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Conserved domains on  [gi|2539978014|ref|WP_296177065|]
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S-(hydroxymethyl)glutathione dehydrogenase/class III alcohol dehydrogenase [Psychrobacter sp. UBA2769]

Protein Classification

S-(hydroxymethyl)glutathione dehydrogenase/class III alcohol dehydrogenase( domain architecture ID 10169723)

S-(hydroxymethyl)glutathione dehydrogenase/class III alcohol dehydrogenase catalyzes the zinc-dependent conversion of formaldehyde and NAD(P) to formate and NAD(P)H, via the formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione; belongs to the medium chain dehydrogenase/reductase (MDR) family

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
6-373 0e+00

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: 740.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   6 IKSKAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQV 85
Cdd:cd08300     1 ITCKAAVAWEAGKPLSIEEVEVAPPKAGEVRIKILATGVCHTDAYTLSGADPEGLFPVILGHEGAGIVESVGEGVTSVKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  86 GDHVIPLYTAECGVCKMCTSGKTNLCSAVRETQGKGLMPDGTTRFYKDGEPIYHYMGCSTFSEYTVLPEISLAKVNKEAP 165
Cdd:cd08300    81 GDHVIPLYTPECGECKFCKSGKTNLCQKIRATQGKGLMPDGTSRFSCKGKPIYHFMGTSTFSEYTVVAEISVAKINPEAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 166 LEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKD 245
Cdd:cd08300   161 LDKVCLLGCGVTTGYGAVLNTAKVEPGSTVAVFGLGAVGLAVIQGAKAAGASRIIGIDINPDKFELAKKFGATDCVNPKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 246 YDKPIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGWGESVIIGVAGAGQEISTRPFQLVTGRVWRGSAFGGVKGR 325
Cdd:cd08300   241 HDKPIQQVLVEMTDGGVDYTFECIGNVKVMRAALEACHKGWGTSVIIGVAAAGQEISTRPFQLVTGRVWKGTAFGGWKSR 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2539978014 326 SELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIH 373
Cdd:cd08300   321 SQVPKLVEDYMKGKIKVDEFITHTMPLDEINEAFDLMHAGKSIRTVVK 368
 
Name Accession Description Interval E-value
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
6-373 0e+00

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: 740.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   6 IKSKAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQV 85
Cdd:cd08300     1 ITCKAAVAWEAGKPLSIEEVEVAPPKAGEVRIKILATGVCHTDAYTLSGADPEGLFPVILGHEGAGIVESVGEGVTSVKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  86 GDHVIPLYTAECGVCKMCTSGKTNLCSAVRETQGKGLMPDGTTRFYKDGEPIYHYMGCSTFSEYTVLPEISLAKVNKEAP 165
Cdd:cd08300    81 GDHVIPLYTPECGECKFCKSGKTNLCQKIRATQGKGLMPDGTSRFSCKGKPIYHFMGTSTFSEYTVVAEISVAKINPEAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 166 LEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKD 245
Cdd:cd08300   161 LDKVCLLGCGVTTGYGAVLNTAKVEPGSTVAVFGLGAVGLAVIQGAKAAGASRIIGIDINPDKFELAKKFGATDCVNPKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 246 YDKPIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGWGESVIIGVAGAGQEISTRPFQLVTGRVWRGSAFGGVKGR 325
Cdd:cd08300   241 HDKPIQQVLVEMTDGGVDYTFECIGNVKVMRAALEACHKGWGTSVIIGVAAAGQEISTRPFQLVTGRVWKGTAFGGWKSR 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2539978014 326 SELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIH 373
Cdd:cd08300   321 SQVPKLVEDYMKGKIKVDEFITHTMPLDEINEAFDLMHAGKSIRTVVK 368
adh_III_F_hyde TIGR02818
S-(hydroxymethyl)glutathione dehydrogenase/class III alcohol dehydrogenase; The members of ...
7-374 0e+00

S-(hydroxymethyl)glutathione dehydrogenase/class III alcohol dehydrogenase; The members of this protein family show dual function. First, they remove formaldehyde, a toxic metabolite, by acting as S-(hydroxymethyl)glutathione dehydrogenase (1.1.1.284). S-(hydroxymethyl)glutathione can form spontaneously from formaldehyde and glutathione, and so this enzyme previously was designated glutathione-dependent formaldehyde dehydrogenase. These same proteins are also designated alcohol dehydrogenase (EC 1.1.1.1) of class III, for activities that do not require glutathione; they tend to show poor activity for ethanol among their various substrate alcohols. [Cellular processes, Detoxification, Energy metabolism, Fermentation]


Pssm-ID: 131865 [Multi-domain]  Cd Length: 368  Bit Score: 703.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   7 KSKAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVG 86
Cdd:TIGR02818   1 KSRAAVAWAAGQPLKIEEVDVEMPQKGEVLVRIVATGVCHTDAFTLSGADPEGVFPVILGHEGAGIVEAVGEGVTSVKVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  87 DHVIPLYTAECGVCKMCTSGKTNLCSAVRETQGKGLMPDGTTRFYKDGEPIYHYMGCSTFSEYTVLPEISLAKVNKEAPL 166
Cdd:TIGR02818  81 DHVIPLYTAECGECKFCLSGKTNLCVAVRETQGKGLMPDGTSRFSKDGQPIYHYMGCSTFSEYTVVPEISLAKINPAAPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 167 EEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKDY 246
Cdd:TIGR02818 161 EEVCLLGCGVTTGIGAVLNTAKVEEGDTVAVFGLGGIGLSVIQGARMAKASRIIAIDINPAKFELAKKLGATDCVNPNDY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 247 DKPIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGWGESVIIGVAGAGQEISTRPFQLVTGRVWRGSAFGGVKGRS 326
Cdd:TIGR02818 241 DKPIQEVIVEITDGGVDYSFECIGNVNVMRAALECCHKGWGESIIIGVAGAGQEISTRPFQLVTGRVWRGSAFGGVKGRT 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2539978014 327 ELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIHF 374
Cdd:TIGR02818 321 ELPGIVEQYMKGEIALDDFVTHTMPLEDINEAFDLMHEGKSIRTVIHY 368
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
17-373 0e+00

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 553.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  17 NQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEgVFPAILGHEGGGIVEQIGEGVTSVQVGDHVIPLYTAE 96
Cdd:COG1062     1 GGPLEIEEVELDEPRPGEVLVRIVAAGLCHSDLHVRDGDLPV-PLPAVLGHEGAGVVEEVGPGVTGVAPGDHVVLSFIPS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  97 CGVCKMCTSGKTNLCSAVRETQGKGLMPDGTTRF-YKDGEPIYHYMGCSTFSEYTVLPEISLAKVNKEAPLEEVCLLGCG 175
Cdd:COG1062    80 CGHCRYCASGRPALCEAGAALNGKGTLPDGTSRLsSADGEPVGHFFGQSSFAEYAVVPERSVVKVDKDVPLELAALLGCG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 176 VTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKDYDkpIQDVIV 255
Cdd:COG1062   160 VQTGAGAVLNTAKVRPGDTVAVFGLGGVGLSAVQGARIAGASRIIAVDPVPEKLELARELGATHTVNPADED--AVEAVR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 256 ELTDGGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEISTRPFQLV-TGRVWRGSAFGGVKGRSELPGYVER 334
Cdd:COG1062   238 ELTGGGVDYAFETTGNPAVIRQALEALRKG-GTVVVVGLAPPGAEISLDPFQLLlTGRTIRGSYFGGAVPRRDIPRLVDL 316
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 2539978014 335 YLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIH 373
Cdd:COG1062   317 YRAGRLPLDELITRRYPLDEINEAFDDLRSGEVIRPVIV 355
PLN02740 PLN02740
Alcohol dehydrogenase-like
4-373 1.94e-153

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 437.31  E-value: 1.94e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   4 KFIKSKAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGE-DPEGVFPAILGHEGGGIVEQIGEGVTS 82
Cdd:PLN02740    7 KVITCKAAVAWGPGEPLVMEEIRVDPPQKMEVRIKILYTSICHTDLSAWKGEnEAQRAYPRILGHEAAGIVESVGEGVED 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  83 VQVGDHVIPLYTAECGVCKMCTSGKTNLCSAVRETQGKGLM-PDGTTRFY--KDGEPIYHYMGCSTFSEYTVLPEISLAK 159
Cdd:PLN02740   87 LKAGDHVIPIFNGECGDCRYCKRDKTNLCETYRVDPFKSVMvNDGKTRFStkGDGQPIYHFLNTSTFTEYTVLDSACVVK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 160 VNKEAPLEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATD 239
Cdd:PLN02740  167 IDPNAPLKKMSLLSCGVSTGVGAAWNTANVQAGSSVAIFGLGAVGLAVAEGARARGASKIIGVDINPEKFEKGKEMGITD 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 240 CINPKDYDKPIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGWGESVIIGVAGAGQEISTRPFQLVTGRVWRGSAF 319
Cdd:PLN02740  247 FINPKDSDKPVHERIREMTGGGVDYSFECAGNVEVLREAFLSTHDGWGLTVLLGIHPTPKMLPLHPMELFDGRSITGSVF 326
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2539978014 320 GGVKGRSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIH 373
Cdd:PLN02740  327 GDFKGKSQLPNLAKQCMQGVVNLDGFITHELPFEKINEAFQLLEDGKALRCLLH 380
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
202-337 1.17e-28

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 108.08  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 202 GIGLSAVigaQMAKAS--RIIAIDINESKFELAKKLGATDCINPKDYDkpIQDVIVELTDG-GVDYSFECIGNVDVMRSA 278
Cdd:pfam00107   1 GVGLAAI---QLAKAAgaKVIAVDGSEEKLELAKELGADHVINPKETD--LVEEIKELTGGkGVDVVFDCVGSPATLEQA 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2539978014 279 LECCHKGwGESVIIGVAGAGQEISTRPFqLVTGRVWRGSAFGgvkGRSELPGYVERYLA 337
Cdd:pfam00107  76 LKLLRPG-GRVVVVGLPGGPLPLPLAPL-LLKELTILGSFLG---SPEEFPEALDLLAS 129
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
37-236 3.06e-05

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 45.07  E-value: 3.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   37 VKIIASGVCHTDAFTLSGEDPEgvfPAILGHEGGGIVEQIGEGVTSVQVGDHVIplytaecgvckmctsgktnlcsavre 116
Cdd:smart00829   1 IEVRAAGLNFRDVLIALGLYPG---EAVLGGECAGVVTRVGPGVTGLAVGDRVM-------------------------- 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  117 tqgkGLMPDGttrfykdgepiyhymgcstFSEYTVLPEISLAKVNKEAPLEEVCLLGCGVTTGMGAVMNTAKVEEGATVA 196
Cdd:smart00829  52 ----GLAPGA-------------------FATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYYALVDLARLRPGESVL 108
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2539978014  197 IF-GLGGIGLSAVIGAQMAKAsRIIAIDINESKFELAKKLG 236
Cdd:smart00829 109 IHaAAGGVGQAAIQLARHLGA-EVFATAGSPEKRDFLRALG 148
 
Name Accession Description Interval E-value
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
6-373 0e+00

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: 740.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   6 IKSKAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQV 85
Cdd:cd08300     1 ITCKAAVAWEAGKPLSIEEVEVAPPKAGEVRIKILATGVCHTDAYTLSGADPEGLFPVILGHEGAGIVESVGEGVTSVKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  86 GDHVIPLYTAECGVCKMCTSGKTNLCSAVRETQGKGLMPDGTTRFYKDGEPIYHYMGCSTFSEYTVLPEISLAKVNKEAP 165
Cdd:cd08300    81 GDHVIPLYTPECGECKFCKSGKTNLCQKIRATQGKGLMPDGTSRFSCKGKPIYHFMGTSTFSEYTVVAEISVAKINPEAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 166 LEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKD 245
Cdd:cd08300   161 LDKVCLLGCGVTTGYGAVLNTAKVEPGSTVAVFGLGAVGLAVIQGAKAAGASRIIGIDINPDKFELAKKFGATDCVNPKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 246 YDKPIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGWGESVIIGVAGAGQEISTRPFQLVTGRVWRGSAFGGVKGR 325
Cdd:cd08300   241 HDKPIQQVLVEMTDGGVDYTFECIGNVKVMRAALEACHKGWGTSVIIGVAAAGQEISTRPFQLVTGRVWKGTAFGGWKSR 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2539978014 326 SELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIH 373
Cdd:cd08300   321 SQVPKLVEDYMKGKIKVDEFITHTMPLDEINEAFDLMHAGKSIRTVVK 368
adh_III_F_hyde TIGR02818
S-(hydroxymethyl)glutathione dehydrogenase/class III alcohol dehydrogenase; The members of ...
7-374 0e+00

S-(hydroxymethyl)glutathione dehydrogenase/class III alcohol dehydrogenase; The members of this protein family show dual function. First, they remove formaldehyde, a toxic metabolite, by acting as S-(hydroxymethyl)glutathione dehydrogenase (1.1.1.284). S-(hydroxymethyl)glutathione can form spontaneously from formaldehyde and glutathione, and so this enzyme previously was designated glutathione-dependent formaldehyde dehydrogenase. These same proteins are also designated alcohol dehydrogenase (EC 1.1.1.1) of class III, for activities that do not require glutathione; they tend to show poor activity for ethanol among their various substrate alcohols. [Cellular processes, Detoxification, Energy metabolism, Fermentation]


Pssm-ID: 131865 [Multi-domain]  Cd Length: 368  Bit Score: 703.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   7 KSKAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVG 86
Cdd:TIGR02818   1 KSRAAVAWAAGQPLKIEEVDVEMPQKGEVLVRIVATGVCHTDAFTLSGADPEGVFPVILGHEGAGIVEAVGEGVTSVKVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  87 DHVIPLYTAECGVCKMCTSGKTNLCSAVRETQGKGLMPDGTTRFYKDGEPIYHYMGCSTFSEYTVLPEISLAKVNKEAPL 166
Cdd:TIGR02818  81 DHVIPLYTAECGECKFCLSGKTNLCVAVRETQGKGLMPDGTSRFSKDGQPIYHYMGCSTFSEYTVVPEISLAKINPAAPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 167 EEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKDY 246
Cdd:TIGR02818 161 EEVCLLGCGVTTGIGAVLNTAKVEEGDTVAVFGLGGIGLSVIQGARMAKASRIIAIDINPAKFELAKKLGATDCVNPNDY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 247 DKPIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGWGESVIIGVAGAGQEISTRPFQLVTGRVWRGSAFGGVKGRS 326
Cdd:TIGR02818 241 DKPIQEVIVEITDGGVDYSFECIGNVNVMRAALECCHKGWGESIIIGVAGAGQEISTRPFQLVTGRVWRGSAFGGVKGRT 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2539978014 327 ELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIHF 374
Cdd:TIGR02818 321 ELPGIVEQYMKGEIALDDFVTHTMPLEDINEAFDLMHEGKSIRTVIHY 368
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
17-373 0e+00

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 553.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  17 NQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEgVFPAILGHEGGGIVEQIGEGVTSVQVGDHVIPLYTAE 96
Cdd:COG1062     1 GGPLEIEEVELDEPRPGEVLVRIVAAGLCHSDLHVRDGDLPV-PLPAVLGHEGAGVVEEVGPGVTGVAPGDHVVLSFIPS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  97 CGVCKMCTSGKTNLCSAVRETQGKGLMPDGTTRF-YKDGEPIYHYMGCSTFSEYTVLPEISLAKVNKEAPLEEVCLLGCG 175
Cdd:COG1062    80 CGHCRYCASGRPALCEAGAALNGKGTLPDGTSRLsSADGEPVGHFFGQSSFAEYAVVPERSVVKVDKDVPLELAALLGCG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 176 VTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKDYDkpIQDVIV 255
Cdd:COG1062   160 VQTGAGAVLNTAKVRPGDTVAVFGLGGVGLSAVQGARIAGASRIIAVDPVPEKLELARELGATHTVNPADED--AVEAVR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 256 ELTDGGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEISTRPFQLV-TGRVWRGSAFGGVKGRSELPGYVER 334
Cdd:COG1062   238 ELTGGGVDYAFETTGNPAVIRQALEALRKG-GTVVVVGLAPPGAEISLDPFQLLlTGRTIRGSYFGGAVPRRDIPRLVDL 316
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 2539978014 335 YLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIH 373
Cdd:COG1062   317 YRAGRLPLDELITRRYPLDEINEAFDDLRSGEVIRPVIV 355
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
6-372 0e+00

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: 548.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   6 IKSKAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEdPEGVFPAILGHEGGGIVEQIGEGVTSVQV 85
Cdd:cd08277     1 IKCKAAVAWEAGKPLVIEEIEVAPPKANEVRIKMLATSVCHTDILAIEGF-KATLFPVILGHEGAGIVESVGEGVTNLKP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  86 GDHVIPLYTAECGVCKMCTSGKTNLCSAVRETqGKGLMPDGTTRFYKDGEPIYHYMGCSTFSEYTVLPEISLAKVNKEAP 165
Cdd:cd08277    80 GDKVIPLFIGQCGECSNCRSGKTNLCQKYRAN-ESGLMPDGTSRFTCKGKKIYHFLGTSTFSQYTVVDENYVAKIDPAAP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 166 LEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKD 245
Cdd:cd08277   159 LEHVCLLGCGFSTGYGAAWNTAKVEPGSTVAVFGLGAVGLSAIMGAKIAGASRIIGVDINEDKFEKAKEFGATDFINPKD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 246 YDKPIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGWGESVIIGVaGAGQEISTRPFQLVTGRVWRGSAFGGVKGR 325
Cdd:cd08277   239 SDKPVSEVIREMTGGGVDYSFECTGNADLMNEALESTKLGWGVSVVVGV-PPGAELSIRPFQLILGRTWKGSFFGGFKSR 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2539978014 326 SELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVI 372
Cdd:cd08277   318 SDVPKLVSKYMNKKFDLDELITHVLPFEEINKGFDLMKSGECIRTVI 364
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
4-374 0e+00

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: 540.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   4 KFIKSKAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPeGVFPAILGHEGGGIVEQIGEGVTSV 83
Cdd:cd08299     4 KVIKCKAAVLWEPKKPFSIEEIEVAPPKAHEVRIKIVATGICRSDDHVVSGKLV-TPFPVILGHEAAGIVESVGEGVTTV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  84 QVGDHVIPLYTAECGVCKMCTSGKTNLCSAVRETQGKGLMPDGTTRFYKDGEPIYHYMGCSTFSEYTVLPEISLAKVNKE 163
Cdd:cd08299    83 KPGDKVIPLFVPQCGKCRACLNPESNLCLKNDLGKPQGLMQDGTSRFTCKGKPIHHFLGTSTFSEYTVVDEIAVAKIDAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 164 APLEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINP 243
Cdd:cd08299   163 APLEKVCLIGCGFSTGYGAAVNTAKVTPGSTCAVFGLGGVGLSAIMGCKAAGASRIIAVDINKDKFAKAKELGATECINP 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 244 KDYDKPIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGWGESVIIGVAGAGQEISTRPFQLVTGRVWRGSAFGGVK 323
Cdd:cd08299   243 QDYKKPIQEVLTEMTDGGVDFSFEVIGRLDTMKAALASCHEGYGVSVIVGVPPSSQNLSINPMLLLTGRTWKGAVFGGWK 322
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2539978014 324 GRSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIHF 374
Cdd:cd08299   323 SKDSVPKLVADYMAKKFNLDPLITHTLPFEKINEGFDLLRSGKSIRTVLTF 373
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
6-373 0e+00

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: 537.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   6 IKSKAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQV 85
Cdd:cd08301     1 ITCKAAVAWEAGKPLVIEEVEVAPPQAMEVRIKILHTSLCHTDVYFWEAKGQTPLFPRILGHEAAGIVESVGEGVTDLKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  86 GDHVIPLYTAECGVCKMCTSGKTNLCSAVRETQGKGLMP-DGTTRFYKDGEPIYHYMGCSTFSEYTVLPEISLAKVNKEA 164
Cdd:cd08301    81 GDHVLPVFTGECKECRHCKSEKSNMCDLLRINTDRGVMInDGKSRFSINGKPIYHFVGTSTFSEYTVVHVGCVAKINPEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 165 PLEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPK 244
Cdd:cd08301   161 PLDKVCLLSCGVSTGLGAAWNVAKVKKGSTVAIFGLGAVGLAVAEGARIRGASRIIGVDLNPSKFEQAKKFGVTEFVNPK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 245 DYDKPIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGWGESVIIGVAGAGQEISTRPFQLVTGRVWRGSAFGGVKG 324
Cdd:cd08301   241 DHDKPVQEVIAEMTGGGVDYSFECTGNIDAMISAFECVHDGWGVTVLLGVPHKDAVFSTHPMNLLNGRTLKGTLFGGYKP 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2539978014 325 RSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIH 373
Cdd:cd08301   321 KTDLPNLVEKYMKKELELEKFITHELPFSEINKAFDLLLKGECLRCILH 369
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
9-372 0e+00

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: 527.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPeGVFPAILGHEGGGIVEQIGEGVTSVQVGDH 88
Cdd:cd05279     2 KAAVLWEKGKPLSIEEIEVAPPKAGEVRIKVVATGVCHTDLHVIDGKLP-TPLPVILGHEGAGIVESIGPGVTTLKPGDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 VIPLYTAECGVCKMCTSGKTNLCSAVRETQGKGLMPDGTTRFYKDGEPIYHYMGCSTFSEYTVLPEISLAKVNKEAPLEE 168
Cdd:cd05279    81 VIPLFGPQCGKCKQCLNPRPNLCSKSRGTNGRGLMSDGTSRFTCKGKPIHHFLGTSTFAEYTVVSEISLAKIDPDAPLEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 169 VCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKDYDK 248
Cdd:cd05279   161 VCLIGCGFSTGYGAAVNTAKVTPGSTCAVFGLGGVGLSVIMGCKAAGASRIIAVDINKDKFEKAKQLGATECINPRDQDK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 249 PIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGWGESVIIGVAGAGQEISTRPFQLVTGRVWRGSAFGGVKGRSEL 328
Cdd:cd05279   241 PIVEVLTEMTDGGVDYAFEVIGSADTLKQALDATRLGGGTSVVVGVPPSGTEATLDPNDLLTGRTIKGTVFGGWKSKDSV 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2539978014 329 PGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVI 372
Cdd:cd05279   321 PKLVALYRQKKFPLDELITHVLPFEEINDGFDLMRSGESIRTIL 364
PLN02740 PLN02740
Alcohol dehydrogenase-like
4-373 1.94e-153

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 437.31  E-value: 1.94e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   4 KFIKSKAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGE-DPEGVFPAILGHEGGGIVEQIGEGVTS 82
Cdd:PLN02740    7 KVITCKAAVAWGPGEPLVMEEIRVDPPQKMEVRIKILYTSICHTDLSAWKGEnEAQRAYPRILGHEAAGIVESVGEGVED 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  83 VQVGDHVIPLYTAECGVCKMCTSGKTNLCSAVRETQGKGLM-PDGTTRFY--KDGEPIYHYMGCSTFSEYTVLPEISLAK 159
Cdd:PLN02740   87 LKAGDHVIPIFNGECGDCRYCKRDKTNLCETYRVDPFKSVMvNDGKTRFStkGDGQPIYHFLNTSTFTEYTVLDSACVVK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 160 VNKEAPLEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATD 239
Cdd:PLN02740  167 IDPNAPLKKMSLLSCGVSTGVGAAWNTANVQAGSSVAIFGLGAVGLAVAEGARARGASKIIGVDINPEKFEKGKEMGITD 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 240 CINPKDYDKPIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGWGESVIIGVAGAGQEISTRPFQLVTGRVWRGSAF 319
Cdd:PLN02740  247 FINPKDSDKPVHERIREMTGGGVDYSFECAGNVEVLREAFLSTHDGWGLTVLLGIHPTPKMLPLHPMELFDGRSITGSVF 326
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2539978014 320 GGVKGRSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIH 373
Cdd:PLN02740  327 GDFKGKSQLPNLAKQCMQGVVNLDGFITHELPFEKINEAFQLLEDGKALRCLLH 380
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
8-372 7.94e-146

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: 416.94  E-value: 7.94e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   8 SKAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPeGVFPAILGHEGGGIVEQIGEGVTSVQVGD 87
Cdd:cd08279     1 MRAAVLHEVGKPLEIEEVELDDPGPGEVLVRIAAAGLCHSDLHVVTGDLP-APLPAVLGHEGAGVVEEVGPGVTGVKPGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  88 HVIPLYTAECGVCKMCTSGKTNLCSAVRETQGkGLMPDGTTRFYKDGEPIYHYMGCSTFSEYTVLPEISLAKVNKEAPLE 167
Cdd:cd08279    80 HVVLSWIPACGTCRYCSRGQPNLCDLGAGILG-GQLPDGTRRFTADGEPVGAMCGLGTFAEYTVVPEASVVKIDDDIPLD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 168 EVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKDYD 247
Cdd:cd08279   159 RAALLGCGVTTGVGAVVNTARVRPGDTVAVIGCGGVGLNAIQGARIAGASRIIAVDPVPEKLELARRFGATHTVNASEDD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 248 kpIQDVIVELTDG-GVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEISTRPFQLV-TGRVWRGSAFGGVKGR 325
Cdd:cd08279   239 --AVEAVRDLTDGrGADYAFEAVGRAATIRQALAMTRKG-GTAVVVGMGPPGETVSLPALELFlSEKRLQGSLYGSANPR 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2539978014 326 SELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVI 372
Cdd:cd08279   316 RDIPRLLDLYRAGRLKLDELVTRRYSLDEINEAFADMLAGENARGVI 362
PLN02827 PLN02827
Alcohol dehydrogenase-like
6-373 9.24e-128

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 371.93  E-value: 9.24e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   6 IKSKAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDaftLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQV 85
Cdd:PLN02827   11 ITCRAAVAWGAGEALVMEEVEVSPPQPLEIRIKVVSTSLCRSD---LSAWESQALFPRIFGHEASGIVESIGEGVTEFEK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  86 GDHVIPLYTAECGVCKMCTSGKTNLCSaVRETQGKGLM-PDGTTRFYKDGEPIYHYMGCSTFSEYTVLPEISLAKVNKEA 164
Cdd:PLN02827   88 GDHVLTVFTGECGSCRHCISGKSNMCQ-VLGLERKGVMhSDQKTRFSIKGKPVYHYCAVSSFSEYTVVHSGCAVKVDPLA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 165 PLEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPK 244
Cdd:PLN02827  167 PLHKICLLSCGVAAGLGAAWNVADVSKGSSVVIFGLGTVGLSVAQGAKLRGASQIIGVDINPEKAEKAKTFGVTDFINPN 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 245 DYDKPIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGWGESVIIGVAGAGQEISTRPFQLVTGRVWRGSAFGGVKG 324
Cdd:PLN02827  247 DLSEPIQQVIKRMTGGGADYSFECVGDTGIATTALQSCSDGWGLTVTLGVPKAKPEVSAHYGLFLSGRTLKGSLFGGWKP 326
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2539978014 325 RSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIH 373
Cdd:PLN02827  327 KSDLPSLVDKYMNKEIMIDEFITHNLSFDEINKAFELMREGKCLRCVIH 375
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
10-372 5.72e-124

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: 362.08  E-value: 5.72e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  10 AAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVfPAILGHEGGGIVEQIGEGVTSVQVGDHV 89
Cdd:cd08281    11 APTPYADSRPLVIEEVELDPPGPGEVLVKIAAAGLCHSDLSVINGDRPRPL-PMALGHEAAGVVVEVGEGVTDLEVGDHV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  90 IPLYTAECGVCKMCTSGKTNLCSAVRETQGKGLMPDGTTRFYKDGEPIYHYMGCSTFSEYTVLPEISLAKVNKEAPLEEV 169
Cdd:cd08281    90 VLVFVPSCGHCRPCAEGRPALCEPGAAANGAGTLLSGGRRLRLRGGEINHHLGVSAFAEYAVVSRRSVVKIDKDVPLEIA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 170 CLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKDYDkp 249
Cdd:cd08281   170 ALFGCAVLTGVGAVVNTAGVRPGQSVAVVGLGGVGLSALLGAVAAGASQVVAVDLNEDKLALARELGATATVNAGDPN-- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 250 IQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEISTRPFQLVT-GRVWRGSAFGGVKGRSEL 328
Cdd:cd08281   248 AVEQVRELTGGGVDYAFEMAGSVPALETAYEITRRG-GTTVTAGLPDPEARLSVPALSLVAeERTLKGSYMGSCVPRRDI 326
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2539978014 329 PGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVI 372
Cdd:cd08281   327 PRYLALYLSGRLPVDKLLTHRLPLDEINEGFDRLAAGEAVRQVI 370
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
6-373 4.83e-119

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: 349.10  E-value: 4.83e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   6 IKSKAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPeGVFPAILGHEGGGIVEQIGEGVTSVQV 85
Cdd:cd08278     1 MKTTAAVVREPGGPFVLEDVELDDPRPDEVLVRIVATGICHTDLVVRDGGLP-TPLPAVLGHEGAGVVEAVGSAVTGLKP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  86 GDHVIpLYTAECGVCKMCTSGKTNLCSAVRETQGKGLMPDGTTRFYK-DGEPIY-HYMGCSTFSEYTVLPEISLAKVNKE 163
Cdd:cd08278    80 GDHVV-LSFASCGECANCLSGHPAYCENFFPLNFSGRRPDGSTPLSLdDGTPVHgHFFGQSSFATYAVVHERNVVKVDKD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 164 APLEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINP 243
Cdd:cd08278   159 VPLELLAPLGCGIQTGAGAVLNVLKPRPGSSIAVFGAGAVGLAAVMAAKIAGCTTIIAVDIVDSRLELAKELGATHVINP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 244 KDYDkpIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEISTRPFQLVT-GRVWRGSAFGGV 322
Cdd:cd08278   239 KEED--LVAAIREITGGGVDYALDTTGVPAVIEQAVDALAPR-GTLALVGAPPPGAEVTLDVNDLLVsGKTIRGVIEGDS 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2539978014 323 KGRSELPGYVERYLAGDIPLQDFIThTMPLEDINEAFDLMHKGESIRTVIH 373
Cdd:cd08278   316 VPQEFIPRLIELYRQGKFPFDKLVT-FYPFEDINQAIADSESGKVIKPVLR 365
Rxyl_3153 TIGR03989
NDMA-dependent alcohol dehydrogenase, Rxyl_3153 family; This model describes a clade within ...
7-374 7.98e-106

NDMA-dependent alcohol dehydrogenase, Rxyl_3153 family; This model describes a clade within the family pfam00107 of zinc-binding dehydrogenases. The family pfam00107 contains class III alcohol dehydrogenases, including enzymes designated S-(hydroxymethyl)glutathione dehydrogenase and NAD/mycothiol-dependent formaldehyde dehydrogenase. Members of the current family occur only in species that contain the very small protein mycofactocin (TIGR03969), a possible cofactor precursor, and radical SAM protein TIGR03962. We name this family for Rxyl_3153, where the lone member of the family co-clusters with these markers in Rubrobacter xylanophilus. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274905 [Multi-domain]  Cd Length: 369  Bit Score: 315.79  E-value: 7.98e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   7 KSKAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVG 86
Cdd:TIGR03989   1 KTKAAVLWGPGQPWEVEEIELDDPKAGEVLVKLVASGLCHSDEHLVTGDLPMPRYPILGGHEGAGVVTKVGPGVTGVKPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  87 DHVIPLYTAECGVCKMCTSGKTNLCSavretQGKGLM-----PDGTTRFYKDGEPIYHYMGCSTFSEYTVLPEISLAKVN 161
Cdd:TIGR03989  81 DHVVLSFIPACGRCRYCSTGLQNLCD-----LGAALLtgsqiSDGTYRFHADGQDVGQMCLLGTFSEYTVVPEASVVKID 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 162 KEAPLEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCI 241
Cdd:TIGR03989 156 DDIPLDKACLVGCGVPTGWGSAVNIADVRPGDTVVVMGIGGVGINAVQGAAVAGARKVIAVDPVEFKREQALKFGATHAF 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 242 NpkDYDKPIQdVIVELTDG-GVDYSFECIGNV--DVMRSALECCHKGwGESVIIGVAG-AGQEISTRPFQLV-TGRVWRG 316
Cdd:TIGR03989 236 A--SMEEAVQ-LVRELTNGqGADKTIITVGEVdgEHIAEALSATRKG-GRVVVTGLGPmADVDVKVNLFELTlLQKELQG 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2539978014 317 SAFGGVKGRSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIHF 374
Cdd:TIGR03989 312 TLFGGANPRADIPRLLELYRAGKLKLDELITRTYTLDQINEGYQDMLDGKNIRGVIVY 369
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
9-372 2.11e-91

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: 278.87  E-value: 2.11e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPeGVFPAILGHEGGGIVEQIGEGVTS---VQV 85
Cdd:cd08263     2 KAAVLKGPNPPLTIEEIPVPRPKEGEILIRVAACGVCHSDLHVLKGELP-FPPPFVLGHEISGEVVEVGPNVENpygLSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  86 GDHVIPLYTAECGVCKMCTSGKTNLC-SAVRETQGKGLMPDGTTR-FYKDGEPIYHY-MGcsTFSEYTVLPEISLAKVNK 162
Cdd:cd08263    81 GDRVVGSFIMPCGKCRYCARGKENLCeDFFAYNRLKGTLYDGTTRlFRLDGGPVYMYsMG--GLAEYAVVPATALAPLPE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 163 EAPLEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVigaQMAK---ASRIIAIDINESKFELAKKLGATD 239
Cdd:cd08263   159 SLDYTESAVLGCAGFTAYGALKHAADVRPGETVAVIGVGGVGSSAI---QLAKafgASPIIAVDVRDEKLAKAKELGATH 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 240 CINPKDYDKPiqDVIVELTDG-GVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEISTRPFQLVT-GRVWRGS 317
Cdd:cd08263   236 TVNAAKEDAV--AAIREITGGrGVDVVVEALGKPETFKLALDVVRDG-GRAVVVGLAPGGATAEIPITRLVRrGIKIIGS 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2539978014 318 aFGGvKGRSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGE-SIRTVI 372
Cdd:cd08263   313 -YGA-RPRQDLPELVGLAASGKLDPEALVTHKYKLEEINEAYENLRKGLiHGRAIV 366
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
9-372 1.50e-85

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 262.36  E-value: 1.50e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDH 88
Cdd:COG1064     2 KAAVLTEPGGPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGVTGFKVGDR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 V-IPLYTAeCGVCKMCTSGKTNLCSAVRETqgkGLMPDGttrfykdgepiyhymgcsTFSEYTVLPEISLAKVNKEAPLE 167
Cdd:COG1064    82 VgVGWVDS-CGTCEYCRSGRENLCENGRFT---GYTTDG------------------GYAEYVVVPARFLVKLPDGLDPA 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 168 EVCLLGCGVTTGMGAVMNtAKVEEGATVAIFGLGGIGLSAVigaQMAKA--SRIIAIDINESKFELAKKLGATDCINPKd 245
Cdd:COG1064   140 EAAPLLCAGITAYRALRR-AGVGPGDRVAVIGAGGLGHLAV---QIAKAlgAEVIAVDRSPEKLELARELGADHVVNSS- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 246 yDKPIQDVIVELTdgGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEIStrPFQLVTGRV-WRGSAFGgvkG 324
Cdd:COG1064   215 -DEDPVEAVRELT--GADVVIDTVGAPATVNAALALLRRG-GRLVLVGLPGGPIPLP--PFDLILKERsIRGSLIG---T 285
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2539978014 325 RSELPGYVERYLAGDIplqDFITHTMPLEDINEAFDLMHKGESI-RTVI 372
Cdd:COG1064   286 RADLQEMLDLAAEGKI---KPEVETIPLEEANEALERLRAGKVRgRAVL 331
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
9-374 8.10e-80

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: 248.13  E-value: 8.10e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQpLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDH 88
Cdd:COG1063     2 KALVLHGPGD-LRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 VIPLYTAECGVCKMCTSGKTNLCsavRETQGKGlmpdgttrfykdgepIYHYMGCstFSEYTVLPEISLAKVNKEAPLEE 168
Cdd:COG1063    81 VVVEPNIPCGECRYCRRGRYNLC---ENLQFLG---------------IAGRDGG--FAEYVRVPAANLVKVPDGLSDEA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 169 VCL---LGCGVttgMGAVMntAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKD 245
Cdd:COG1063   141 AALvepLAVAL---HAVER--AGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARELGADAVVNPRE 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 246 YDkpIQDVIVELTDG-GVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEIstrPFQLVTGR--VWRGSaFGGV 322
Cdd:COG1063   216 ED--LVEAVRELTGGrGADVVIEAVGAPAALEQALDLVRPG-GTVVLVGVPGGPVPI---DLNALVRKelTLRGS-RNYT 288
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2539978014 323 kgRSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKG--ESIRTVIHF 374
Cdd:COG1063   289 --REDFPEALELLASGRIDLEPLITHRFPLDDAPEAFEAAADRadGAIKVVLDP 340
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
34-328 2.65e-67

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: 213.72  E-value: 2.65e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  34 EVLVKIIASGVCHTDAFTLSGEDPEGV-FPAILGHEGGGIVEQIGEGVTSVQVGDHVIPLYTAECGVCKMCTSGKTNLCs 112
Cdd:cd05188     1 EVLVRVEAAGLCGTDLHIRRGGYPPPPkLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNLGCGTCELCRELCPGGG- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 113 avretqgkglmpdgttrfykdgepIYHYMGCSTFSEYTVLPEISLAKVNKEAPLEEVCLLGCGVTTGMGAVMNTAKVEEG 192
Cdd:cd05188    80 ------------------------ILGEGLDGGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVLKPG 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 193 ATVAIFGLGGIGLSAVIGAQMAKAsRIIAIDINESKFELAKKLGATDCINPKDYDKPiqDVIVELTDGGVDYSFECIGNV 272
Cdd:cd05188   136 DTVLVLGAGGVGLLAAQLAKAAGA-RVIVTDRSDEKLELAKELGADHVIDYKEEDLE--EELRLTGGGGADVVIDAVGGP 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2539978014 273 DVMRSALECCHKGwGESVIIGVAGAGQEISTRPFQLVTGRVWRGSAFGGVKGRSEL 328
Cdd:cd05188   213 ETLAQALRLLRPG-GRIVVVGGTSGGPPLDDLRRLLFKELTIIGSTGGTREDFEEA 267
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
8-372 1.92e-66

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: 214.43  E-value: 1.92e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   8 SKAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTS----- 82
Cdd:cd08231     1 ARAAVLTGPGKPLEIREVPLPDLEPGAVLVRVRLAGVCGSDVHTVAGRRPRVPLPIILGHEGVGRVVALGGGVTTdvage 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  83 -VQVGDHVIPLYTAECGVCKMCTSGKTNLCSAVRetqgkglmPDGTTRFYKDGepiyHYMGCstFSEYTVL-PEISLAKV 160
Cdd:cd08231    81 pLKVGDRVTWSVGAPCGRCYRCLVGDPTKCENRK--------KYGHEASCDDP----HLSGG--YAEHIYLpPGTAIVRV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 161 NKEAPLEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDC 240
Cdd:cd08231   147 PDNVPDEVAAPANCALATVLAALDRAGPVGAGDTVVVQGAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAREFGADAT 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 241 INPKDYDKPIQDVIV-ELTDG-GVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEISTRPFQLVtgRVW---R 315
Cdd:cd08231   227 IDIDELPDPQRRAIVrDITGGrGADVVIEASGHPAAVPEGLELLRRG-GTYVLVGSVAPAGTVPLDPERIV--RKNltiI 303
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2539978014 316 GSAFGGVKGRSELPGYVERYlAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVI 372
Cdd:cd08231   304 GVHNYDPSHLYRAVRFLERT-QDRFPFAELVTHRYPLEDINEALELAESGTALKVVI 359
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
19-373 6.27e-66

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: 212.11  E-value: 6.27e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  19 PLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGV-FPAILGHEGGGIVEQIGEGVTSVQVGDHVIPLYTAEC 97
Cdd:cd08254    13 LLVLEEVPVPEPGPGEVLVKVKAAGVCHSDLHILDGGVPTLTkLPLTLGHEIAGTVVEVGAGVTNFKVGDRVAVPAVIPC 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  98 GVCKMCTSGKTNLCsavRETQGKGLMPDGttrfykdgepiyhymgcsTFSEYTVLPEISLAKVNKEAPLEEVCLLGCGVT 177
Cdd:cd08254    93 GACALCRRGRGNLC---LNQGMPGLGIDG------------------GFAEYIVVPARALVPVPDGVPFAQAAVATDAVL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 178 TGMGAVMNTAKVEEGATVAIFGLGGIGLSAVigaQMAKA--SRIIAIDINESKFELAKKLGATDCINPKdyDKPIQDVIV 255
Cdd:cd08254   152 TPYHAVVRAGEVKPGETVLVIGLGGLGLNAV---QIAKAmgAAVIAVDIKEEKLELAKELGADEVLNSL--DDSPKDKKA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 256 ELTDGGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEISTrpFQLVTGRV-WRGSaFGGVkgRSELPGYVER 334
Cdd:cd08254   227 AGLGGGFDVIFDFVGTQPTFEDAQKAVKPG-GRIVVVGLGRDKLTVDL--SDLIARELrIIGS-FGGT--PEDLPEVLDL 300
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2539978014 335 YLAGDIplqDFITHTMPLEDINEAFDLMHKGE-SIRTVIH 373
Cdd:cd08254   301 IAKGKL---DPQVETRPLDEIPEVLERLHKGKvKGRVVLV 337
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
9-372 1.33e-58

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: 193.30  E-value: 1.33e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDH 88
Cdd:cd08259     2 KAAILHKPNKPLQIEEVPDPEPGPGEVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVGEGVERFKPGDR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 VIPLYTAECGVCKMCTSGKTNLCSAVRETqgkGLMPDGttrfykdgepiyhymgcsTFSEYTVLPEISLAKVNKEAPLEE 168
Cdd:cd08259    82 VILYYYIPCGKCEYCLSGEENLCRNRAEY---GEEVDG------------------GFAEYVKVPERSLVKLPDNVSDES 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 169 VCLLGCGVTTGMGAvMNTAKVEEGATVAI-FGLGGIGLSAVigaQMAKA--SRIIAIDINESKFELAKKLGATDCINPKD 245
Cdd:cd08259   141 AALAACVVGTAVHA-LKRAGVKKGDTVLVtGAGGGVGIHAI---QLAKAlgARVIAVTRSPEKLKILKELGADYVIDGSK 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 246 YDKPIQDViveltdGGVDYSFECIGNVDVMRSaLECCHKGwGESVIIGVAGaGQEISTRPFQLVTGRV-WRGSAFGgvkG 324
Cdd:cd08259   217 FSEDVKKL------GGADVVIELVGSPTIEES-LRSLNKG-GRLVLIGNVT-PDPAPLRPGLLILKEIrIIGSISA---T 284
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2539978014 325 RSELPGYVERYLAGDI-PLqdfITHTMPLEDINEAFDLMHKGESI-RTVI 372
Cdd:cd08259   285 KADVEEALKLVKEGKIkPV---IDRVVSLEDINEALEDLKSGKVVgRIVL 331
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
9-362 1.75e-58

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: 193.20  E-value: 1.75e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDH 88
Cdd:cd08260     2 RAAVYEEFGEPLEIREVPDPEPPPDGVVVEVEACGVCRSDWHGWQGHDPDVTLPHVPGHEFAGVVVEVGEDVSRWRVGDR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 VIPLYTAECGVCKMCTSGKTNLCSAVretQGKGLMPDGttrfykdgepiyhymgcsTFSEYTVLP--EISLAKVNKEAPL 166
Cdd:cd08260    82 VTVPFVLGCGTCPYCRAGDSNVCEHQ---VQPGFTHPG------------------SFAEYVAVPraDVNLVRLPDDVDF 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 167 EEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKAsRIIAIDINESKFELAKKLGATDCINPKDY 246
Cdd:cd08260   141 VTAAGLGCRFATAFRALVHQARVKPGEWVAVHGCGGVGLSAVMIASALGA-RVIAVDIDDDKLELARELGAVATVNASEV 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 247 DKPiQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEISTRPFQLVTGrvwRGSAFGGVKG-- 324
Cdd:cd08260   220 EDV-AAAVRDLTGGGAHVSVDALGIPETCRNSVASLRKR-GRHVQVGLTLGEEAGVALPMDRVVA---RELEIVGSHGmp 294
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2539978014 325 RSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLM 362
Cdd:cd08260   295 AHRYDAMLALIASGKLDPEPLVGRTISLDEAPDALAAM 332
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
9-373 9.18e-58

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: 191.27  E-value: 9.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQpLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDH 88
Cdd:cd08235     2 KAAVLHGPND-VRLEEVPVPEPGPGEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGDGVTGFKVGDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 VIPLYTAECGVCKMCTSGKTNLCSavretqgkglmpdgttRFYKDGepiYHYMGcsTFSEYTVLPEISLAK--VNK---- 162
Cdd:cd08235    81 VFVAPHVPCGECHYCLRGNENMCP----------------NYKKFG---NLYDG--GFAEYVRVPAWAVKRggVLKlpdn 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 163 ----EAPLEE---VCLLGcgvttgmgavMNTAKVEEGATVAIFGLGGIGLsavIGAQMAK---ASRIIAIDINESKFELA 232
Cdd:cd08235   140 vsfeEAALVEplaCCINA----------QRKAGIKPGDTVLVIGAGPIGL---LHAMLAKasgARKVIVSDLNEFRLEFA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 233 KKLGATDCINPKDYDKPiqDVIVELTDG-GVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEIStrpfqLVTG 311
Cdd:cd08235   207 KKLGADYTIDAAEEDLV--EKVRELTDGrGADVVIVATGSPEAQAQALELVRKG-GRILFFGGLPKGSTVN-----IDPN 278
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539978014 312 RVWRG--SAFGGVKGRSElpgYVERYL----AGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIH 373
Cdd:cd08235   279 LIHYReiTITGSYAASPE---DYKEALeliaSGKIDVKDLITHRFPLEDIEEAFELAADGKSLKIVIT 343
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
9-373 2.06e-57

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: 190.05  E-value: 2.06e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQpLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEdPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDH 88
Cdd:cd08234     2 KALVYEGPGE-LEVEEVPVPEPGPDEVLIKVAACGICGTDLHIYEGE-FGAAPPLVPGHEFAGVVVAVGSKVTGFKVGDR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 VI--PLYTaeCGVCKMCTSGKTNLC---SAVretqgkglmpdGTTRfykDGepiyhymGcstFSEYTVLPEISLAKVNKE 163
Cdd:cd08234    80 VAvdPNIY--CGECFYCRRGRPNLCenlTAV-----------GVTR---NG-------G---FAEYVVVPAKQVYKIPDN 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 164 APLEEVCL---LGCgvttgmgAV--MNTAKVEEGATVAIFGLGGIGLsavIGAQMAK---ASRIIAIDINESKFELAKKL 235
Cdd:cd08234   134 LSFEEAALaepLSC-------AVhgLDLLGIKPGDSVLVFGAGPIGL---LLAQLLKlngASRVTVAEPNEEKLELAKKL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 236 GATDCINPKDYDKPIQDvivELTDGGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEISTRPFQLvtgrvwr 315
Cdd:cd08234   204 GATETVDPSREDPEAQK---EDNPYGFDVVIEATGVPKTLEQAIEYARRG-GTVLVFGVYAPDARVSISPFEI------- 272
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2539978014 316 gsaFG---GVKGRSELPGYVERYLA----GDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIH 373
Cdd:cd08234   273 ---FQkelTIIGSFINPYTFPRAIAllesGKIDVKGLVSHRLPLEEVPEALEGMRSGGALKVVVV 334
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
17-374 3.80e-57

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: 189.32  E-value: 3.80e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  17 NQPLSIEEVDVMLP--RKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDHV--IPl 92
Cdd:cd08261     7 EKPGRLEVVDIPEPvpGAGEVLVRVKRVGICGSDLHIYHGRNPFASYPRILGHELSGEVVEVGEGVAGLKVGDRVvvDP- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  93 YTaECGVCKMCTSGKTNLCSAVRETqgkGLMPDGTtrfykdgepiyhymgcstFSEYTVLPEiSLAKVNKEAPLEEVCLL 172
Cdd:cd08261    86 YI-SCGECYACRKGRPNCCENLQVL---GVHRDGG------------------FAEYIVVPA-DALLVPEGLSLDQAALV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 173 GCgVTTGMGAVmNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKAsRIIAIDINESKFELAKKLGATDCINPKDYDkpIQD 252
Cdd:cd08261   143 EP-LAIGAHAV-RRAGVTAGDTVLVVGAGPIGLGVIQVAKARGA-RVIVVDIDDERLEFARELGADDTINVGDED--VAA 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 253 VIVELTDG-GVDYSFECIGNVDVMRSALE-CCHKGwgESVIIGVAGAGQEISTRPF-----QLVTGRVWRGSAFGGVkgr 325
Cdd:cd08261   218 RLRELTDGeGADVVIDATGNPASMEEAVElVAHGG--RVVLVGLSKGPVTFPDPEFhkkelTILGSRNATREDFPDV--- 292
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2539978014 326 selpgyVERYLAGDIPLQDFITHTMPLEDINEAFDLM--HKGESIRTVIHF 374
Cdd:cd08261   293 ------IDLLESGKVDPEALITHRFPFEDVPEAFDLWeaPPGGVIKVLIEF 337
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
9-366 6.37e-57

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: 188.92  E-value: 6.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSG--EDPEGV-FPAILGHEGGGIVEQIGEGVTSVQV 85
Cdd:cd05284     2 KAARLYEYGKPLRLEDVPVPEPGPGQVLVRVGGAGVCHSDLHVIDGvwGGILPYkLPFTLGHENAGWVEEVGSGVDGLKE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  86 GDHVI--PLYTaeCGVCKMCTSGKTNLCSAVRETqgkGLMPDGttrfykdgepiyhymgcsTFSEYTVLPEISLAKVNKE 163
Cdd:cd05284    82 GDPVVvhPPWG--CGTCRYCRRGEENYCENARFP---GIGTDG------------------GFAEYLLVPSRRLVKLPRG 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 164 APLEEVCLLGCGVTTGMGAVMNTAKV-EEGATVAIFGLGGIGlsaVIGAQMAKA---SRIIAIDINESKFELAKKLGATD 239
Cdd:cd05284   139 LDPVEAAPLADAGLTAYHAVKKALPYlDPGSTVVVIGVGGLG---HIAVQILRAltpATVIAVDRSEEALKLAERLGADH 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 240 CINPKDydkPIQDVIVELTDG-GVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGqEISTRPFqLVTGRVWRGSa 318
Cdd:cd05284   216 VLNASD---DVVEEVRELTGGrGADAVIDFVGSDETLALAAKLLAKG-GRYVIVGYGGHG-RLPTSDL-VPTEISVIGS- 288
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2539978014 319 FGGvkGRSELPGYVERYLAGDIPLQdfiTHTMPLEDINEAFDLMHKGE 366
Cdd:cd05284   289 LWG--TRAELVEVVALAESGKVKVE---ITKFPLEDANEALDRLREGR 331
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
9-366 1.63e-56

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: 188.20  E-value: 1.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQpLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEgVFPAILGHEGGGIVEQIGEGVTSVQVGDH 88
Cdd:cd08236     2 KALVLTGPGD-LRYEDIPKPEPGPGEVLVKVKACGICGSDIPRYLGTGAY-HPPLVLGHEFSGTVEEVGSGVDDLAVGDR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 V--IPLYTaeCGVCKMCTSGKTNLCSAvretqgkglmpdgttrfykdgepiYHYMGCS---TFSEYTVLPEISLAKVNKE 163
Cdd:cd08236    80 VavNPLLP--CGKCEYCKKGEYSLCSN------------------------YDYIGSRrdgAFAEYVSVPARNLIKIPDH 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 164 APLEEVCLLGcGVTTGMGAVMNtAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINP 243
Cdd:cd08236   134 VDYEEAAMIE-PAAVALHAVRL-AGITLGDTVVVIGAGTIGLLAIQWLKILGAKRVIAVDIDDEKLAVARELGADDTINP 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 244 KDYDkpiQDVIVELTDG-GVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEISTRPFQLVTGR--VWRGS--A 318
Cdd:cd08236   212 KEED---VEKVRELTEGrGADLVIEAAGSPATIEQALALARPG-GKVVLVGIPYGDVTLSEEAFEKILRKelTIQGSwnS 287
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2539978014 319 FGGVKGRSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGE 366
Cdd:cd08236   288 YSAPFPGDEWRTALDLLASGKIKVEPLITHRLPLEDGPAAFERLADRE 335
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
9-374 2.10e-56

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: 187.87  E-value: 2.10e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDH 88
Cdd:cd05278     2 KALVYLGPGKIGLEEVPDPKIQGPHDAIVRVTATSICGSDLHIYRGGVPGAKHGMILGHEFVGEVVEVGSDVKRLKPGDR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 VIPLYTAECGVCKMCTSGKTNLCsavrETQGKGLMPDGttrfYKDGepiyhymgcsTFSEYTVLPE--ISLAKVNKEAPL 166
Cdd:cd05278    82 VSVPCITFCGRCRFCRRGYHAHC----ENGLWGWKLGN----RIDG----------GQAEYVRVPYadMNLAKIPDGLPD 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 167 EEVCLLGCGVTTGM-GAVMntAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKD 245
Cdd:cd05278   144 EDALMLSDILPTGFhGAEL--AGIKPGSTVAVIGAGPVGLCAVAGARLLGAARIIAVDSNPERLDLAKEAGATDIINPKN 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 246 YDkpIQDVIVELTDG-GVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEIStrPFQLVTGRVWRGSAfGGVKG 324
Cdd:cd05278   222 GD--IVEQILELTGGrGVDCVIEAVGFEETFEQAVKVVRPG-GTIANVGVYGKPDPLP--LLGEWFGKNLTFKT-GLVPV 295
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2539978014 325 RSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGES--IRTVIHF 374
Cdd:cd05278   296 RARMPELLDLIEEGKIDPSKLITHRFPLDDILKAYRLFDNKPDgcIKVVIRP 347
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
20-373 8.20e-54

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: 180.89  E-value: 8.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  20 LSIEEVDVMLPRKGEVLVKIIASGVCHTD-------AFTLSGEDPegvfPAILGHEGGGIVEQIGEGVTSVQVGDHVipl 92
Cdd:cd05281    13 AELVEVPVPKPGPGEVLIKVLAASICGTDvhiyewdEWAQSRIKP----PLIFGHEFAGEVVEVGEGVTRVKVGDYV--- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  93 yTAE----CGVCKMCTSGKTNLCsavRETQGKGLMPDGTtrfykdgepiyhymgcstFSEYTVLPEISLAKVNKEAPLEE 168
Cdd:cd05281    86 -SAEthivCGKCYQCRTGNYHVC---QNTKILGVDTDGC------------------FAEYVVVPEENLWKNDKDIPPEI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 169 VcllgcGVTTGMGAVMNTAKVEE--GATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKDY 246
Cdd:cd05281   144 A-----SIQEPLGNAVHTVLAGDvsGKSVLITGCGPIGLMAIAVAKAAGASLVIASDPNPYRLELAKKMGADVVINPREE 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 247 DkpIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVagAGQEIStrpFQLVTGRVWRGSAFGGVKGRS 326
Cdd:cd05281   219 D--VVEVKSVTDGTGVDVVLEMSGNPKAIEQGLKALTPG-GRVSILGL--PPGPVD---IDLNNLVIFKGLTVQGITGRK 290
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2539978014 327 --ELPGYVERYL-AGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIH 373
Cdd:cd05281   291 mfETWYQVSALLkSGKVDLSPVITHKLPLEDFEEAFELMRSGKCGKVVLY 340
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
9-374 1.41e-51

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: 175.03  E-value: 1.41e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPN-QPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDP-EGVFPAILGHEGGGIVEQIGEGVTSVQVG 86
Cdd:cd08297     2 KAAVVEEFGeKPYEVKDVPVPEPGPGEVLVKLEASGVCHTDLHAALGDWPvKPKLPLIGGHEGAGVVVAVGPGVSGLKVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  87 DHV--IPLYTAeCGVCKMCTSGKTNLCsavRETQGKGLMPDGttrfykdgepiyhymgcsTFSEYTVLPEISLAKVNKEA 164
Cdd:cd08297    82 DRVgvKWLYDA-CGKCEYCRTGDETLC---PNQKNSGYTVDG------------------TFAEYAIADARYVTPIPDGL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 165 PLEEVCLLGC-GVTTgMGAVmNTAKVEEGATVAIFGLGGiGLsAVIGAQMAKA--SRIIAIDINESKFELAKKLGATDCI 241
Cdd:cd08297   140 SFEQAAPLLCaGVTV-YKAL-KKAGLKPGDWVVISGAGG-GL-GHLGVQYAKAmgLRVIAIDVGDEKLELAKELGADAFV 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 242 NPKDYDkPIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAgAGQEISTRPFQLV-TGRVWRGSAFG 320
Cdd:cd08297   216 DFKKSD-DVEAVKELTGGGGAHAVVVTAVSAAAYEQALDYLRPG-GTLVCVGLP-PGGFIPLDPFDLVlRGITIVGSLVG 292
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2539978014 321 gvkGRSELPGYVERYLAGDIplQDFIThTMPLEDINEAFDLMHKGESI-RTVIHF 374
Cdd:cd08297   293 ---TRQDLQEALEFAARGKV--KPHIQ-VVPLEDLNEVFEKMEEGKIAgRVVVDF 341
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
9-373 2.67e-51

(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: 174.65  E-value: 2.67e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQpLSIEEVDVMLPRKGEVLVKIIASGVCHTD---------AFTLSGEDPE--GVFPAILGHEGGGIVEQIG 77
Cdd:cd08233     2 KAARYHGRKD-IRVEEVPEPPVKPGEVKIKVAWCGICGSDlheyldgpiFIPTEGHPHLtgETAPVTLGHEFSGVVVEVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  78 EGVTSVQVGDHVIPLYTAECGVCKMCTSGKTNLCSAVRETqgkGLM-PDGTtrfykdgepiyhymgcstFSEYTVLPEIS 156
Cdd:cd08233    81 SGVTGFKVGDRVVVEPTIKCGTCGACKRGLYNLCDSLGFI---GLGgGGGG------------------FAEYVVVPAYH 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 157 LAKVNKEAPLEEVCL---LgcgvTTGMGAVmNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAK 233
Cdd:cd08233   140 VHKLPDNVPLEEAALvepL----AVAWHAV-RRSGFKPGDTALVLGAGPIGLLTILALKAAGASKIIVSEPSEARRELAE 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 234 KLGATDCINPKDYDkpIQDVIVELTDG-GVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAgqEISTRPFQLV-TG 311
Cdd:cd08233   215 ELGATIVLDPTEVD--VVAEVRKLTGGgGVDVSFDCAGVQATLDTAIDALRPR-GTAVNVAIWEK--PISFNPNDLVlKE 289
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2539978014 312 RVWRGSAfggvkgrselpGYVERYLA--------GDIPLQDFITHTMPLEDI-NEAFD--LMHKGESIRTVIH 373
Cdd:cd08233   290 KTLTGSI-----------CYTREDFEevidllasGKIDAEPLITSRIPLEDIvEKGFEelINDKEQHVKILVS 351
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
20-374 3.11e-50

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: 171.35  E-value: 3.11e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  20 LSIEEVDVMLPRKGEVLVKIIASGVCHTD-AFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDHVIPLYTAECG 98
Cdd:cd08239    12 VELREFPVPVPGPGEVLLRVKASGLCGSDlHYYYHGHRAPAYQGVIPGHEPAGVVVAVGPGVTHFRVGDRVMVYHYVGCG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  99 VCKMCTSGKTNLCSAVRETQGkglmpdgttrFYKDGepiyhymGCstfSEYTVLPEISLAKVNKEAPLEEVCLLGCGVTT 178
Cdd:cd08239    92 ACRNCRRGWMQLCTSKRAAYG----------WNRDG-------GH---AEYMLVPEKTLIPLPDDLSFADGALLLCGIGT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 179 GMGAVMNtAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKDYDkpiQDVIVELT 258
Cdd:cd08239   152 AYHALRR-VGVSGRDTVLVVGAGPVGLGALMLARALGAEDVIGVDPSPERLELAKALGADFVINSGQDD---VQEIRELT 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 259 DG-GVDYSFECIGNVDVMRSALECCHKgWGESVIIGVaGAGQEISTRPFQLVTGRVWRGSAFGGVKGRSELPGYVERYLa 337
Cdd:cd08239   228 SGaGADVAIECSGNTAARRLALEAVRP-WGRLVLVGE-GGELTIEVSNDLIRKQRTLIGSWYFSVPDMEECAEFLARHK- 304
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2539978014 338 gdIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIHF 374
Cdd:cd08239   305 --LEVDRLVTHRFGLDQAPEAYALFAQGESGKVVFVF 339
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
7-372 9.52e-49

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: 167.79  E-value: 9.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   7 KSKAAIAWGpnQPLSIEEVDVMLPRKGEVLVKIIASGVCHTD------------AFTLSGEDPEGVFPAILGHEGGGIVE 74
Cdd:cd08240     2 KAAAVVEPG--KPLEEVEIDTPKPPGTEVLVKVTACGVCHSDlhiwdggydlggGKTMSLDDRGVKLPLVLGHEIVGEVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  75 QIGEGVTSVQVGDHVIPLYTAECGVCKMCTSGKTNLCSAVRETqgkGLMPDGTtrfykdgepiyhymgcstFSEYTVLPE 154
Cdd:cd08240    80 AVGPDAADVKVGDKVLVYPWIGCGECPVCLAGDENLCAKGRAL---GIFQDGG------------------YAEYVIVPH 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 155 ISLAKVNKEAPLEEVCLLGC-GVTTgMGAVMNTAKVEEGATVAIFGLGGIGLSAVigaQMAKA---SRIIAIDINESKFE 230
Cdd:cd08240   139 SRYLVDPGGLDPALAATLACsGLTA-YSAVKKLMPLVADEPVVIIGAGGLGLMAL---ALLKAlgpANIIVVDIDEAKLE 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 231 LAKKLGATDCINPKDYDKPIQdvIVELTDGGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEISTrPFQLVT 310
Cdd:cd08240   215 AAKAAGADVVVNGSDPDAAKR--IIKAAGGGVDAVIDFVNNSATASLAFDILAKG-GKLVLVGLFGGEATLPL-PLLPLR 290
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2539978014 311 GRVWRGSAFGGVKGRSELPGYVERYLAGDIPLQdfithTMPLEDINEAFDLMHKGESI-RTVI 372
Cdd:cd08240   291 ALTIQGSYVGSLEELRELVALAKAGKLKPIPLT-----ERPLSDVNDALDDLKAGKVVgRAVL 348
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
15-373 3.23e-48

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: 166.13  E-value: 3.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  15 GPNQpLSIEEVDVMLPRKGEVLVKIIASGVCHTDA-FTLSGedPEGVF----PAILGHEGGGIVEQIGEGVTSVQVGDHV 89
Cdd:cd05285     6 GPGD-LRLEERPIPEPGPGEVLVRVRAVGICGSDVhYYKHG--RIGDFvvkePMVLGHESAGTVVAVGSGVTHLKVGDRV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  90 -----IPlytaeCGVCKMCTSGKTNLCSAVRetqgkglmpdgttrFYkdGEPIYHymGcsTFSEYTVLPEISLAKVNKEA 164
Cdd:cd05285    83 aiepgVP-----CRTCEFCKSGRYNLCPDMR--------------FA--ATPPVD--G--TLCRYVNHPADFCHKLPDNV 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 165 PLEE--------VCLLGCgvttgmgavmNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLG 236
Cdd:cd05285   138 SLEEgalveplsVGVHAC----------RRAGVRPGDTVLVFGAGPIGLLTAAVAKAFGATKVVVTDIDPSRLEFAKELG 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 237 ATDCINPKDYDKP-IQDVIVELTDG-GVDYSFECIGNVDVMRSALECCHKGwGESVIIGVagaGQEISTRPFQLVTGR-- 312
Cdd:cd05285   208 ATHTVNVRTEDTPeSAEKIAELLGGkGPDVVIECTGAESCIQTAIYATRPG-GTVVLVGM---GKPEVTLPLSAASLRei 283
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2539978014 313 ----VWRgsafggvkgrselpgYVERY------LA-GDIPLQDFITHTMPLEDINEAFDLMHKG--ESIRTVIH 373
Cdd:cd05285   284 dirgVFR---------------YANTYptaielLAsGKVDVKPLITHRFPLEDAVEAFETAAKGkkGVIKVVIE 342
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
11-372 1.12e-45

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: 159.73  E-value: 1.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  11 AIAWgpNQPLSIEEVDVMLPR---KGEVLVKIIASGVCHTDAFTLSGEDPEGVfPAILGHEGGGIVEQIGEGVTSVQVGD 87
Cdd:cd08284     3 AVVF--KGPGDVRVEEVPIPQiqdPTDAIVKVTAAAICGSDLHIYRGHIPSTP-GFVLGHEFVGEVVEVGPEVRTLKVGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  88 HVIPLYTAECGVCKMCTSGKTNLCsavreTQGKGLMPDGTTRfykdgepiyhYMGCStfSEYTVLP--EISLAKVNKEAP 165
Cdd:cd08284    80 RVVSPFTIACGECFYCRRGQSGRC-----AKGGLFGYAGSPN----------LDGAQ--AEYVRVPfaDGTLLKLPDGLS 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 166 LEEVCLLGCGVTTGMGAVMNtAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATdCINPKD 245
Cdd:cd08284   143 DEAALLLGDILPTGYFGAKR-AQVRPGDTVAVIGCGPVGLCAVLSAQVLGAARVFAVDPVPERLERAAALGAE-PINFED 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 246 yDKPIQDVIvELTDG-GVDYSFECIGNVDVMRSALECCHKgWGESVIIGVAGAgQEIstrPFQL-------VTGRVWRGS 317
Cdd:cd08284   221 -AEPVERVR-EATEGrGADVVLEAVGGAAALDLAFDLVRP-GGVISSVGVHTA-EEF---PFPGldaynknLTLRFGRCP 293
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2539978014 318 AfggvkgRSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVI 372
Cdd:cd08284   294 V------RSLFPELLPLLESGRLDLEFLIDHRMPLEEAPEAYRLFDKRKVLKVVL 342
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
9-366 1.39e-45

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: 159.02  E-value: 1.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDH 88
Cdd:cd08245     1 KAAVVHAAGGPLEPEEVPVPEPGPGEVLIKIEACGVCHTDLHAAEGDWGGSKYPLVPGHEIVGEVVEVGAGVEGRKVGDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 V-IPLYTAECGVCKMCTSGKTNLCSAVRETQgkglmpdgttrfykdgepiYHYMGcsTFSEYTVLPEISLAKVNKEAPLE 167
Cdd:cd08245    81 VgVGWLVGSCGRCEYCRRGLENLCQKAVNTG-------------------YTTQG--GYAEYMVADAEYTVLLPDGLPLA 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 168 EVCLLGC-GVTTGMGAVMNTAKveEGATVAIFGLGGIGLSAVigaQMAKA--SRIIAIDINESKFELAKKLGATDCINPK 244
Cdd:cd08245   140 QAAPLLCaGITVYSALRDAGPR--PGERVAVLGIGGLGHLAV---QYARAmgFETVAITRSPDKRELARKLGADEVVDSG 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 245 DYDKpiqdviVELTDGGVDYSFECIGNVDVMRSALECCHKGwGESVIIGvAGAGQEISTRPFQLVTGRVW-RGSAFGGVK 323
Cdd:cd08245   215 AELD------EQAAAGGADVILVTVVSGAAAEAALGGLRRG-GRIVLVG-LPESPPFSPDIFPLIMKRQSiAGSTHGGRA 286
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2539978014 324 GRSELPGYVERylaGDIPLqdfITHTMPLEDINEAFDLMHKGE 366
Cdd:cd08245   287 DLQEALDFAAE---GKVKP---MIETFPLDQANEAYERMEKGD 323
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
11-361 9.93e-44

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: 155.77  E-value: 9.93e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  11 AIAW-GPNQpLSIEEV-DVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDH 88
Cdd:cd08283     3 ALVWhGKGD-VRVEEVpDPKIEDPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGPEVRNLKVGDR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 VIPLYTAECGVCKMCTSGKTNLCSavretqgkglmpdgTTRFYKDGEPIYHYMGCSTF-------------SEYTVLP-- 153
Cdd:cd08283    82 VVVPFTIACGECFYCKRGLYSQCD--------------NTNPSAEMAKLYGHAGAGIFgyshltggyaggqAEYVRVPfa 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 154 EISLAKVNKEAPLEEVCLLGCGVTTG-MGAVMntAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELA 232
Cdd:cd08283   148 DVGPFKIPDDLSDEKALFLSDILPTGyHAAEL--AEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 233 KKLGATDCINPKDYDKPIqDVIVELTDG-GVDYSFECIG---------------------NVDVMRSALECCHKGwGESV 290
Cdd:cd08283   226 RSHLGAETINFEEVDDVV-EALRELTGGrGPDVCIDAVGmeahgsplhkaeqallkletdRPDALREAIQAVRKG-GTVS 303
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2539978014 291 IIGVAGAGqeisTRPFQLvtgrvwrGSAF--------GGVKGRSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDL 361
Cdd:cd08283   304 IIGVYGGT----VNKFPI-------GAAMnkgltlrmGQTHVQRYLPRLLELIESGELDPSFIITHRLPLEDAPEAYKI 371
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
9-372 1.77e-43

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: 153.55  E-value: 1.77e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDH 88
Cdd:cd08296     2 KAVQVTEPGGPLELVERDVPLPGPGEVLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVGEGVSRWKVGDR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 V-IPLYTAECGVCKMCTSGKTNLCSAVRETqgkglmpdGTTRfykDGepiyhymgcsTFSEYTVLPEISLAKVNKEAPLE 167
Cdd:cd08296    82 VgVGWHGGHCGTCDACRRGDFVHCENGKVT--------GVTR---DG----------GYAEYMLAPAEALARIPDDLDAA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 168 EVCLLGC-GVTTgMGAVMNTaKVEEGATVAIFGLGGIGLSAVigaQMAKAS--RIIAIDINESKFELAKKLGATDCINPK 244
Cdd:cd08296   141 EAAPLLCaGVTT-FNALRNS-GAKPGDLVAVQGIGGLGHLAV---QYAAKMgfRTVAISRGSDKADLARKLGAHHYIDTS 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 245 DydkpiQDVIVELTD-GGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEIStrPFQLVTGRvwrgsafGGVK 323
Cdd:cd08296   216 K-----EDVAEALQElGGAKLILATAPNAKAISALVGGLAPR-GKLLILGAAGEPVAVS--PLQLIMGR-------KSIH 280
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2539978014 324 GrselpgyverYLAGDIP----------LQDF--ITHTMPLEDINEAFDLMHKGES-IRTVI 372
Cdd:cd08296   281 G----------WPSGTALdsedtlkfsaLHGVrpMVETFPLEKANEAYDRMMSGKArFRVVL 332
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
9-374 5.72e-42

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: 150.08  E-value: 5.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQPlSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDH 88
Cdd:cd08285     2 KAFAMLGIGKV-GWIEKPIPVCGPNDAIVRPTAVAPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGSEVKDFKPGDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 VIplytaecgVCKMCTSGKTNLCSAVRETQGKGLMpdGTTRF--YKDGepiyhymgcsTFSEYTVLPE--ISLAKVNKEA 164
Cdd:cd08285    81 VI--------VPAITPDWRSVAAQRGYPSQSGGML--GGWKFsnFKDG----------VFAEYFHVNDadANLAPLPDGL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 165 PLEEVCLLGCGVTTGMGAVMNtAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPK 244
Cdd:cd08285   141 TDEQAVMLPDMMSTGFHGAEL-ANIKLGDTVAVFGIGPVGLMAVAGARLRGAGRIIAVGSRPNRVELAKEYGATDIVDYK 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 245 DYDkpIQDVIVELTDG-GVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEIstrPFQLVtgrVWrGSAFGGVK 323
Cdd:cd08285   220 NGD--VVEQILKLTGGkGVDAVIIAGGGQDTFEQALKVLKPG-GTISNVNYYGEDDYL---PIPRE---EW-GVGMGHKT 289
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2539978014 324 GRSEL-PG---YVERYLA----GDIPLQDFITH-TMPLEDINEAFDLMHKGES--IRTVIHF 374
Cdd:cd08285   290 INGGLcPGgrlRMERLASlieyGRVDPSKLLTHhFFGFDDIEEALMLMKDKPDdlIKPVIIF 351
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
9-372 1.75e-40

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: 145.91  E-value: 1.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQpLSIEEV-DVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEgVFPAILGHEGGGIVEQIGEGVTSVQVGD 87
Cdd:cd08287     2 RATVIHGPGD-IRVEEVpDPVIEEPTDAVIRVVATCVCGSDLWPYRGVSPT-RAPAPIGHEFVGVVEEVGSEVTSVKPGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  88 HVIPLYTAECGVCKMCTSGKTNLCSAVretQGKGLMPDGttrfykdgepiyhYMGcstfsEYTVLPEI--SLAKVNKEAP 165
Cdd:cd08287    80 FVIAPFAISDGTCPFCRAGFTTSCVHG---GFWGAFVDG-------------GQG-----EYVRVPLAdgTLVKVPGSPS 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 166 LEEVCL-----LGCGVTTGMGAVMnTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDC 240
Cdd:cd08287   139 DDEDLLpsllaLSDVMGTGHHAAV-SAGVRPGSTVVVVGDGAVGLCAVLAAKRLGAERIIAMSRHEDRQALAREFGATDI 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 241 INPKDYDKPiqDVIVELTDG-GVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEISTRP--FQLVTgrvWRGs 317
Cdd:cd08287   218 VAERGEEAV--ARVRELTGGvGADAVLECVGTQESMEQAIAIARPG-GRVGYVGVPHGGVELDVRElfFRNVG---LAG- 290
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2539978014 318 afGGVKGRSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVI 372
Cdd:cd08287   291 --GPAPVRRYLPELLDDVLAGRINPGRVFDLTLPLDEVAEGYRAMDERRAIKVLL 343
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
9-360 4.71e-40

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: 144.70  E-value: 4.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQpLSIEEVD---VMLPrkGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQV 85
Cdd:cd08286     2 KALVYHGPGK-ISWEDRPkptIQEP--TDAIVKMLKTTICGTDLHILKGDVPTVTPGRILGHEGVGVVEEVGSAVTNFKV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  86 GDHVIPLYTAECGVCKMCTSGKTNLCsavrETQG--KGLMPDGTTrfykdgepiyhymgcstfSEYTVLP--EISLAKVN 161
Cdd:cd08286    79 GDRVLISCISSCGTCGYCRKGLYSHC----ESGGwiLGNLIDGTQ------------------AEYVRIPhaDNSLYKLP 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 162 KEAPLEEVCLLGCGVTTGM-GAVMNtAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDC 240
Cdd:cd08286   137 EGVDEEAAVMLSDILPTGYeCGVLN-GKVKPGDTVAIVGAGPVGLAALLTAQLYSPSKIIMVDLDDNRLEVAKKLGATHT 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 241 INPKDYDkpIQDVIVELTDG-GVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQE------------ISTRPFQ 307
Cdd:cd08286   216 VNSAKGD--AIEQVLELTDGrGVDVVIEAVGIPATFELCQELVAPG-GHIANVGVHGKPVDlhleklwiknitITTGLVD 292
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2539978014 308 LVTgrvwrgsafggvkgrseLPGYVERYLAGDIPLQDFITHTMPLEDINEAFD 360
Cdd:cd08286   293 TNT-----------------TPMLLKLVSSGKLDPSKLVTHRFKLSEIEKAYD 328
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
15-374 1.06e-39

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 143.36  E-value: 1.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  15 GPNQpLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGV-FPAILGHEGGGIVEQIGEGVTSVQVGDHVIply 93
Cdd:COG0604    11 GPEV-LELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPLPPgLPFIPGSDAAGVVVAVGEGVTGFKVGDRVA--- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  94 taecgvckmctsgktnlcsavretqgkGLMPDGTtrfykdgepiyhymgcstFSEYTVLPEISLAKVNKEAPLEEVCLLG 173
Cdd:COG0604    87 ---------------------------GLGRGGG------------------YAEYVVVPADQLVPLPDGLSFEEAAALP 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 174 CGVTTGMGAVMNTAKVEEGATVAIFG-LGGIGLSAVigaQMAKAS--RIIAIDINESKFELAKKLGATDCINPKDYDkpI 250
Cdd:COG0604   122 LAGLTAWQALFDRGRLKPGETVLVHGaAGGVGSAAV---QLAKALgaRVIATASSPEKAELLRALGADHVIDYREED--F 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 251 QDVIVELTDG-GVDYSFECIGNvDVMRSALECCHKGwGESVIIGVA-GAGQEISTRPFqLVTGRVWRGSAFGGVKG---R 325
Cdd:COG0604   197 AERVRALTGGrGVDVVLDTVGG-DTLARSLRALAPG-GRLVSIGAAsGAPPPLDLAPL-LLKGLTLTGFTLFARDPaerR 273
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2539978014 326 SELPGYVERYLAGDIPLQdfITHTMPLEDINEAFDLMHKGESI-RTVIHF 374
Cdd:COG0604   274 AALAELARLLAAGKLRPV--IDRVFPLEEAAEAHRLLESGKHRgKVVLTV 321
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
20-367 1.40e-39

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 143.43  E-value: 1.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  20 LSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGED-PEGVFPA--ILGHEGGGIVEQIGEGVTSVQVGDHViplyTAE 96
Cdd:PRK05396   13 LWLTDVPVPEPGPNDVLIKVKKTAICGTDVHIYNWDEwAQKTIPVpmVVGHEFVGEVVEVGSEVTGFKVGDRV----SGE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  97 ----CGVCKMCTSGKTNLCsavRETQGKGLMPDGttrfykdgepiyhymgcsTFSEYTVLPEISLAKVNKEAPLEEVCL- 171
Cdd:PRK05396   89 ghivCGHCRNCRAGRRHLC---RNTKGVGVNRPG------------------AFAEYLVIPAFNVWKIPDDIPDDLAAIf 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 172 --LGCGVTTgmgaVMNTAKVeeGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKDYDkp 249
Cdd:PRK05396  148 dpFGNAVHT----ALSFDLV--GEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELARKMGATRAVNVAKED-- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 250 IQDVIVELTDG-GVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEIStrpFQLVtgrVWRGSAFGGVKGRsel 328
Cdd:PRK05396  220 LRDVMAELGMTeGFDVGLEMSGAPSAFRQMLDNMNHG-GRIAMLGIPPGDMAID---WNKV---IFKGLTIKGIYGR--- 289
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2539978014 329 pgyvERY---------LAGDIPLQDFITHTMPLEDINEAFDLMHKGES 367
Cdd:PRK05396  290 ----EMFetwykmsalLQSGLDLSPIITHRFPIDDFQKGFEAMRSGQS 333
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
9-270 4.26e-39

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 142.10  E-value: 4.26e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDH 88
Cdd:PRK13771    2 KAVILPGFKQGYRIEEVPDPKPGKDEVVIKVNYAGLCYRDLLQLQGFYPRMKYPVILGHEVVGTVEEVGENVKGFKPGDR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 VIPLYTAECGVCKMCTSGKTNLCsavRETQGKGLMPDGttrfykdgepiyhymgcsTFSEYTVLPEISLAKVNKEAPLEE 168
Cdd:PRK13771   82 VASLLYAPDGTCEYCRSGEEAYC---KNRLGYGEELDG------------------FFAEYAKVKVTSLVKVPPNVSDEG 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 169 VCLLGCgVTTGMGAVMNTAKVEEGATVAIFGL-GGIGLSAVigaQMAKA--SRIIAIDINESKFELAKKLgATDCINPKD 245
Cdd:PRK13771  141 AVIVPC-VTGMVYRGLRRAGVKKGETVLVTGAgGGVGIHAI---QVAKAlgAKVIAVTSSESKAKIVSKY-ADYVIVGSK 215
                         250       260
                  ....*....|....*....|....*
gi 2539978014 246 YDKPIQDViveltdGGVDYSFECIG 270
Cdd:PRK13771  216 FSEEVKKI------GGADIVIETVG 234
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
17-366 1.57e-38

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


Pssm-ID: 176258 [Multi-domain]  Cd Length: 329  Bit Score: 140.40  E-value: 1.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  17 NQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDHV--IPLYT 94
Cdd:cd08298    14 ENPLRLTEVPVPEPGPGEVLIKVEACGVCRTDLHIVEGDLPPPKLPLIPGHEIVGRVEAVGPGVTRFSVGDRVgvPWLGS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  95 AeCGVCKMCTSGKTNLCSAVRETqgkglmpdGTTRfykDGepiyhymgcsTFSEYTVLPEISLAKVNKEAPLEEVCLLGC 174
Cdd:cd08298    94 T-CGECRYCRSGRENLCDNARFT--------GYTV---DG----------GYAEYMVADERFAYPIPEDYDDEEAAPLLC 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 175 GVTTGMGAVMnTAKVEEGATVAIFGLGGiglSAVIGAQMAKA--SRIIAIDINESKFELAKKLGATDCINPKDY-DKPIQ 251
Cdd:cd08298   152 AGIIGYRALK-LAGLKPGQRLGLYGFGA---SAHLALQIARYqgAEVFAFTRSGEHQELARELGADWAGDSDDLpPEPLD 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 252 DVIVeltdggvdysFECIGnvDVMRSALECCHKgwGESVIIGVAGaGQEISTRPFQLVTG-RVWRGSAFGGVK-GRSELP 329
Cdd:cd08298   228 AAII----------FAPVG--ALVPAALRAVKK--GGRVVLAGIH-MSDIPAFDYELLWGeKTIRSVANLTRQdGEEFLK 292
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2539978014 330 gyveryLAGDIPLQDfITHTMPLEDINEAFDLMHKGE 366
Cdd:cd08298   293 ------LAAEIPIKP-EVETYPLEEANEALQDLKEGR 322
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
8-293 2.33e-38

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: 139.37  E-value: 2.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   8 SKAAIAWGPnQPLSIE--EVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQV 85
Cdd:cd08258     1 MKALVKTGP-GPGNVElrEVPEPEPGPGEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEVGPDVEGWKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  86 GDHVIPLYTAE-CGVCKMCTSGKTNLCSavrETQGKGLMPDGttrfykdgepiyhymgcsTFSEYTVLPEISLAKVNKEA 164
Cdd:cd08258    80 GDRVVSETTFStCGRCPYCRRGDYNLCP---HRKGIGTQADG------------------GFAEYVLVPEESLHELPENL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 165 PLEEVCL---LGCGVTtgmgAVMNTAKVEEGATVAIFGLGGIGLSAvigAQMAKAS----RIIAIDINESKFELAKKLGA 237
Cdd:cd08258   139 SLEAAALtepLAVAVH----AVAERSGIRPGDTVVVFGPGPIGLLA---AQVAKLQgatvVVVGTEKDEVRLDVAKELGA 211
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2539978014 238 TDC----INPKDYDKpiqdvivELTDG-GVDYSFECIGNVDVMRSALECCHKGwGESVIIG 293
Cdd:cd08258   212 DAVnggeEDLAELVN-------EITDGdGADVVIECSGAVPALEQALELLRKG-GRIVQVG 264
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
20-374 3.59e-37

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: 136.98  E-value: 3.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  20 LSIEEVDVMLPRKGEVLVKIIASGVChtdaftlsGED----PEGVF-------PAILGHEGGGIVEQIGEGVTSVQVGDH 88
Cdd:cd08232     9 LRVEERPAPEPGPGEVRVRVAAGGIC--------GSDlhyyQHGGFgtvrlrePMVLGHEVSGVVEAVGPGVTGLAPGQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 VIPLYTAECGVCKMCTSGKTNLCSAVRetqgkglmpdgttrFYKDGEPIYHYMGcsTFSEYTVLPEISLAKVNKEAPLEE 168
Cdd:cd08232    81 VAVNPSRPCGTCDYCRAGRPNLCLNMR--------------FLGSAMRFPHVQG--GFREYLVVDASQCVPLPDGLSLRR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 169 --------VCLLGCgvttgmgavmNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDC 240
Cdd:cd08232   145 aalaeplaVALHAV----------NRAGDLAGKRVLVTGAGPIGALVVAAARRAGAAEIVATDLADAPLAVARAMGADET 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 241 INPKDYDKPIQdvivELTDGGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEIstrPFQLVTGR--VWRGS- 317
Cdd:cd08232   215 VNLARDPLAAY----AADKGDFDVVFEASGAPAALASALRVVRPG-GTVVQVGMLGGPVPL---PLNALVAKelDLRGSf 286
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2539978014 318 AFGgvkgrSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLM-HKGESIRTVIHF 374
Cdd:cd08232   287 RFD-----DEFAEAVRLLAAGRIDVRPLITAVFPLEEAAEAFALAaDRTRSVKVQLSF 339
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
16-365 4.28e-36

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: 134.16  E-value: 4.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  16 PNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDHVIPLYTA 95
Cdd:cd05283     8 ASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDRVGVGCQV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  96 E-CGVCKMCTSGKTNLCSAvretqgkglMPDGTTRFYKDGEPiyHYMGcstFSEYTVLPEISLAKVNKEAPLEEVC-LLG 173
Cdd:cd05283    88 DsCGTCEQCKSGEEQYCPK---------GVVTYNGKYPDGTI--TQGG---YADHIVVDERFVFKIPEGLDSAAAApLLC 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 174 CGVTTgmGAVMNTAKVEEGATVAIFGLGGIGlsaVIGAQMAKA--SRIIAIDINESKFELAKKLGATDCINPKD------ 245
Cdd:cd05283   154 AGITV--YSPLKRNGVGPGKRVGVVGIGGLG---HLAVKFAKAlgAEVTAFSRSPSKKEDALKLGADEFIATKDpeamkk 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 246 YDKPIqDVIVELTDGGVDYSFEcignVDVMRSAlecchkgwGESVIIGVAGAGQEIStrPFQLVTGR--VWrGSAFGGVK 323
Cdd:cd05283   229 AAGSL-DLIIDTVSASHDLDPY----LSLLKPG--------GTLVLVGAPEEPLPVP--PFPLIFGRksVA-GSLIGGRK 292
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2539978014 324 GRSELpgyveryLagdiplqDF--------ITHTMPLEDINEAFDLMHKG 365
Cdd:cd05283   293 ETQEM-------L-------DFaaehgikpWVEVIPMDGINEALERLEKG 328
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
9-366 1.19e-35

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


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 133.15  E-value: 1.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAI--AWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGV-FPAILGHEGGGIVEQIGEGVTSVQV 85
Cdd:cd08266     2 KAVVirGHGGPEVLEYGDLPEPEPGPDEVLVRVKAAALNHLDLWVRRGMPGIKLpLPHILGSDGAGVVEAVGPGVTNVKP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  86 GDHVIPLYTAECGVCKMCTSGKTNLCsAVRETQGkglmpdgttrFYKDGepiyhymgcsTFSEYTVLPEISLAKVNKEAP 165
Cdd:cd08266    82 GQRVVIYPGISCGRCEYCLAGRENLC-AQYGILG----------EHVDG----------GYAEYVAVPARNLLPIPDNLS 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 166 LEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGLG-GIGLSAVigaQMAKA--SRIIAIDINESKFELAKKLGATDCIN 242
Cdd:cd08266   141 FEEAAAAPLTFLTAWHMLVTRARLRPGETVLVHGAGsGVGSAAI---QIAKLfgATVIATAGSEDKLERAKELGADYVID 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 243 PKDYDKPiqDVIVELTDG-GVDYSFECIGNvDVMRSALECCHKGwGESVIIGvAGAGQEISTrPFQLVTGRVWR--GSaF 319
Cdd:cd08266   218 YRKEDFV--REVRELTGKrGVDVVVEHVGA-ATWEKSLKSLARG-GRLVTCG-ATTGYEAPI-DLRHVFWRQLSilGS-T 290
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2539978014 320 GGVKGR-SELPGYVERylaGDIplQDFITHTMPLEDINEAFDLMHKGE 366
Cdd:cd08266   291 MGTKAElDEALRLVFR---GKL--KPVIDSVFPLEEAAEAHRRLESRE 333
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
9-374 1.17e-34

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 130.15  E-value: 1.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGE--DPEGVfpaILGHEGGGIVEQIGEGVTSVQVG 86
Cdd:PRK09422    2 KAAVVNKDHTGDVVVEKTLRPLKHGEALVKMEYCGVCHTDLHVANGDfgDKTGR---ILGHEGIGIVKEVGPGVTSLKVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  87 DHV-IPLYTAECGVCKMCTSGKTNLCsavRETQGKGLMPDGTtrfykdgepiyhyMG--CSTFSEYTV-LPEislakvnK 162
Cdd:PRK09422   79 DRVsIAWFFEGCGHCEYCTTGRETLC---RSVKNAGYTVDGG-------------MAeqCIVTADYAVkVPE-------G 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 163 EAPLEEVCLLGCGVTTgMGAVmNTAKVEEGATVAIFGLGGIGLSAVigaQMAK---ASRIIAIDINESKFELAKKLGATD 239
Cdd:PRK09422  136 LDPAQASSITCAGVTT-YKAI-KVSGIKPGQWIAIYGAGGLGNLAL---QYAKnvfNAKVIAVDINDDKLALAKEVGADL 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 240 CINPKDYDkpiqDV--IVELTDGGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEISTrPFQLVTGRVWRGS 317
Cdd:PRK09422  211 TINSKRVE----DVakIIQEKTGGAHAAVVTAVAKAAFNQAVDAVRAG-GRVVAVGLPPESMDLSI-PRLVLDGIEVVGS 284
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2539978014 318 AFGgvkGRSELPGYVERYLAGDI-PlqdfITHTMPLEDINEAFDLMHKGE-SIRTVIHF 374
Cdd:PRK09422  285 LVG---TRQDLEEAFQFGAEGKVvP----KVQLRPLEDINDIFDEMEQGKiQGRMVIDF 336
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
20-373 8.54e-34

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: 128.79  E-value: 8.54e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  20 LSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSgEDPEGV--------FPAILGHEGGGIVEQIGEGVTSVQVGDHVip 91
Cdd:cd08265    39 LRVEDVPVPNLKPDEILIRVKACGICGSDIHLYE-TDKDGYilypglteFPVVIGHEFSGVVEKTGKNVKNFEKGDPV-- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  92 lyTAE----CGVCKMCTSGKTNLCSAVRETqgkGLMPDGTtrfykdgepiyhymgcstFSEYTVLPE------ISLAKVN 161
Cdd:cd08265   116 --TAEemmwCGMCRACRSGSPNHCKNLKEL---GFSADGA------------------FAEYIAVNAryaweiNELREIY 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 162 KEAPLEEVCLLGCGVTTGMGAVMNTAK-VEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDC 240
Cdd:cd08265   173 SEDKAFEAGALVEPTSVAYNGLFIRGGgFRPGAYVVVYGAGPIGLAAIALAKAAGASKVIAFEISEERRNLAKEMGADYV 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 241 INP-KDYDKPIQDVIVELTDG-GVDYSFECIGNVDVMRSALEcchkgwgESVIIG--VAGAGQEISTRPFQLVTGRVWRG 316
Cdd:cd08265   253 FNPtKMRDCLSGEKVMEVTKGwGADIQVEAAGAPPATIPQME-------KSIAINgkIVYIGRAATTVPLHLEVLQVRRA 325
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2539978014 317 SAFG--GVKGRSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGESIRTVIH 373
Cdd:cd08265   326 QIVGaqGHSGHGIFPSVIKLMASGKIDMTKIITARFPLEGIMEAIKAASERTDGKITIL 384
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
15-365 9.62e-33

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: 124.39  E-value: 9.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  15 GPNQpLSIEEVDVMLPRKGEVLVKIIASGVCHTDafTLSGEDPEGVF-----PAILGHEGGGIVEQIGEGVTSVQVGDHV 89
Cdd:cd08269     3 GPGR-FEVEEHPRPTPGPGQVLVRVEGCGVCGSD--LPAFNQGRPWFvypaePGGPGHEGWGRVVALGPGVRGLAVGDRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  90 IPLytaecgvckmctsgktnlcsavretqgkglmpdgttrfykdgepiyhymGCSTFSEYTVLPEISLAKVNKEA----- 164
Cdd:cd08269    80 AGL-------------------------------------------------SGGAFAEYDLADADHAVPLPSLLdgqaf 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 165 PLEEvclLGCGVTtgmgaVMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINpk 244
Cdd:cd08269   111 PGEP---LGCALN-----VFRRGWIRAGKTVAVIGAGFIGLLFLQLAAAAGARRVIAIDRRPARLALARELGATEVVT-- 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 245 DYDKPIQDVIVELTDG-GVDYSFECIGNVDVMRSALECChkgwGESVIIGVAGAGQ-EISTRPFQLVTgrvWRGSAF-GG 321
Cdd:cd08269   181 DDSEAIVERVRELTGGaGADVVIEAVGHQWPLDLAGELV----AERGRLVIFGYHQdGPRPVPFQTWN---WKGIDLiNA 253
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2539978014 322 VKGRSE-----LPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKG 365
Cdd:cd08269   254 VERDPRiglegMREAVKLIADGRLDLGSLLTHEFPLEELGDAFEAARRR 302
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
9-365 1.06e-32

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: 124.21  E-value: 1.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAI--AWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSG---EDPEGVFPAILGHEGGGIVEQIGEGVTSV 83
Cdd:cd05289     2 KAVRihEYGGPEVLELADVPTPEPGPGEVLVKVHAAGVNPVDLKIREGllkAAFPLTLPLIPGHDVAGVVVAVGPGVTGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  84 QVGDHVIplytaecgvckmctsgktnlcsavretqgkglmpdGTTRFYKDGepiyhymgcsTFSEYTVLPEISLAKVNKE 163
Cdd:cd05289    82 KVGDEVF-----------------------------------GMTPFTRGG----------AYAEYVVVPADELALKPAN 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 164 APLEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFG-LGGIGLSAVigaQMAKA--SRIIAIdINESKFELAKKLGATDC 240
Cdd:cd05289   117 LSFEEAAALPLAGLTAWQALFELGGLKAGQTVLIHGaAGGVGSFAV---QLAKArgARVIAT-ASAANADFLRSLGADEV 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 241 InpkDYDKpiQDVIVELTDGGVDYSFECIGnVDVMRSALECCHKGwgeSVIIGVAGAGQEISTRPFQLVTGRVWRGSAFG 320
Cdd:cd05289   193 I---DYTK--GDFERAAAPGGVDAVLDTVG-GETLARSLALVKPG---GRLVSIAGPPPAEQAAKRRGVRAGFVFVEPDG 263
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 2539978014 321 gvKGRSELPGYVErylAGDIPLqdFITHTMPLEDINEAFDLMHKG 365
Cdd:cd05289   264 --EQLAELAELVE---AGKLRP--VVDRVFPLEDAAEAHERLESG 301
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
9-270 1.23e-32

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: 125.40  E-value: 1.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQpLSIEEVDVmlPRK---GEVLVKIIASGVCHTDAFTLsgedpEGVFPA----ILGHEGGGIVEQIGEGVT 81
Cdd:cd08282     2 KAVVYGGPGN-VAVEDVPD--PKIehpTDAIVRITTTAICGSDLHMY-----RGRTGAepglVLGHEAMGEVEEVGSAVE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  82 SVQVGDHVIPLYTAECGVCKMCTSGKTNLCSAVretqgkGLMPDGTTRFYKDGEPiyhYMGCStfSEYTVLP--EISLAK 159
Cdd:cd08282    74 SLKVGDRVVVPFNVACGRCRNCKRGLTGVCLTV------NPGRAGGAYGYVDMGP---YGGGQ--AEYLRVPyaDFNLLK 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 160 VNKEAPLEEVC---LLGCGVTTGMGAVMnTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLG 236
Cdd:cd08282   143 LPDRDGAKEKDdylMLSDIFPTGWHGLE-LAGVQPGDTVAVFGAGPVGLMAAYSAILRGASRVYVVDHVPERLDLAESIG 221
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2539978014 237 ATDcINPKDYDKPIQdvIVELTDGGVDYSFECIG 270
Cdd:cd08282   222 AIP-IDFSDGDPVEQ--ILGLEPGGVDRAVDCVG 252
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
9-372 1.62e-31

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: 122.13  E-value: 1.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPnQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGE-----DPEGV----FPAILGHEGGGIVEQIGEG 79
Cdd:cd08256     2 RAVVCHGP-QDYRLEEVPVPRPGPGEILVKVEACGICAGDIKCYHGApsfwgDENQPpyvkPPMIPGHEFVGRVVELGEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  80 VTS--VQVGDHVIPLYTAECGVCKMCTSGKTNLCSA------VRETQGkglmpdgttrfykdgepiyhymgcsTFSEYTV 151
Cdd:cd08256    81 AEErgVKVGDRVISEQIVPCWNCRFCNRGQYWMCQKhdlygfQNNVNG-------------------------GMAEYMR 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 152 LPEISLA-KVNKEAPLEEVCL---LGCGVTTgmgavMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINES 227
Cdd:cd08256   136 FPKEAIVhKVPDDIPPEDAILiepLACALHA-----VDRANIKFDDVVVLAGAGPLGLGMIGAARLKNPKKLIVLDLKDE 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 228 KFELAKKLGATDCINPKDYDKPIQdvIVELTDG-GVDYSFECIGNVDVMRSALECCHKgWGESVIIGVAGagqEISTRPF 306
Cdd:cd08256   211 RLALARKFGADVVLNPPEVDVVEK--IKELTGGyGCDIYIEATGHPSAVEQGLNMIRK-LGRFVEFSVFG---DPVTVDW 284
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 307 QLVTGRV---WRGSAFggvkGRSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGE-SIRTVI 372
Cdd:cd08256   285 SIIGDRKeldVLGSHL----GPYCYPIAIDLIASGRLPTDGIVTHQFPLEDFEEAFELMARGDdSIKVVL 350
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
9-366 3.28e-30

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: 118.07  E-value: 3.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPN-QPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPeGVFPAILGHEGGGIVEQIGEGVTSVQVGD 87
Cdd:cd08249     2 KAAVLTGPGgGLLVVVDVPVPKPGPDEVLVKVKAVALNPVDWKHQDYGFI-PSYPAILGCDFAGTVVEVGSGVTRFKVGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  88 HViplytaeCGVCKMctsgktnlcsavretqgkglmpdGTTRFYKDGepiyhymgcsTFSEYTVLPEISLAKVNKEAPLE 167
Cdd:cd08249    81 RV-------AGFVHG-----------------------GNPNDPRNG----------AFQEYVVADADLTAKIPDNISFE 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 168 EVCLLGCGVTT-GMG---------AVMNTAKVEEGATVAIFGlggiGLSAV--IGAQMAKAS--RIIAIdINESKFELAK 233
Cdd:cd08249   121 EAATLPVGLVTaALAlfqklglplPPPKPSPASKGKPVLIWG----GSSSVgtLAIQLAKLAgyKVITT-ASPKNFDLVK 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 234 KLGATDCInpkDY-DKPIQDVIVELTDGGVDYSFECIGNVDVMRSALEcchkgwgesvIIGVAGAGQEISTRPFQLVTGR 312
Cdd:cd08249   196 SLGADAVF---DYhDPDVVEDIRAATGGKLRYALDCISTPESAQLCAE----------ALGRSGGGKLVSLLPVPEETEP 262
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2539978014 313 --------VWRGSAFGGVKGRSELPGYVERYLAGDIPLQDFITHTMP-----LEDINEAFDLMHKGE 366
Cdd:cd08249   263 rkgvkvkfVLGYTVFGEIPEDREFGEVFWKYLPELLEEGKLKPHPVRvveggLEGVQEGLDLLRKGK 329
dearomat_had TIGR03201
6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase; Members of this protein family are ...
15-372 4.13e-29

6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase; Members of this protein family are 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase, an enzyme in the anaerobic metabolism of aromatic enzymes by way of benzoyl-CoA, as seen in Thauera aromatica, Geobacter metallireducens, and Azoarcus sp. The experimentally characterized form from T. aromatica uses only NAD+, not NADP+. Note that Rhodopseudomonas palustris uses a different pathway to perform a similar degradation of benzoyl-CoA to 3-hydroxpimelyl-CoA.


Pssm-ID: 132245 [Multi-domain]  Cd Length: 349  Bit Score: 115.39  E-value: 4.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  15 GPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTD-AFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVqVGDHVIPLY 93
Cdd:TIGR03201   6 EPGKPMVKTRVEIPELGAGDVVVKVAGCGVCHTDlSYYYMGVRTNHALPLALGHEISGRVIQAGAGAASW-IGKAVIVPA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  94 TAECGVCKMCTSGKTNLCSAVRetqgkglMPDGTTRfykdgepiyhymgcSTFSEYTVLPEISLAKVNKEA------PLE 167
Cdd:TIGR03201  85 VIPCGECELCKTGRGTICRAQK-------MPGNDMQ--------------GGFASHIVVPAKGLCVVDEARlaaaglPLE 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 168 EVCLLGCGVTTGMGAVMNtAKVEEGATVAIFGLGGIGLSAVigaQMAKA--SRIIAIDINESKFELAKKLGATDCINPKD 245
Cdd:TIGR03201 144 HVSVVADAVTTPYQAAVQ-AGLKKGDLVIVIGAGGVGGYMV---QTAKAmgAAVVAIDIDPEKLEMMKGFGADLTLNPKD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 246 YD-KPIQDVI--------VELTDGGVdysFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEistrpFQLVTGRVWRG 316
Cdd:TIGR03201 220 KSaREVKKLIkafakargLRSTGWKI---FECSGSKPGQESALSLLSHG-GTLVVVGYTMAKTE-----YRLSNLMAFHA 290
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2539978014 317 SAFGGVKGRSEL-PGYVERYLAGDIPLQDFItHTMPLEDINEAFDLMHKGESIRTVI 372
Cdd:TIGR03201 291 RALGNWGCPPDRyPAALDLVLDGKIQLGPFV-ERRPLDQIEHVFAAAHHHKLKRRAI 346
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
202-337 1.17e-28

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 108.08  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 202 GIGLSAVigaQMAKAS--RIIAIDINESKFELAKKLGATDCINPKDYDkpIQDVIVELTDG-GVDYSFECIGNVDVMRSA 278
Cdd:pfam00107   1 GVGLAAI---QLAKAAgaKVIAVDGSEEKLELAKELGADHVINPKETD--LVEEIKELTGGkGVDVVFDCVGSPATLEQA 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2539978014 279 LECCHKGwGESVIIGVAGAGQEISTRPFqLVTGRVWRGSAFGgvkGRSELPGYVERYLA 337
Cdd:pfam00107  76 LKLLRPG-GRVVVVGLPGGPLPLPLAPL-LLKELTILGSFLG---SPEEFPEALDLLAS 129
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
33-159 2.31e-27

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: 103.84  E-value: 2.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  33 GEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDHVIPLYTAECGVCKMCTSGKTNLCS 112
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYNLCP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2539978014 113 AVRETqgkGLMPDGttrfykdgepiyhymgcsTFSEYTVLPEISLAK 159
Cdd:pfam08240  81 NGRFL---GYDRDG------------------GFAEYVVVPERNLVP 106
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
20-320 4.81e-26

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


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 106.85  E-value: 4.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  20 LSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGV-FPAILGHEGGGIVEQIGEGVTSVQVGDHVIPLYTAEcg 98
Cdd:cd08276    15 LKLVEEPVPEPGPGEVLVRVHAVSLNYRDLLILNGRYPPPVkDPLIPLSDGAGEVVAVGEGVTRFKVGDRVVPTFFPN-- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  99 vckmctsgktnlcsavretqgkglmpdgttrfYKDGEPIYHYMGCS-------TFSEYTVLPEISLAKVNKEAPLEEVCL 171
Cdd:cd08276    93 --------------------------------WLDGPPTAEDEASAlggpidgVLAEYVVLPEEGLVRAPDHLSFEEAAT 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 172 LGCGVTTGMGAVMNTAKVEEGATVAIFGLGGIGLSAvigAQMAKAS--RIIAIDINESKFELAKKLGATDCINPK---DY 246
Cdd:cd08276   141 LPCAGLTAWNALFGLGPLKPGDTVLVQGTGGVSLFA---LQFAKAAgaRVIATSSSDEKLERAKALGADHVINYRttpDW 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2539978014 247 DKPIQdvivELTDG-GVDYSFEcIGNVDVMRSALECCHKGwGESVIIGV-AGAGQEISTRPFqLVTGRVWRGSAFG 320
Cdd:cd08276   218 GEEVL----KLTGGrGVDHVVE-VGGPGTLAQSIKAVAPG-GVISLIGFlSGFEAPVLLLPL-LTKGATLRGIAVG 286
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
13-372 1.87e-24

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


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 101.91  E-value: 1.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  13 AWGPNQPLSIEEVDVMLP--RKGEVLVKIIASGVCHTDAFTLSGeDPEGV----FPAILGHEGGGIVEQIGEGVTSVQVG 86
Cdd:cd08267     5 RYGSPEVLLLLEVEVPIPtpKPGEVLVKVHAASVNPVDWKLRRG-PPKLLlgrpFPPIPGMDFAGEVVAVGSGVTRFKVG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  87 DHVIplytaecGVCKMCTSGktnlcsavretqgkglmpdgttrfykdgepiyhymgcsTFSEYTVLPEISLAKVNKEAPL 166
Cdd:cd08267    84 DEVF-------GRLPPKGGG--------------------------------------ALAEYVVAPESGLAKKPEGVSF 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 167 EEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGL-GGIGLSAVigaQMAKAS--RIIAIDiNESKFELAKKLGATDCInp 243
Cdd:cd08267   119 EEAAALPVAGLTALQALRDAGKVKPGQRVLINGAsGGVGTFAV---QIAKALgaHVTGVC-STRNAELVRSLGADEVI-- 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 244 kDYDKpiQDVIVELTDGGV-DYSFECIGNVDvmRSALECCHKGWGESVIIGVAGagqeistRPFQLVTGRVWRGSAFGGV 322
Cdd:cd08267   193 -DYTT--EDFVALTAGGEKyDVIFDAVGNSP--FSLYRASLALKPGGRYVSVGG-------GPSGLLLVLLLLPLTLGGG 260
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2539978014 323 KGRSElpgyverylagdiplqdFITHTMPLEDINEAFDLMHKGEsIRTVI 372
Cdd:cd08267   261 GRRLK-----------------FFLAKPNAEDLEQLAELVEEGK-LKPVI 292
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
9-362 3.65e-24

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: 101.04  E-value: 3.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAI--AWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGV-FPAILGHEGGGIVEQIGEGVTSVQV 85
Cdd:cd08241     2 KAVVckELGGPEDLVLEEVPPEPGAPGEVRIRVEAAGVNFPDLLMIQGKYQVKPpLPFVPGSEVAGVVEAVGEGVTGFKV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  86 GDHVIplytaecgvckmctsgktnlcsavretqgkGLMPDGTtrfykdgepiyhymgcstFSEYTVLPEISLAKVNKEAP 165
Cdd:cd08241    82 GDRVV------------------------------ALTGQGG------------------FAEEVVVPAAAVFPLPDGLS 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 166 LEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGL-GGIGLSAVigaQMAKA--SRIIAIDINESKFELAKKLGATDCIN 242
Cdd:cd08241   114 FEEAAALPVTYGTAYHALVRRARLQPGETVLVLGAaGGVGLAAV---QLAKAlgARVIAAASSEEKLALARALGADHVID 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 243 PKDYDkpIQDVIVELTDG-GVDYSFECIGNvDVMRSALECCHKGwGESVIIGVAgAGqEISTRPFQL-------VTGrVW 314
Cdd:cd08241   191 YRDPD--LRERVKALTGGrGVDVVYDPVGG-DVFEASLRSLAWG-GRLLVIGFA-SG-EIPQIPANLlllknisVVG-VY 263
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2539978014 315 RGSAfggvkgRSELPGYVER--------YLAGDIPLQdfITHTMPLEDINEAFDLM 362
Cdd:cd08241   264 WGAY------ARREPELLRAnlaelfdlLAEGKIRPH--VSAVFPLEQAAEALRAL 311
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
20-281 2.40e-23

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


Pssm-ID: 176189 [Multi-domain]  Cd Length: 320  Bit Score: 99.05  E-value: 2.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  20 LSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGvFPAILGHEGGGIVEQIGEGVTSVQVGDHVIplytaecgv 99
Cdd:cd05286    14 LEYEDVPVPEPGPGEVLVRNTAIGVNFIDTYFRSGLYPLP-LPFVLGVEGAGVVEAVGPGVTGFKVGDRVA--------- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 100 ckmctsgktnlcsavretqgkglmpdgttrfykdgepiyhYMGC-STFSEYTVLPEISLAKVNKEAPLEEV--CLLgcgv 176
Cdd:cd05286    84 ----------------------------------------YAGPpGAYAEYRVVPASRLVKLPDGISDETAaaLLL---- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 177 tTGMGAVM---NTAKVEEGATVAIFGL-GGIGLsavIGAQMAKA--SRIIAIDINESKFELAKKLGATDCINPKDYDkpI 250
Cdd:cd05286   120 -QGLTAHYllrETYPVKPGDTVLVHAAaGGVGL---LLTQWAKAlgATVIGTVSSEEKAELARAAGADHVINYRDED--F 193
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2539978014 251 QDVIVELTDG-GVDYSFECIGnVDVMRSALEC 281
Cdd:cd05286   194 VERVREITGGrGVDVVYDGVG-KDTFEGSLDS 224
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
20-367 4.33e-23

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: 98.19  E-value: 4.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  20 LSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVfPAILGHEGGGIVEQIGEGVTSVQVGDHVIPLYTAECGV 99
Cdd:cd08264    14 LKVEDVKDPKPGPGEVLIRVKMAGVNPVDYNVINAVKVKPM-PHIPGAEFAGVVEEVGDHVKGVKKGDRVVVYNRVFDGT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 100 CKMCTSGKTNLCsavRETQGKGLMPDGttrfykdgepiyhymgcsTFSEYTVLPEISLAKVNKEAPLEEVCLLGCGVTTG 179
Cdd:cd08264    93 CDMCLSGNEMLC---RNGGIIGVVSNG------------------GYAEYIVVPEKNLFKIPDSISDELAASLPVAALTA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 180 MGAvMNTAKVEEGATVAIFGLGG-IGLSAVigaQMAK--ASRIIAIdineSKFELAKKLGATDCInpkDYDKPIQDViVE 256
Cdd:cd08264   152 YHA-LKTAGLGPGETVVVFGASGnTGIFAV---QLAKmmGAEVIAV----SRKDWLKEFGADEVV---DYDEVEEKV-KE 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 257 LTdGGVDYSFECIGNvdvmrsalecchKGWGESV-IIGVAG--------AGQEISTRPFQLVTGRVwrgSAFGGVKG-RS 326
Cdd:cd08264   220 IT-KMADVVINSLGS------------SFWDLSLsVLGRGGrlvtfgtlTGGEVKLDLSDLYSKQI---SIIGSTGGtRK 283
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2539978014 327 ELPGYVEryLAGDIPLqdFITHTMPLEDINEAFDLMHKGES 367
Cdd:cd08264   284 ELLELVK--IAKDLKV--KVWKTFKLEEAKEALKELFSKER 320
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
9-270 9.45e-23

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 97.24  E-value: 9.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAI--AWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGV-FPAILGHEGGGIVEQIGEGVTSVQV 85
Cdd:cd08272     2 KALVleSFGGPEVFELREVPRPQPGPGQVLVRVHASGVNPLDTKIRRGGAAARPpLPAILGCDVAGVVEAVGEGVTRFRV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  86 GDHVIplytaecgvckMCTSGktnlcsaVRETQGkglmpdgttrfykdgepiyhymgcsTFSEYTVLPEISLAKVNKEAP 165
Cdd:cd08272    82 GDEVY-----------GCAGG-------LGGLQG-------------------------SLAEYAVVDARLLALKPANLS 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 166 LEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIF-GLGGIGLSAVigaQMAKA--SRIIAIDINEsKFELAKKLGATDCIn 242
Cdd:cd08272   119 MREAAALPLVGITAWEGLVDRAAVQAGQTVLIHgGAGGVGHVAV---QLAKAagARVYATASSE-KAAFARSLGADPII- 193
                         250       260
                  ....*....|....*....|....*....
gi 2539978014 243 pkDYDKPIQDVIVELTDG-GVDYSFECIG 270
Cdd:cd08272   194 --YYRETVVEYVAEHTGGrGFDVVFDTVG 220
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
51-372 2.08e-22

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: 95.42  E-value: 2.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  51 TLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDHVIPLYTAecgvckmctsgktnlcsavretqgkglmpdgttrf 130
Cdd:cd08255    10 GLSTGTEKLPLPLPPGYSSVGRVVEVGSGVTGFKPGDRVFCFGPH----------------------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 131 ykdgepiyhymgcstfSEYTVLPEISLAKVNKEAPLEEVCLLGCGvTTGMGAVMNtAKVEEGATVAIFGLGGIGLSAvig 210
Cdd:cd08255    55 ----------------AERVVVPANLLVPLPDGLPPERAALTALA-ATALNGVRD-AEPRLGERVAVVGLGLVGLLA--- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 211 AQMAK---ASRIIAIDINESKFELAKKLGATDCINpkdydkpiQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGwG 287
Cdd:cd08255   114 AQLAKaagAREVVGVDPDAARRELAEALGPADPVA--------ADTADEIGGRGADVVIEASGSPSALETALRLLRDR-G 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 288 ESVIIGVAGAGQEISTRPF-----QLVTGRVwrgsafGGVkgRSELPGY----------VERYLAgDIPLQDFITHTMPL 352
Cdd:cd08255   185 RVVLVGWYGLKPLLLGEEFhfkrlPIRSSQV------YGI--GRYDRPRrwtearnleeALDLLA-EGRLEALITHRVPF 255
                         330       340
                  ....*....|....*....|..
gi 2539978014 353 EDINEAFDLM--HKGESIRTVI 372
Cdd:cd08255   256 EDAPEAYRLLfeDPPECLKVVL 277
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
17-373 3.28e-22

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: 96.22  E-value: 3.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  17 NQPLSIEEVDVMLPRKGEVLVKIIASGVCHTD----------AFTLSGEDPEGVFPAI-LGHEGGGIVEQIGEGVTS-VQ 84
Cdd:cd08262     8 DGPLVVRDVPDPEPGPGQVLVKVLACGICGSDlhatahpeamVDDAGGPSLMDLGADIvLGHEFCGEVVDYGPGTERkLK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  85 VGDHVIPLYTAECGVCKMCtsgktnlcsavretqGKGLMPDgttrfykdgepiyHYMGcstFSEYTVLPEISLAKVNKEA 164
Cdd:cd08262    88 VGTRVTSLPLLLCGQGASC---------------GIGLSPE-------------APGG---YAEYMLLSEALLLRVPDGL 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 165 PLEEVCLLGcGVTTGMGAVmNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPK 244
Cdd:cd08262   137 SMEDAALTE-PLAVGLHAV-RRARLTPGEVALVIGCGPIGLAVIAALKARGVGPIVASDFSPERRALALAMGADIVVDPA 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 245 DyDKPIQDVIVELTDGGV---DYSFECIGNVDVMRSALECCHKGwgeSVIIGVAGAGQEISTRPFQlvtgRVWRGSA--F 319
Cdd:cd08262   215 A-DSPFAAWAAELARAGGpkpAVIFECVGAPGLIQQIIEGAPPG---GRIVVVGVCMESDNIEPAL----AIRKELTlqF 286
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2539978014 320 GGVKGRSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHKGES-IRTVIH 373
Cdd:cd08262   287 SLGYTPEEFADALDALAEGKVDVAPMVTGTVGLDGVPDAFEALRDPEHhCKILVD 341
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
10-270 8.94e-22

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 94.65  E-value: 8.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  10 AAIAW---GPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVG 86
Cdd:cd08271     2 KAWVLpkpGAALQLTLEEIEIPGPGAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTGWKVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  87 DHVipLYTAecgvckmctsgktnlcsavretqgkGLMPDGTtrfykdgepiyhymgcstFSEYTVLPEISLAKVNKEAPL 166
Cdd:cd08271    82 DRV--AYHA-------------------------SLARGGS------------------FAEYTVVDARAVLPLPDSLSF 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 167 EEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFGL-GGIGLSAVigaQMAKAS--RIIAIdINESKFELAKKLGATDCInp 243
Cdd:cd08271   117 EEAAALPCAGLTAYQALFKKLRIEAGRTILITGGaGGVGSFAV---QLAKRAglRVITT-CSKRNFEYVKSLGADHVI-- 190
                         250       260
                  ....*....|....*....|....*....
gi 2539978014 244 kDY-DKPIQDVIVELTDG-GVDYSFECIG 270
Cdd:cd08271   191 -DYnDEDVCERIKEITGGrGVDAVLDTVG 218
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
34-257 1.00e-21

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 94.90  E-value: 1.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  34 EVLVKIIASGVCHTDAFTLSGEDPEgVFPAILGHEGGGIVEQIGEGVTSVQVGDHV--IPLYTaeCGVCKMCTSGKTNLC 111
Cdd:PRK10309   27 DVLVKVASSGLCGSDIPRIFKNGAH-YYPITLGHEFSGYVEAVGSGVDDLHPGDAVacVPLLP--CFTCPECLRGFYSLC 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 112 SAvretqgkglmpdgttrfykdgepiYHYMGCSTF---SEYTVLPEISLAKVNKEAPLEEVCLLGcGVTTGMGAVmNTAK 188
Cdd:PRK10309  104 AK------------------------YDFIGSRRDggnAEYIVVKRKNLFALPTDMPIEDGAFIE-PITVGLHAF-HLAQ 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 189 VEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKDYDKP-IQDVIVEL 257
Cdd:PRK10309  158 GCEGKNVIIIGAGTIGLLAIQCAVALGAKSVTAIDINSEKLALAKSLGAMQTFNSREMSAPqIQSVLREL 227
PLN02702 PLN02702
L-idonate 5-dehydrogenase
29-367 7.78e-21

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 92.53  E-value: 7.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  29 LPRKG--EVLVKIIASGVCHTDAF---TLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDHVIPLYTAECGVCKMC 103
Cdd:PLN02702   36 LPPLGphDVRVRMKAVGICGSDVHylkTMRCADFVVKEPMVIGHECAGIIEEVGSEVKHLVVGDRVALEPGISCWRCNLC 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 104 TSGKTNLCsavretqgkglmPDgtTRFYkdGEPIYHymgcSTFSEYTVLPEISLAKVNKEAPLEEVCL---LGCGVTTgm 180
Cdd:PLN02702  116 KEGRYNLC------------PE--MKFF--ATPPVH----GSLANQVVHPADLCFKLPENVSLEEGAMcepLSVGVHA-- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 181 gavMNTAKVEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCI----NPKDYDKPIQDvIVE 256
Cdd:PLN02702  174 ---CRRANIGPETNVLVMGAGPIGLVTMLAARAFGAPRIVIVDVDDERLSVAKQLGADEIVlvstNIEDVESEVEE-IQK 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 257 LTDGGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVagaGQEISTRPFQLVTGRvwRGSAFGGVKGRSELPGYVERYL 336
Cdd:PLN02702  250 AMGGGIDVSFDCVGFNKTMSTALEATRAG-GKVCLVGM---GHNEMTVPLTPAAAR--EVDVVGVFRYRNTWPLCLEFLR 323
                         330       340       350
                  ....*....|....*....|....*....|...
gi 2539978014 337 AGDIPLQDFITH--TMPLEDINEAFDLMHKGES 367
Cdd:PLN02702  324 SGKIDVKPLITHrfGFSQKEVEEAFETSARGGN 356
PRK10083 PRK10083
putative oxidoreductase; Provisional
16-364 7.60e-20

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 89.41  E-value: 7.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  16 PNQpLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDHVIPLYTA 95
Cdd:PRK10083    9 PNS-LAIEERPIPQPAAGEVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGEGVDAARIGERVAVDPVI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  96 ECGVCKMCTSGKTNLCSAVretQGKGLMPDGttrfykdgepiyhymgcsTFSEYTVLP-----EISLAKVNKEAPLEEVC 170
Cdd:PRK10083   88 SCGHCYPCSIGKPNVCTSL---VVLGVHRDG------------------GFSEYAVVPaknahRIPDAIADQYAVMVEPF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 171 LLGCGVTtgmgavmNTAKVEEGATVAIFGLGGIGLSAVigaQMAKA----SRIIAIDINESKFELAKKLGATDCINpkDY 246
Cdd:PRK10083  147 TIAANVT-------GRTGPTEQDVALIYGAGPVGLTIV---QVLKGvynvKAVIVADRIDERLALAKESGADWVIN--NA 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 247 DKPIQDViveLTDGGVDYS--FECIGNVDVMRSALECChkgwGESVIIGVAGAGQEISTRPFQLVTGRvwRGSAFGGVKG 324
Cdd:PRK10083  215 QEPLGEA---LEEKGIKPTliIDAACHPSILEEAVTLA----SPAARIVLMGFSSEPSEIVQQGITGK--ELSIFSSRLN 285
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2539978014 325 RSELPGYVERYLAGDIPLQDFITHTMPLEDINEAFDLMHK 364
Cdd:PRK10083  286 ANKFPVVIDWLSKGLIDPEKLITHTFDFQHVADAIELFEK 325
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
13-368 1.03e-18

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: 85.96  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  13 AWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSG--EDPEGVfPAILGHEGGGIVEQIGEGVTSVQVGDHVi 90
Cdd:cd05276     8 EPGGPEVLELGEVPKPAPGPGEVLIRVAAAGVNRADLLQRQGlyPPPPGA-SDILGLEVAGVVVAVGPGVTGWKVGDRV- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  91 plytaeCGVCkmctsgktnlcsavretQGKGlmpdgttrfykdgepiyhymgcstFSEYTVLPEISLAKVNKE------A 164
Cdd:cd05276    86 ------CALL-----------------AGGG------------------------YAEYVVVPAGQLLPVPEGlslveaA 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 165 PLEEVCLlgcgvtTGMGAVMNTAKVEEGATVAIF-GLGGIGLSAVigaQMAKAS--RIIAIDINESKFELAKKLGATDCI 241
Cdd:cd05276   119 ALPEVFF------TAWQNLFQLGGLKAGETVLIHgGASGVGTAAI---QLAKALgaRVIATAGSEEKLEACRALGADVAI 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 242 NPKDYDkpIQDVIVELTDG-GVDYSFECIG------NVDVMrsALEcchkgwGESVIIGV-AGAGQEISTRPF----QLV 309
Cdd:cd05276   190 NYRTED--FAEEVKEATGGrGVDVILDMVGgdylarNLRAL--APD------GRLVLIGLlGGAKAELDLAPLlrkrLTL 259
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2539978014 310 TGRVWRGSafgGVKGRSELPGYVER----YLAGDIpLQDFITHTMPLEDINEAFDLMHKGESI 368
Cdd:cd05276   260 TGSTLRSR---SLEEKAALAAAFREhvwpLFASGR-IRPVIDKVFPLEEAAEAHRRMESNEHI 318
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
15-270 3.43e-18

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


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 84.19  E-value: 3.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  15 GPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPE-GVFPAILGHEGGGIVEQIGEGVTSVQVGDHVIPLY 93
Cdd:cd08268    10 GGPEVLRIEELPVