFKATLF----PVILGHEGAGIVESVGEGVTNLKPGDKVIPLFIGQCGECSNCRSGKTN 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 110 LC--PHMEFAATPPyDGTLR------------------TYYITTEDFCTKLPKQISVEEGALFE-PMSVAVHAMTR-GNL 167
Cdd:cd08277 104 LCqkYRANESGLMP-DGTSRftckgkkiyhflgtstfsQYTVVDENYVAKIDPAAPLEHVCLLGcGFSTGYGAAWNtAKV 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 168 KCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAqKYVGAKPFtpIAAKeneslpDYAQRYKQAIIE-KYG 246
Cdd:cd08277 183 EPGSTVAVFGLGAVGLSAIMGAKIAGASRIIGVDINEDKFEKA-KEFGATDF--INPK------DSDKPVSEVIREmTGG 253

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 247 EFDFAVDATGVGICIHTAVLALKRG-GTFVQAGNGkpvidfPINHIINYEINVLgSFRYAHGCYKQSLFLVSN--GLV-- 321
Cdd:cd08277 254 GVDYSFECTGNADLMNEALESTKLGwGVSVVVGVP------PGAELSIRPFQLI-LGRTWKGSFFGGFKSRSDvpKLVsk 326

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 19111912 322 ------DVKPLITHRFAFKDALKAYETVASGEEgvLKVII 355
Cdd:cd08277 327 ymnkkfDLDELITHVLPFEEINKGFDLMKSGEC--IRTVI 364
PRK10083 PRK10083
putative oxidoreductase; Provisional
 6-355 8.07e-19

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 86.33  E-value: 8.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912    6 KAFVLRKKMDTAIEDRPGQTLTDDhQVKVAIKATGICGSDVHYWKegGIGDFIlKKPMILGHESAGVVVEVGKGVSSLKP 85
Cdd:PRK10083   2 KSIVIEKPNSLAIEERPIPQPAAG-EVRVKVKLAGICGSDSHIYR--GHNPFA-KYPRVIGHEFFGVIDAVGEGVDAARI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   86 GDPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATpPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRG 165
Cdd:PRK10083  78 GERVAVDPVISCGHCYPCSIGKPNVCTSLVVLGV-HRDGGFSEYAVVPAKNAHRIPDAIADQYAVMVEPFTIAANVTGRT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  166 NLKCGSRVLVMGCGTVGLLMMAVAK-AYGAIDIVAVDASPSRVEFAQKyVGAKpftPIAAKENESLPDyaqrykqAIIEK 244
Cdd:PRK10083 157 GPTEQDVALIYGAGPVGLTIVQVLKgVYNVKAVIVADRIDERLALAKE-SGAD---WVINNAQEPLGE-------ALEEK 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  245 YGEFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSfRYAHGCYKQSLFLVSNGLVDVK 324
Cdd:PRK10083 226 GIKPTLIIDAACHPSILEEAVTLASPAARIVLMGFSSEPSEIVQQGITGKELSIFSS-RLNANKFPVVIDWLSKGLIDPE 304

                        330       340       350
                 ....*....|....*....|....*....|.
gi 19111912  325 PLITHRFAFKDALKAYETVASGEEGVLKVII 355
Cdd:PRK10083 305 KLITHTFDFQHVADAIELFEKDQRHCCKVLL 335
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 31-355 1.03e-18

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: 86.12  E-value: 1.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  31 QVKVAIKATGICGSDVhywkegGIGDFILKKP------MILGHESaGVVVEVGKGVSSLKPGDPVA--VEPGCVcrLCDY 102
Cdd:cd08230  27 EVLVRTLEVGVCGTDR------EIVAGEYGTAppgedfLVLGHEA-LGVVEEVGDGSGLSPGDLVVptVRRPPG--KCLN 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 103 CRSGRYNLCPHMEF--AATPPYDGTLRTYYITTEDFCTKLPKQISvEEGALFEPMSVAVHAMTRGNLKC-------GSRV 173
Cdd:cd08230  98 CRIGRPDFCETGEYteRGIKGLHGFMREYFVDDPEYLVKVPPSLA-DVGVLLEPLSVVEKAIEQAEAVQkrlptwnPRRA 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 174 LVMGCGTVGLLMMAVAKAYGAIDIVA--VDASPSRVEFAQ----KYVGAKPfTPIAAKeneslpdyaqrykqaiiEKYGE 247
Cdd:cd08230 177 LVLGAGPIGLLAALLLRLRGFEVYVLnrRDPPDPKADIVEelgaTYVNSSK-TPVAEV-----------------KLVGE 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 248 FDFAVDATGVGICIHTAVLALKRGGTFVQAG--NGKPVIDFPINHIINY----EINVLGSFRYAHGCYKQSLFLVSNGLV 321
Cdd:cd08230 239 FDLIIEATGVPPLAFEALPALAPNGVVILFGvpGGGREFEVDGGELNRDlvlgNKALVGSVNANKRHFEQAVEDLAQWKY 318

                       330       340       350
                ....*....|....*....|....*....|....*...
gi 19111912 322 D----VKPLITHRFAFKDALKAYETvasGEEGVLKVII 355
Cdd:cd08230 319 RwpgvLERLITRRVPLEEFAEALTE---KPDGEIKVVI 353
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 18-347 6.45e-18

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: 83.27  E-value: 6.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  18 IEDRPGQTLTDdHQVKVAIKATGICGSDVHYWKegGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGcvc 97
Cdd:COG0604  17 LEEVPVPEPGP-GEVLVRVKAAGVNPADLLIRR--GLYPLPPGLPFIPGSDAAGVVVAVGEGVTGFKVGDRVAGLGR--- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  98 rlcdycrsgrynlcphmefaatppyDGTLRTYYITTEDFCTKLPKQISVEEGA-LFEPMSVAVHAM-TRGNLKCGSRVLV 175
Cdd:COG0604  91 -------------------------GGGYAEYVVVPADQLVPLPDGLSFEEAAaLPLAGLTAWQALfDRGRLKPGETVLV 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 176 MGC-GTVGLLMMAVAKAYGAiDIVAVDASPSRVEFAQKYvGAKPFtpIAAKEneslPDYAQRYKqAIIEKYGeFDFAVDA 254
Cdd:COG0604 146 HGAaGGVGSAAVQLAKALGA-RVIATASSPEKAELLRAL-GADHV--IDYRE----EDFAERVR-ALTGGRG-VDVVLDT 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 255 TGvGICIHTAVLALKRGGTFVQAGN-GKPVIDFPINHIINYEINVLGSFRYAHGCYK-----QSLF-LVSNGlvDVKPLI 327
Cdd:COG0604 216 VG-GDTLARSLRALAPGGRLVSIGAaSGAPPPLDLAPLLLKGLTLTGFTLFARDPAErraalAELArLLAAG--KLRPVI 292

                       330       340
                ....*....|....*....|
gi 19111912 328 THRFAFKDALKAYETVASGE 347
Cdd:COG0604 293 DRVFPLEEAAEAHRLLESGK 312
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 30-347 8.74e-18

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


Pssm-ID: 176261 [Multi-domain]  Cd Length: 369  Bit Score: 83.50  E-value: 8.74e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  30 HQVKVAIKATGICGSDVHYWK-EGGIGDFilkkPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRY 108
Cdd:cd08301  28 MEVRIKILHTSLCHTDVYFWEaKGQTPLF----PRILGHEAAGIVESVGEGVTDLKPGDHVLPVFTGECKECRHCKSEKS 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 109 NLCPHMEF---AATPPYDGTLR-----------------TYYITTEDFC-TKLPKQISVEEGALFE-PMSVAVHAMTR-G 165
Cdd:cd08301 104 NMCDLLRIntdRGVMINDGKSRfsingkpiyhfvgtstfSEYTVVHVGCvAKINPEAPLDKVCLLScGVSTGLGAAWNvA 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 166 NLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYvGAKPFTPIAakeneslpDYAQRYKQAIIEKY 245
Cdd:cd08301 184 KVKKGSTVAIFGLGAVGLAVAEGARIRGASRIIGVDLNPSKFEQAKKF-GVTEFVNPK--------DHDKPVQEVIAEMT 254

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 246 -GEFDFAVDATGVGICIHTAVLALKRG-GTFVQAGNGKPVIDFPInHIINY--EINVLGSFryaHGCYKQSL---FLVS- 317
Cdd:cd08301 255 gGGVDYSFECTGNIDAMISAFECVHDGwGVTVLLGVPHKDAVFST-HPMNLlnGRTLKGTL---FGGYKPKTdlpNLVEk 330

                       330       340       350
                ....*....|....*....|....*....|..
gi 19111912 318 --NGLVDVKPLITHRFAFKDALKAYETVASGE 347
Cdd:cd08301 331 ymKKELELEKFITHELPFSEINKAFDLLLKGE 362
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 6-346 1.00e-17

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: 82.61  E-value: 1.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLR---KKMDTAIEDRPGQTLTDDhQVKVAIKATGICGSDVHyWKEGGIGDFI-LKKPMILGHESAGVVVEVGKGVS 81
Cdd:cd05289   2 KAVRIHeygGPEVLELADVPTPEPGPG-EVLVKVHAAGVNPVDLK-IREGLLKAAFpLTLPLIPGHDVAGVVVAVGPGVT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  82 SLKPGDPVavepgcvcrlcdYCRSGrynlcphmefaatPPYDGTLRTYYITTEDFCTKLPKQISVEEGAlfepmSVAVHA 161
Cdd:cd05289  80 GFKVGDEV------------FGMTP-------------FTRGGAYAEYVVVPADELALKPANLSFEEAA-----ALPLAG 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 162 MT-------RGNLKCGSRVLVMG-CGTVGLLMMAVAKAYGAidIVAVDASPSRVEFAQKYvGAKPFTpiaakeneslpDY 233
Cdd:cd05289 130 LTawqalfeLGGLKAGQTVLIHGaAGGVGSFAVQLAKARGA--RVIATASAANADFLRSL-GADEVI-----------DY 195

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 234 -AQRYKQAIIEkyGEFDFAVDATGVGICIHTAVLaLKRGGTFVqagngkPVIDFPINHIINYEINVLGSFRYAHGCYKQ- 311
Cdd:cd05289 196 tKGDFERAAAP--GGVDAVLDTVGGETLARSLAL-VKPGGRLV------SIAGPPPAEQAAKRRGVRAGFVFVEPDGEQl 266

                       330       340       350
                ....*....|....*....|....*....|....*..
gi 19111912 312 -SLF-LVSNGLvdVKPLITHRFAFKDALKAYETVASG 346
Cdd:cd05289 267 aELAeLVEAGK--LRPVVDRVFPLEDAAEAHERLESG 301
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
181-318 1.51e-17

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 78.03  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   181 VGLLMMAVAKAYGAiDIVAVDASPSRVEFAQKYvGAKPFtpIAAKEneslPDYAQRYKqAIIEKYGeFDFAVDATGVGIC 260
Cdd:pfam00107   2 VGLAAIQLAKAAGA-KVIAVDGSEEKLELAKEL-GADHV--INPKE----TDLVEEIK-ELTGGKG-VDVVFDCVGSPAT 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19111912   261 IHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAHGCYKQSLFLVSN 318
Cdd:pfam00107  72 LEQALKLLRPGGRVVVVGLPGGPLPLPLAPLLLKELTILGSFLGSPEEFPEALDLLAS 129
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
 6-216 1.55e-17

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: 82.36  E-value: 1.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLTDDHQVKVAIKATGICGSDVHYWKegGIGDFILKKPMilGHESAGVVVEVGKGVSSLKP 85
Cdd:cd08287   2 RATVIHGPGDIRVEEVPDPVIEEPTDAVIRVVATCVCGSDLWPYR--GVSPTRAPAPI--GHEFVGVVEEVGSEVTSVKP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  86 GDPVaVEPGCV-CRLCDYCRSGRYNLCPHMEFAAT------------PPYDGTLrtyyittedfcTKLPKQISVEEG--- 149
Cdd:cd08287  78 GDFV-IAPFAIsDGTCPFCRAGFTTSCVHGGFWGAfvdggqgeyvrvPLADGTL-----------VKVPGSPSDDEDllp 145

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 150 ---ALFEPMSVAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYvGA 216
Cdd:cd08287 146 sllALSDVMGTGHHAAVSAGVRPGSTVVVVGDGAVGLCAVLAAKRLGAERIIAMSRHEDRQALAREF-GA 214
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 30-278 3.03e-17

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


Pssm-ID: 176202 [Multi-domain]  Cd Length: 350  Bit Score: 81.89  E-value: 3.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  30 HQVKVAIKATGICGSDVHYWkEGGI---GDFILKK-------PMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRL 99
Cdd:cd08240  26 TEVLVKVTACGVCHSDLHIW-DGGYdlgGGKTMSLddrgvklPLVLGHEIVGEVVAVGPDAADVKVGDKVLVYPWIGCGE 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 100 CDYCRSGRYNLCPHMEFAATPPyDGTLRTYYITTEDFCTKLPKQISVEEGALFePMS--VAVHAMTRGNLKCGSR-VLVM 176
Cdd:cd08240 105 CPVCLAGDENLCAKGRALGIFQ-DGGYAEYVIVPHSRYLVDPGGLDPALAATL-ACSglTAYSAVKKLMPLVADEpVVII 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 177 GCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYvGAkpftpiAAKENESLPDYAQRykqaIIEKY-GEFDFAVDAT 255
Cdd:cd08240 183 GAGGLGLMALALLKALGPANIIVVDIDEAKLEAAKAA-GA------DVVVNGSDPDAAKR----IIKAAgGGVDAVIDFV 251

                       250       260
                ....*....|....*....|...
gi 19111912 256 GVGICIHTAVLALKRGGTFVQAG 278
Cdd:cd08240 252 NNSATASLAFDILAKGGKLVLVG 274
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
 30-256 4.71e-15

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: 75.34  E-value: 4.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  30 HQVKVAIKATGICGSDVHYWkeGGI---GDFilkkPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSG 106
Cdd:cd08300  28 GEVRIKILATGVCHTDAYTL--SGAdpeGLF----PVILGHEGAGIVESVGEGVTSVKPGDHVIPLYTPECGECKFCKSG 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 107 RYNLCPHMEfaAT------PpyDGTLR--------TYYITTEDFC--TKLPkQISV---EEGALFEPMSVAVHAMTRG-- 165
Cdd:cd08300 102 KTNLCQKIR--ATqgkglmP--DGTSRfsckgkpiYHFMGTSTFSeyTVVA-EISVakiNPEAPLDKVCLLGCGVTTGyg 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 166 ------NLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYvGAKPFTpiaakeNESlpDYAQRYKQ 239
Cdd:cd08300 177 avlntaKVEPGSTVAVFGLGAVGLAVIQGAKAAGASRIIGIDINPDKFELAKKF-GATDCV------NPK--DHDKPIQQ 247

                       250
                ....*....|....*...
gi 19111912 240 AIIEKY-GEFDFAVDATG 256
Cdd:cd08300 248 VLVEMTdGGVDYTFECIG 265
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 29-346 9.92e-15

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: 74.17  E-value: 9.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  29 DHQVKVAIKATGICGSDVHYWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVavepgcvcrlcdycrsgrY 108
Cdd:cd08267  26 PGEVLVKVHAASVNPVDWKLRRGPPKLLLGRPFPPIPGMDFAGEVVAVGSGVTRFKVGDEV------------------F 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 109 NLCPHMEFaatppydGTLRTYYITTEDFCTKLPKQISVEEGAlfepmSVAVHAMT-------RGNLKCGSRVLVMGC-GT 180
Cdd:cd08267  88 GRLPPKGG-------GALAEYVVAPESGLAKKPEGVSFEEAA-----ALPVAGLTalqalrdAGKVKPGQRVLINGAsGG 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 181 VGLLMMAVAKAYGAIdIVAVdASPSRVEFAqKYVGAkpftpiaakeneslpDYAQRYKQ--AIIEKYGE--FDFAVDATG 256
Cdd:cd08267 156 VGTFAVQIAKALGAH-VTGV-CSTRNAELV-RSLGA---------------DEVIDYTTedFVALTAGGekYDVIFDAVG 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 257 -VGICIHTAVLALKRGGTFVQAGNGKPVIDFPinHIINYEINVLGSFRYahgcykqSLFLVSNGLVD------------V 323
Cdd:cd08267 218 nSPFSLYRASLALKPGGRYVSVGGGPSGLLLV--LLLLPLTLGGGGRRL-------KFFLAKPNAEDleqlaelveegkL 288

                       330       340
                ....*....|....*....|...
gi 19111912 324 KPLITHRFAFKDALKAYETVASG 346
Cdd:cd08267 289 KPVIDSVYPLEDAPEAYRRLKSG 311
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
 6-301 1.99e-14

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 73.14  E-value: 1.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912    6 KAFVLRKKMDT-AIEDRPGQTLTDDhQVKVAIKATGICGSDVHYwKEGGIGDfilKKPMILGHESAGVVVEVGKGVSSLK 84
Cdd:PRK09422   2 KAAVVNKDHTGdVVVEKTLRPLKHG-EALVKMEYCGVCHTDLHV-ANGDFGD---KTGRILGHEGIGIVKEVGPGVTSLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   85 PGDPVAVE---PGCVCrlCDYCRSGRYNLCPHMEFAAtppY--DGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAV 159
Cdd:PRK09422  77 VGDRVSIAwffEGCGH--CEYCTTGRETLCRSVKNAG---YtvDGGMAEQCIVTADYAVKVPEGLDPAQASSITCAGVTT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  160 H-AMTRGNLKCGSRVLVMGCGTVGLLMMAVAK-AYGAiDIVAVDASPSRVEFAqKYVGAKpfTPIAAKENESLPDYAQry 237
Cdd:PRK09422 152 YkAIKVSGIKPGQWIAIYGAGGLGNLALQYAKnVFNA-KVIAVDINDDKLALA-KEVGAD--LTINSKRVEDVAKIIQ-- 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19111912  238 kqaiiEKYGEFDFAVdATGVG-ICIHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGS 301
Cdd:PRK09422 226 -----EKTGGAHAAV-VTAVAkAAFNQAVDAVRAGGRVVAVGLPPESMDLSIPRLVLDGIEVVGS 284
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
 30-346 3.69e-14

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: 72.73  E-value: 3.69e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  30 HQVKVAIKATGICGSDVHYWKeggiGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAvePGCV--CRLCDYCRSGR 107
Cdd:cd08299  33 HEVRIKIVATGICRSDDHVVS----GKLVTPFPVILGHEAAGIVESVGEGVTTVKPGDKVI--PLFVpqCGKCRACLNPE 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 108 YNLCphMEFAATPP----YDGTLR--------TYYITTEDFC--TKLpKQISV---EEGALFEpmSVAV----------H 160
Cdd:cd08299 107 SNLC--LKNDLGKPqglmQDGTSRftckgkpiHHFLGTSTFSeyTVV-DEIAVakiDAAAPLE--KVCLigcgfstgygA 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 161 AMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAqKYVGakpftpiaAKENESLPDYAQRYKQA 240
Cdd:cd08299 182 AVNTAKVTPGSTCAVFGLGGVGLSAIMGCKAAGASRIIAVDINKDKFAKA-KELG--------ATECINPQDYKKPIQEV 252

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 241 IIEKYGE-FDFAVDATGVGICIHTAVLALKRG-GTFVQAGNGKPVIDFPINHII-----NYEINVLGSFRYAHGCYKqsl 313
Cdd:cd08299 253 LTEMTDGgVDFSFEVIGRLDTMKAALASCHEGyGVSVIVGVPPSSQNLSINPMLlltgrTWKGAVFGGWKSKDSVPK--- 329

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 19111912 314 fLVS---NGLVDVKPLITHRFAFKDALKAYETVASG 346
Cdd:cd08299 330 -LVAdymAKKFNLDPLITHTLPFEKINEGFDLLRSG 364
PLN02740 PLN02740
Alcohol dehydrogenase-like
 31-347 2.68e-12

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 67.13  E-value: 2.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   31 QVKVAIKATGICGSDVHYWKegGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRYNL 110
Cdd:PLN02740  37 EVRIKILYTSICHTDLSAWK--GENEAQRAYPRILGHEAAGIVESVGEGVEDLKAGDHVIPIFNGECGDCRYCKRDKTNL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  111 CPHME---FAATPPYDGTLR----------TYYITTEDFC--TKLPKQ--ISVEEGALFEPMSVAVHAMTRG-------- 165
Cdd:PLN02740 115 CETYRvdpFKSVMVNDGKTRfstkgdgqpiYHFLNTSTFTeyTVLDSAcvVKIDPNAPLKKMSLLSCGVSTGvgaawnta 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  166 NLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAqKYVGAKPFtpIAAKENEslpdyaQRYKQAIIE-K 244
Cdd:PLN02740 195 NVQAGSSVAIFGLGAVGLAVAEGARARGASKIIGVDINPEKFEKG-KEMGITDF--INPKDSD------KPVHERIREmT 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  245 YGEFDFAVDATGVGICIHTAVLALKRG-GTFVQAG-NGKPVIdFPINHIINYE-----INVLGSFRYAhgcyKQSLFLVS 317
Cdd:PLN02740 266 GGGVDYSFECAGNVEVLREAFLSTHDGwGLTVLLGiHPTPKM-LPLHPMELFDgrsitGSVFGDFKGK----SQLPNLAK 340

                        330       340       350
                 ....*....|....*....|....*....|...
gi 19111912  318 ---NGLVDVKPLITHRFAFKDALKAYETVASGE 347
Cdd:PLN02740 341 qcmQGVVNLDGFITHELPFEKINEAFQLLEDGK 373
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
 29-288 8.55e-12

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 65.67  E-value: 8.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   29 DHQVKVAIKATGICGSDVHYWK-EGGIGDFilkkPMILGHESAGVVVEVGKGVSSLKPGDPVAVepGCV---CRLCDYCR 104
Cdd:PLN02586  37 DEDVTVKILYCGVCHSDLHTIKnEWGFTRY----PIVPGHEIVGIVTKLGKNVKKFKEGDRVGV--GVIvgsCKSCESCD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  105 SGRYNLCPHMEFAATPPY-DGTlRTY------YITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTR--GNLKCGSRVLV 175
Cdd:PLN02586 111 QDLENYCPKMIFTYNSIGhDGT-KNYggysdmIVVDQHFVLRFPDNLPLDAGAPLLCAGITVYSPMKyyGMTEPGKHLGV 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  176 MGCGTVGLLMMAVAKAYGaIDIVAVDASPSRVEFAQKYVGAKPFTpiaakenesLPDYAQRYKQAIiekyGEFDFAVDAT 255
Cdd:PLN02586 190 AGLGGLGHVAVKIGKAFG-LKVTVISSSSNKEDEAINRLGADSFL---------VSTDPEKMKAAI----GTMDYIIDTV 255

                        250       260       270
                 ....*....|....*....|....*....|...
gi 19111912  256 GVGICIHTAVLALKRGGTFVQAGNGKPVIDFPI 288
Cdd:PLN02586 256 SAVHALGPLLGLLKVNGKLITLGLPEKPLELPI 288
adh_fam_2 TIGR02822
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
 21-278 2.48e-11

zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct subset of the larger family of oxidoreductases that includes zinc-binding alcohol dehydrogenases and NADPH:quinone reductases (pfam00107). The gene neighborhood of members of this family is not conserved and it appears that no members are characterized. The sequence of the family includes 6 invariant cysteine residues and one invariant histidine. It appears that no member is characterized. [Energy metabolism, Fermentation]


Pssm-ID: 131869 [Multi-domain]  Cd Length: 329  Bit Score: 64.17  E-value: 2.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912    21 RPGQTltddhQVKVAIKATGICGSDVHYWKeggiGDFILKKPMIL-GHESAGVVVEVGKGVSSLKPGDPVAVE-PGCVCR 98
Cdd:TIGR02822  24 RPGPG-----ELLVRVRACGVCRTDLHVSE----GDLPVHRPRVTpGHEVVGEVAGRGADAGGFAVGDRVGIAwLRRTCG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912    99 LCDYCRSGRYNLCPHMEFAATPPyDGTLRTYYITTEDFCTKLPKQISVEEGA-LFEPMSVAVHAMTRGNLKCGSRVLVMG 177
Cdd:TIGR02822  95 VCRYCRRGAENLCPASRYTGWDT-DGGYAEYTTVPAAFAYRLPTGYDDVELApLLCAGIIGYRALLRASLPPGGRLGLYG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   178 CGTVGLLMMAVAKAYGA-IDIVAVDASPSRVEFAqkyVGAKPFTPIAAKENESLpdyaqrykqaiiekygefDFAVDATG 256
Cdd:TIGR02822 174 FGGSAHLTAQVALAQGAtVHVMTRGAAARRLALA---LGAASAGGAYDTPPEPL------------------DAAILFAP 232

                         250       260
                  ....*....|....*....|..
gi 19111912   257 VGICIHTAVLALKRGGTFVQAG 278
Cdd:TIGR02822 233 AGGLVPPALEALDRGGVLAVAG 254
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 30-216 4.30e-11

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: 63.42  E-value: 4.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  30 HQVKVAIKATGICGSDVHYwKEGGIGDfiLKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVE-PGCVCRLCDYCRSGRY 108
Cdd:cd08296  26 GEVLIKVEACGVCHSDAFV-KEGAMPG--LSYPRVPGHEVVGRIDAVGEGVSRWKVGDRVGVGwHGGHCGTCDACRRGDF 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 109 NLCPHMEFAATpPYDGTLRTYYITTEDFCTKLPKQISVEEGAlfePM---SVAV-HAMTRGNLKCGSRVLVMGCGTVGLL 184
Cdd:cd08296 103 VHCENGKVTGV-TRDGGYAEYMLAPAEALARIPDDLDAAEAA---PLlcaGVTTfNALRNSGAKPGDLVAVQGIGGLGHL 178

                       170       180       190
                ....*....|....*....|....*....|..
gi 19111912 185 MMAVAKAYGaIDIVAVDASPSRVEFAQKyVGA 216
Cdd:cd08296 179 AVQYAAKMG-FRTVAISRGSDKADLARK-LGA 208
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 124-355 2.16e-09

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: 57.98  E-value: 2.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 124 GTLRTYYITTEDFCTKLPKQISVEEGAlfepmSVAVHAMT-------RGNLKCGSRVLVMG-CGTVGLLMMAVAKAYGAi 195
Cdd:cd08253  97 GTAAEYVVVPADQLVPLPDGVSFEQGA-----ALGIPALTayralfhRAGAKAGETVLVHGgSGAVGHAAVQLARWAGA- 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 196 DIVAVDASPSRVEFAQKyVGAkpftpiAAKENESLPDYAQRYKQA--------IIEKYGEFDFAVDATgvgicihtavlA 267
Cdd:cd08253 171 RVIATASSAEGAELVRQ-AGA------DAVFNYRAEDLADRILAAtagqgvdvIIEVLANVNLAKDLD-----------V 232

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 268 LKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAHGCYKQSLFL--VSNGLVD--VKPLITHRFAFKDALKAYETV 343
Cdd:cd08253 233 LAPGGRIVVYGSGGLRGTIPINPLMAKEASIRGVLLYTATPEERAAAAeaIAAGLADgaLRPVIAREYPLEEAAAAHEAV 312

                       250
                ....*....|...
gi 19111912 344 -ASGEEGvlKVII 355
Cdd:cd08253 313 eSGGAIG--KVVL 323
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 30-212 4.18e-09

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: 56.81  E-value: 4.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  30 HQVKVAIKATGICGSDVHYWKEGGIGDfilkkPMILGHESAGVVVEVGKGVSSLKPGDPV-AVEPGCvcrlcdycrsgry 108
Cdd:cd05195   1 DEVEVEVKAAGLNFRDVLVALGLLPGD-----ETPLGLECSGIVTRVGSGVTGLKVGDRVmGLAPGA------------- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 109 nlcphmefaatppydgtLRTYYITTEDFCTKLPKQISVEEGALFePMSV--AVHAM-TRGNLKCGSRVLVM-GCGTVGLL 184
Cdd:cd05195  63 -----------------FATHVRVDARLVVKIPDSLSFEEAATL-PVAYltAYYALvDLARLQKGESVLIHaAAGGVGQA 124

                       170       180
                ....*....|....*....|....*...
gi 19111912 185 MMAVAKAYGAIDIVAVDaSPSRVEFAQK 212
Cdd:cd05195 125 AIQLAQHLGAEVFATVG-SEEKREFLRE 151
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 6-355 8.48e-09

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: 56.35  E-value: 8.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRK---KMDTAIED---RPGQtltdDHQVKVAIKATGICGSDV------HYWKeggigdfiLKKPMILGHESAGVV 73
Cdd:cd08241   2 KAVVCKElggPEDLVLEEvppEPGA----PGEVRIRVEAAGVNFPDLlmiqgkYQVK--------PPLPFVPGSEVAGVV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  74 VEVGKGVSSLKPGDPVAVepgcvcrlcdycrsgrynLCPHmefaatppydGTLRTYYITTEDFCTKLPKQISVEEGALFe 153
Cdd:cd08241  70 EAVGEGVTGFKVGDRVVA------------------LTGQ----------GGFAEEVVVPAAAVFPLPDGLSFEEAAAL- 120

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 154 PMS--VAVHAMT-RGNLKCGSRVLVMGC-GTVGLlmMAV--AKAYGAIdIVAVDASPSRVEFAQKYvGAkpftpiAAKEN 227
Cdd:cd08241 121 PVTygTAYHALVrRARLQPGETVLVLGAaGGVGL--AAVqlAKALGAR-VIAAASSEEKLALARAL-GA------DHVID 190

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 228 ESLPDYAQRYKqAIIEKYGeFDFAVDATGvGICIHTAVLALKRGGTFVqagngkpVIDF--------PINHIINYEINVL 299
Cdd:cd08241 191 YRDPDLRERVK-ALTGGRG-VDVVYDPVG-GDVFEASLRSLAWGGRLL-------VIGFasgeipqiPANLLLLKNISVV 260

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19111912 300 GSF---------RYAHGCYKQSLFLVSNGLvdVKPLITHRFAFKDALKAYETVASGeEGVLKVII 355
Cdd:cd08241 261 GVYwgayarrepELLRANLAELFDLLAEGK--IRPHVSAVFPLEQAAEALRALADR-KATGKVVL 322
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 31-347 1.25e-08

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


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 55.68  E-value: 1.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  31 QVKVAIKATGICGSDVhYWKEGG-IGDFILkkPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVcrlcdycrSGRYn 109
Cdd:cd08268  29 EVLIRVEAIGLNRADA-MFRRGAyIEPPPL--PARLGYEAAGVVEAVGAGVTGFAVGDRVSVIPAAD--------LGQY- 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 110 lcphmefaatppydGTLRTYYITTEDFCTKLPKQIS-VEEGALFEPMSVAVHAMTR-GNLKCGSRVLVMGC-GTVGLLMM 186
Cdd:cd08268  97 --------------GTYAEYALVPAAAVVKLPDGLSfVEAAALWMQYLTAYGALVElAGLRPGDSVLITAAsSSVGLAAI 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 187 AVAKAYGAIDIvAVDASPSRVEFAQKYvGAkpfTPIAAKENESLPDYAQRykqaIIEKYGeFDFAVDATG---VGICIHt 263
Cdd:cd08268 163 QIANAAGATVI-ATTRTSEKRDALLAL-GA---AHVIVTDEEDLVAEVLR----ITGGKG-VDVVFDPVGgpqFAKLAD- 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 264 avlALKRGGTFVQAGN-GKPVIDFPI-NHIINY---EINVLGSFRYAHGCYKQSLFLVSNGLVD--VKPLITHRFAFKDA 336
Cdd:cd08268 232 ---ALAPGGTLVVYGAlSGEPTPFPLkAALKKSltfRGYSLDEITLDPEARRRAIAFILDGLASgaLKPVVDRVFPFDDI 308

                       330
                ....*....|.
gi 19111912 337 LKAYETVASGE 347
Cdd:cd08268 309 VEAHRYLESGQ 319
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 29-347 2.36e-08

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: 55.05  E-value: 2.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  29 DHQVKVAIKATGIcgSDVHYWkeggIGDFILKKPM--ILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSG 106
Cdd:cd08264  26 PGEVLIRVKMAGV--NPVDYN----VINAVKVKPMphIPGAEFAGVVEEVGDHVKGVKKGDRVVVYNRVFDGTCDMCLSG 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 107 RYNLCPH---MEFAAtppyDGTLRTYYITTEDFCTKLPKQISVEEGAlfePMSVAV----HAMTRGNLKCGSRVLVMGC- 178
Cdd:cd08264 100 NEMLCRNggiIGVVS----NGGYAEYIVVPEKNLFKIPDSISDELAA---SLPVAAltayHALKTAGLGPGETVVVFGAs 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 179 GTVGLLMMAVAKAYGAiDIVAVdaspSRVEFAQKYvgakpftpiAAKENESLPDYAQRYKqaiiEKYGEFDFAVDATGVG 258
Cdd:cd08264 173 GNTGIFAVQLAKMMGA-EVIAV----SRKDWLKEF---------GADEVVDYDEVEEKVK----EITKMADVVINSLGSS 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 259 IcIHTAVLALKRGGTFVQAG--NGKPV-IDfpINHIINYEINVLGSFRyahGCYKQSLFLVSNgLVDVKPLITHRFAFKD 335
Cdd:cd08264 235 F-WDLSLSVLGRGGRLVTFGtlTGGEVkLD--LSDLYSKQISIIGSTG---GTRKELLELVKI-AKDLKVKVWKTFKLEE 307

                       330
                ....*....|..
gi 19111912 336 ALKAYETVASGE 347
Cdd:cd08264 308 AKEALKELFSKE 319
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 120-346 1.13e-07

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


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 52.92  E-value: 1.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 120 PPYDGTLRTYYITTEDFCTKLPKQISVEEGALFepmsvAVHAMT-------RGNLKCGSRVLVMGCGTVGLLMMAVAKAY 192
Cdd:cd08276 109 GPIDGVLAEYVVLPEEGLVRAPDHLSFEEAATL-----PCAGLTawnalfgLGPLKPGDTVLVQGTGGVSLFALQFAKAA 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 193 GAIDIvAVDASPSRVEFAQKyVGAKpfTPIAAKENeslPDYAQRyKQAIIEKYGeFDFAVDATGVGicihT---AVLALK 269
Cdd:cd08276 184 GARVI-ATSSSDEKLERAKA-LGAD--HVINYRTT---PDWGEE-VLKLTGGRG-VDHVVEVGGPG----TlaqSIKAVA 250

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 270 RGGTF----VQAGNGKPVIDFPI--NHIINYEINVlGSfryahgcykQSLFLVSNGLVD---VKPLITHRFAFKDALKAY 340
Cdd:cd08276 251 PGGVIsligFLSGFEAPVLLLPLltKGATLRGIAV-GS---------RAQFEAMNRAIEahrIRPVIDRVFPFEEAKEAY 320


                ....*.
gi 19111912 341 ETVASG 346
Cdd:cd08276 321 RYLESG 326
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
 29-288 1.68e-07

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 52.33  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   29 DHQVKVAIKATGICGSDVHYWKEG-GIGDFilkkPMILGHESAGVVVEVGKGVSSLKPGDPVAVepGCV---CRLCDYCR 104
Cdd:PLN02178  31 ENDVTVKILFCGVCHSDLHTIKNHwGFSRY----PIIPGHEIVGIATKVGKNVTKFKEGDRVGV--GVIigsCQSCESCN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  105 SGRYNLCPHMEFA-ATPPYDGT-----LRTYYITTEDFCTKLPKQISVEEGA--------LFEPMSvaVHAMTRgnlKCG 170
Cdd:PLN02178 105 QDLENYCPKVVFTyNSRSSDGTrnqggYSDVIVVDHRFVLSIPDGLPSDSGApllcagitVYSPMK--YYGMTK---ESG 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  171 SRVLVMGCGTVGLLMMAVAKAYGaIDIVAVDASPSRVEFAQKYVGAKPFTpiaakenesLPDYAQRYKQAIiekyGEFDF 250
Cdd:PLN02178 180 KRLGVNGLGGLGHIAVKIGKAFG-LRVTVISRSSEKEREAIDRLGADSFL---------VTTDSQKMKEAV----GTMDF 245

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 19111912  251 AVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPI 288
Cdd:PLN02178 246 IIDTVSAEHALLPLFSLLKVSGKLVALGLPEKPLDLPI 283
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
 34-219 2.03e-07

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 52.11  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   34 VAIKAT--GICGSDVHYWK-EGGIGDFilkkPMILGHESAGVVVEVGKGVSSLKPGDPVAVepGCV---CRLCDYCRSGR 107
Cdd:PLN02514  37 VVIKVIycGICHTDLHQIKnDLGMSNY----PMVPGHEVVGEVVEVGSDVSKFTVGDIVGV--GVIvgcCGECSPCKSDL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  108 YNLCPHMEFAAT------PPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTR--GNLKCGSRVLVMGCG 179
Cdd:PLN02514 111 EQYCNKRIWSYNdvytdgKPTQGGFASAMVVDQKFVVKIPEGMAPEQAAPLLCAGVTVYSPLShfGLKQSGLRGGILGLG 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19111912  180 TVGLLMMAVAKAYGAiDIVAVDASPSRVEFAQKYVGAKPF 219
Cdd:PLN02514 191 GVGHMGVKIAKAMGH-HVTVISSSDKKREEALEHLGADDY 229
PLN02827 PLN02827
Alcohol dehydrogenase-like
 31-213 2.73e-07

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 51.83  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   31 QVKVAIKATGICGSDVHYWKEGGIgdfilkKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRYNL 110
Cdd:PLN02827  39 EIRIKVVSTSLCRSDLSAWESQAL------FPRIFGHEASGIVESIGEGVTEFEKGDHVLTVFTGECGSCRHCISGKSNM 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  111 CP----------HMEFAATPPYDGTLRTYYITTEDFC--TKLPKQISVEEGALfEPM------SVAVHA-----MTRGNL 167
Cdd:PLN02827 113 CQvlglerkgvmHSDQKTRFSIKGKPVYHYCAVSSFSeyTVVHSGCAVKVDPL-APLhkicllSCGVAAglgaaWNVADV 191

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 19111912  168 KCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKY 213
Cdd:PLN02827 192 SKGSSVVIFGLGTVGLSVAQGAKLRGASQIIGVDINPEKAEKAKTF 237
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 6-275 4.14e-07

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


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 51.05  E-value: 4.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDT---AIEDRPGQTLTDDhQVKVAIKATGICGSDVhYWKEGGIGDFIlKKPMILGHESAGVVVEVGKGVSS 82
Cdd:cd08275   1 RAVVLTGFGGLdklKVEKEALPEPSSG-EVRVRVEACGLNFADL-MARQGLYDSAP-KPPFVPGFECAGTVEAVGEGVKD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  83 LKPGDPVAVepgcvcrlcdYCRSGRYnlcphmefaatppydgtlRTYYITTEDFCTKLPKQISVEEGALFePMS-----V 157
Cdd:cd08275  78 FKVGDRVMG----------LTRFGGY------------------AEVVNVPADQVFPLPDGMSFEEAAAF-PVNyltayY 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 158 AVHAMtrGNLKCGSRVLV-MGCGTVGLLMMAVAKAYGAIDIVAvDASPSRVEfaqkyvgakpftpiAAKEN--ESLPDY- 233
Cdd:cd08275 129 ALFEL--GNLRPGQSVLVhSAAGGVGLAAGQLCKTVPNVTVVG-TASASKHE--------------ALKENgvTHVIDYr 191

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 19111912 234 AQRYKQAIIEKYGE-FDFAVDATGvGICIHTAVLALKRGGTFV 275
Cdd:cd08275 192 TQDYVEEVKKISPEgVDIVLDALG-GEDTRKSYDLLKPMGRLV 233
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 6-275 8.10e-07

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: 50.27  E-value: 8.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLT-DDHQVKVAIKATGICGSDvhyWK--EGGigdFILKKPMILGHESAGVVVEVGKGVSS 82
Cdd:cd08249   2 KAAVLTGPGGGLLVVVDVPVPKpGPDEVLVKVKAVALNPVD---WKhqDYG---FIPSYPAILGCDFAGTVVEVGSGVTR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  83 LKPGDPVAVepgcvcrlcdYCRSGRYNlcphmefaatPPYDGTLRTYYITTEDFCTKLPKQISVEEGA------------ 150
Cdd:cd08249  76 FKVGDRVAG----------FVHGGNPN----------DPRNGAFQEYVVADADLTAKIPDNISFEEAAtlpvglvtaala 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 151 LFEPMSVAVHAMTRGNLKCGSRVLVMGCGT-VGLLMMAVAKAYGaIDIVAVdASPSRVEFAQKYvGA-KPFtpiaakene 228
Cdd:cd08249 136 LFQKLGLPLPPPKPSPASKGKPVLIWGGSSsVGTLAIQLAKLAG-YKVITT-ASPKNFDLVKSL-GAdAVF--------- 203

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 19111912 229 slpDY--AQRYKQAIIEKYGEFDFAVDATGVG----ICihTAVLALKRGGTFV 275
Cdd:cd08249 204 ---DYhdPDVVEDIRAATGGKLRYALDCISTPesaqLC--AEALGRSGGGKLV 251
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 62-346 8.92e-07

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: 50.30  E-value: 8.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  62 PMILGHESAGVVVEVGKGVSSLKPGDPVavepgcvcrlcdycrsgrynlcphmeFAATPPYD-GTLRTYYITTEDFCTKL 140
Cdd:cd08248  74 PLTLGRDCSGVVVDIGSGVKSFEIGDEV--------------------------WGAVPPWSqGTHAEYVVVPENEVSKK 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 141 PKQISVEEGAlfepmSVAVHAMT-------RGNL----KCGSRVLVMG-CGTVGLLMMAVAKAYGAidIVAVDASPSRVE 208
Cdd:cd08248 128 PKNLSHEEAA-----SLPYAGLTawsalvnVGGLnpknAAGKRVLILGgSGGVGTFAIQLLKAWGA--HVTTTCSTDAIP 200

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 209 FAqKYVGAK---PFTPIAAKENeslpdyaqrykqaiIEKYGEFDFAVDATGVGICIHtAVLALKRGGTFVQAGNgkPV-- 283
Cdd:cd08248 201 LV-KSLGADdviDYNNEDFEEE--------------LTERGKFDVILDTVGGDTEKW-ALKLLKKGGTYVTLVS--PLlk 262

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 284 -IDFP-------INHIINYEINVLGSFRyaHGCYKQSLFLVS-------NGLVD---VKPLITHRFAFKDALKAYETVAS 345
Cdd:cd08248 263 nTDKLglvggmlKSAVDLLKKNVKSLLK--GSHYRWGFFSPSgsaldelAKLVEdgkIKPVIDKVFPFEEVPEAYEKVES 340


                .
gi 19111912 346 G 346
Cdd:cd08248 341 G 341
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 160-212 1.48e-06

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 47.62  E-value: 1.48e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 19111912 160 HAMTRGNLKCGSRVLVMGCGTvGLLMMAVAKAYGAiDIVAVDASPSRVEFAQK 212
Cdd:COG2230  42 LILRKLGLKPGMRVLDIGCGW-GGLALYLARRYGV-RVTGVTLSPEQLEYARE 92
sorbose_phosphate_red cd08238
L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, ...
 6-227 1.57e-06

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: 49.75  E-value: 1.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   6 KAFVLRKKMDTAIEDRPGQTLTDDhQVKVAIKATGICGSDVHYWKEGG----IGDFILKKPMILGHESAGVVVEVGKG-V 80
Cdd:cd08238   4 KAWRMYGKGDLRLEKFELPEIADD-EILVRVISDSLCFSTWKLALQGSdhkkVPNDLAKEPVILGHEFAGTILKVGKKwQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  81 SSLKPGDPVAVEPGCvcrlcdYCRSGRYnlCPHMEFaatpPYDGTLRTYYITTEDF----CTKLPKQISVEEGALFEPMS 156
Cdd:cd08238  83 GKYKPGQRFVIQPAL------ILPDGPS--CPGYSY----TYPGGLATYHIIPNEVmeqdCLLIYEGDGYAEASLVEPLS 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 157 VAVHAMT------------RGNLKCGSRVLVMGC-GTVGLlmMAVAKA-YGAID---IVAVDASPSRVEFAQKYvgakpF 219
Cdd:cd08238 151 CVIGAYTanyhlqpgeyrhRMGIKPGGNTAILGGaGPMGL--MAIDYAiHGPIGpslLVVTDVNDERLARAQRL-----F 223


                ....*...
gi 19111912 220 TPIAAKEN 227
Cdd:cd08238 224 PPEAASRG 231
ribitol-5-phosphate_DH cd08237
ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of ...
 41-212 3.68e-06

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: 48.13  E-value: 3.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  41 ICGSDVHYWKeGGIGDFILKK--PMILGHESagVVVEVGKGVSSLKPGDPVAVEPgCVCRLCD------YCRSGRYnlcp 112
Cdd:cd08237  37 ICHADQRYYQ-GNRSPEALKKklPMALIHEG--IGVVVSDPTGTYKVGTKVVMVP-NTPVEKDeiipenYLPSSRF---- 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 113 hmefaATPPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRGN---LKCGSRVLVMGCGTVGLLM-MAV 188
Cdd:cd08237 109 -----RSSGYDGFMQDYVFLPPDRLVKLPDNVDPEVAAFTELVSVGVHAISRFEqiaHKDRNVIGVWGDGNLGYITaLLL 183

                       170       180
                ....*....|....*....|....*..
gi 19111912 189 AKAYGAIDIVAVDASPSRVE---FAQK 212
Cdd:cd08237 184 KQIYPESKLVVFGKHQEKLDlfsFADE 210
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 31-275 8.90e-06

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 46.78  E-value: 8.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  31 QVKVAIKATGIcgSDVHYWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAvepgcvcrlcdYCRSGrynl 110
Cdd:cd08272  29 QVLVRVHASGV--NPLDTKIRRGGAAARPPLPAILGCDVAGVVEAVGEGVTRFRVGDEVY-----------GCAGG---- 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 111 cphmeFAATPpydGTLRTYYITTEDFCTKLPKQISVEEGALFePMsVAVHAM----TRGNLKCGSRVLVM-GCGTVGLLM 185
Cdd:cd08272  92 -----LGGLQ---GSLAEYAVVDARLLALKPANLSMREAAAL-PL-VGITAWeglvDRAAVQAGQTVLIHgGAGGVGHVA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 186 MAVAKAYGAidIVAVDASPSRVEFAQKYvGAkpfTPIAakeneslpDYAQRYKQAIIEKYGE--FDFAVDATGvGICIHT 263
Cdd:cd08272 162 VQLAKAAGA--RVYATASSEKAAFARSL-GA---DPII--------YYRETVVEYVAEHTGGrgFDVVFDTVG-GETLDA 226

                       250
                ....*....|..
gi 19111912 264 AVLALKRGGTFV 275
Cdd:cd08272 227 SFEAVALYGRVV 238
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
 64-355 1.78e-05

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: 46.26  E-value: 1.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  64 ILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATPPYDGTLRTYYITTEDFCTKLPKQ 143
Cdd:cd08246  84 IGGSDASGIVWAVGEGVKNWKVGDEVVVHCSVWDGNDPERAGGDPMFDPSQRIWGYETNYGSFAQFALVQATQLMPKPKH 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 144 ISVEEGALFEPMSVAVHAMTRG----NLKCGSRVLVMGcGTVGLLMMAV--AKAYGAIDiVAVDASPSRVEFAQK----- 212
Cdd:cd08246 164 LSWEEAAAYMLVGATAYRMLFGwnpnTVKPGDNVLIWG-ASGGLGSMAIqlARAAGANP-VAVVSSEEKAEYCRAlgaeg 241

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 213 --------YVGAKPftPIAAKENESLPDYAQRYKQAIIEKYGE-------FDFAVDATgvgicIHTAVLALKRGGTFVQ- 276
Cdd:cd08246 242 vinrrdfdHWGVLP--DVNSEAYTAWTKEARRFGKAIWDILGGredpdivFEHPGRAT-----FPTSVFVCDRGGMVVIc 314

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 277 AGNGKPVIDFPINHIINYEINVLGSfRYAHgcYKQS---LFLVSNGLVDvkPLITHRFAFKDALKAYETVASGEEGVLKV 353
Cdd:cd08246 315 AGTTGYNHTYDNRYLWMRQKRIQGS-HFAN--DREAaeaNRLVMKGRID--PCLSKVFSLDETPDAHQLMHRNQHHVGNM 389


                ..
gi 19111912 354 II 355
Cdd:cd08246 390 AV 391
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 18-346 2.56e-05

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: 45.35  E-value: 2.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  18 IEDRPGQTLTDDhQVKVAIKATGICGSDVHYWKeGGIGDFIlKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCvc 97
Cdd:cd05282  16 LVSLPIPPPGPG-EVLVRMLAAPINPSDLITIS-GAYGSRP-PLPAVPGNEGVGVVVEVGSGVSGLLVGQRVLPLGGE-- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  98 rlcdycrsgrynlcphmefaatppydGTLRTYYITTEDFCTKLPKQISVEEGALF--EPMSVAVHAMTRGNLKCGSRVLV 175
Cdd:cd05282  91 --------------------------GTWQEYVVAPADDLIPVPDSISDEQAAMLyiNPLTAWLMLTEYLKLPPGDWVIQ 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 176 MGCG-TVGLLMMAVAKAYGaIDIVAVDASPSRVEfaqkyvgakPFTPIAAKE--NESLPDYAQRYKQAIieKYGEFDFAV 252
Cdd:cd05282 145 NAANsAVGRMLIQLAKLLG-FKTINVVRRDEQVE---------ELKALGADEviDSSPEDLAQRVKEAT--GGAGARLAL 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 253 DATGvGICIHTAVLALKRGGTFVQAGN-GKPVIDFPINHIINYEINVLG-----SFRYAHGCYKQSLF-----LVSNGlv 321
Cdd:cd05282 213 DAVG-GESATRLARSLRPGGTLVNYGLlSGEPVPFPRSVFIFKDITVRGfwlrqWLHSATKEAKQETFaevikLVEAG-- 289

                       330       340
                ....*....|....*....|....*...
gi 19111912 322 DVKPLITHRFA---FKDALKAYETVASG 346
Cdd:cd05282 290 VLTTPVGAKFPledFEEAVAAAEQPGRG 317
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 156-275 4.83e-05

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 43.75  E-value: 4.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 156 SVAVHAMTRGNLKCGSRVLVMGCGTvGLLMMAVAKAYGAiDIVAVDASPSRVEFAQKyvgakpftpIAAKENESLPDYAQ 235
Cdd:COG0500  13 GLAALLALLERLPKGGRVLDLGCGT-GRNLLALAARFGG-RVIGIDLSPEAIALARA---------RAAKAGLGNVEFLV 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 19111912 236 R-YKQAIIEKYGEFDFAVDATgvgiCIH-------TAVL-----ALKRGGTFV 275
Cdd:COG0500  82 AdLAELDPLPAESFDLVVAFG----VLHhlppeerEALLrelarALKPGGVLL 130
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
170-212 9.77e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 40.96  E-value: 9.77e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 19111912 170 GSRVLVMGCGTvGLLMMAVAKAYGAIDIVAVDASPSRVEFAQK 212
Cdd:COG4106   2 PRRVLDLGCGT-GRLTALLAERFPGARVTGVDLSPEMLARARA 43
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 173-219 1.24e-04

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 40.62  E-value: 1.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 19111912   173 VLVMGCGTvGLLMMAVAKAYGAiDIVAVDASPSRVEFAQKYVGAKPF 219
Cdd:pfam13649   1 VLDLGCGT-GRLTLALARRGGA-RVTGVDLSPEMLERARERAAEAGL 45
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 18-213 1.99e-04

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 42.71  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   18 IEDRPGQTLTDDhQVKVAIKATGICGSDV-----HYWKEGGIGDfilkkpmILGHESAGVVVEVGKGVSSLKPGDPV-AV 91
Cdd:PTZ00354  18 IGESPKPAPKRN-DVLIKVSAAGVNRADTlqrqgKYPPPPGSSE-------ILGLEVAGYVEDVGSDVKRFKEGDRVmAL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   92 EPGcvcrlcdycrsGRYNlcphmEFAATPpydgtlrtyyittEDFCTKLPKQISVEE-GALFEPMSVAVHAMTR-GNLKC 169
Cdd:PTZ00354  90 LPG-----------GGYA-----EYAVAH-------------KGHVMHIPQGYTFEEaAAIPEAFLTAWQLLKKhGDVKK 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 19111912  170 GSRVLV-MGCGTVGLLMMAVAKAYGAIDIVAVdASPSRVEFAQKY 213
Cdd:PTZ00354 141 GQSVLIhAGASGVGTAAAQLAEKYGAATIITT-SSEEKVDFCKKL 184
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 124-213 4.35e-04

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 41.60  E-value: 4.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912    124 GTLRTYYITTEDFCTKLPKQISVEEGAlfepmSV------AVHAM-TRGNLKCGSRVLV-MGCGTVGLLMMAVAKAYGAi 195
Cdd:smart00829  56 GAFATRVVTDARLVVPIPDGWSFEEAA-----TVpvvfltAYYALvDLARLRPGESVLIhAAAGGVGQAAIQLARHLGA- 129

                           90
                   ....*....|....*...
gi 19111912    196 DIVAVDASPSRVEFAQKY 213
Cdd:smart00829 130 EVFATAGSPEKRDFLRAL 147
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 170-213 5.03e-04

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 39.62  E-value: 5.03e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 19111912 170 GSRVLVMGCGTvGLLMMAVAKAyGAiDIVAVDASPSRVEFAQKY 213
Cdd:COG2227  25 GGRVLDVGCGT-GRLALALARR-GA-DVTGVDISPEALEIARER 65
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 172-228 1.04e-03

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 39.79  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 19111912   172 RVLVMGCGTVGLLMMAVAKAYGAIdIVAVDASPSRVEFAQKYVGAKPFTPIAAKENE 228
Cdd:pfam01262  30 KVLVIGGGVAGLNAAATAKGLGAI-VTILDVRPARLEQLESILGAKFVETLYSQAEL 85
PRK14968 PRK14968
putative methyltransferase; Provisional
 168-212 1.75e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.11  E-value: 1.75e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 19111912  168 KCGSRVLVMGCGTvGLLMMAVAKAygAIDIVAVDASPSRVEFAQK 212
Cdd:PRK14968  22 KKGDRVLEVGTGS-GIVAIVAAKN--GKKVVGVDINPYAVECAKC 63
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 128-209 3.73e-03

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: 38.56  E-value: 3.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 128 TYYITTEDFCTKLPKQISVEEGALFEPMSV-AVHAMTRGNLKCGSRVLVM-GCGTVGLLMMAVAKAYGAIdIVAVDASPS 205
Cdd:cd08251  78 TLVTVPEDQVVRKPASLSFEEACALPVVFLtVIDAFARAGLAKGEHILIQtATGGTGLMAVQLARLKGAE-IYATASSDD 156


                ....
gi 19111912 206 RVEF 209
Cdd:cd08251 157 KLEY 160
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
160-201 5.05e-03

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 38.23  E-value: 5.05e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 19111912 160 HAMTRG-------NLKCGSRVLVMGCGTvGLLMMAVAKaYGAIDIVAVD 201
Cdd:COG2264 132 HPTTRLclealekLLKPGKTVLDVGCGS-GILAIAAAK-LGAKRVLAVD 178
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 29-216 5.19e-03

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: 38.19  E-value: 5.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912  29 DHQVKVAIKATGICGSDV-----HYWKEGGIGDfilkkpmILGHESAGVVVEVGKGVSSLKPGDPV-AVEPGcvcrlcdy 102
Cdd:cd05276  27 PGEVLIRVAAAGVNRADLlqrqgLYPPPPGASD-------ILGLEVAGVVVAVGPGVTGWKVGDRVcALLAG-------- 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 103 crsGRYnlcphMEFAATPpydgtlrtyyittEDFCTKLPKQISVEEGA-LFEPMSVAVHAM-TRGNLKCGSRVLVMGcGT 180
Cdd:cd05276  92 ---GGY-----AEYVVVP-------------AGQLLPVPEGLSLVEAAaLPEVFFTAWQNLfQLGGLKAGETVLIHG-GA 149

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 19111912 181 --VGLLMMAVAKAYGAIdIVAVDASPSRVEFAQKYvGA 216
Cdd:cd05276 150 sgVGTAAIQLAKALGAR-VIATAGSEEKLEACRAL-GA 185
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
157-212 7.63e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 37.19  E-value: 7.63e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19111912 157 VAVHAMTRGNLKcGSRVLVMGCGTvGLLMMAvAKAYGAIDIVAVDASPSRVEFAQK 212
Cdd:COG2263  34 LLHLAYLRGDIE-GKTVLDLGCGT-GMLAIG-AALLGAKKVVGVDIDPEALEIARE 86
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 170-275 8.46e-03

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 36.51  E-value: 8.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912 170 GSRVLVMGCGTvGLLMMAVAKAYGaiDIVAVDASPSRVEFAQKYVGAKPF--TPIAAK-ENESLPDyaqrykqaiiekyG 246
Cdd:COG2226  23 GARVLDLGCGT-GRLALALAERGA--RVTGVDISPEMLELARERAAEAGLnvEFVVGDaEDLPFPD-------------G 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 19111912 247 EFDFAvdatgvgICIHT--------AVLA-----LKRGGTFV 275
Cdd:COG2226  87 SFDLV-------ISSFVlhhlpdpeRALAeiarvLKPGGRLV 121
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 174-274 8.55e-03

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 35.42  E-value: 8.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111912   174 LVMGCGTvGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYVGAKPFTPIAakenesLPDYAQRykQAIIEKYGEFDFAVd 253
Cdd:pfam08242   1 LEIGCGT-GTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAV------RVELFQL--DLGELDPGSFDVVV- 70

                          90       100       110
                  ....*....|....*....|....*....|.
gi 19111912   254 ATGVgicIH-----TAVL-----ALKRGGTF 274
Cdd:pfam08242  71 ASNV---LHhladpRAVLrnirrLLKPGGVL 98
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
170-212 9.37e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 37.32  E-value: 9.37e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 19111912 170 GSRVLVMGCGTvGLL-MMAVAkaYGAIDIVAVDASPSRVEFAQK 212
Cdd:COG4076  36 GDVVLDIGTGS-GLLsMLAAR--AGAKKVYAVEVNPDIAAVARR 76
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH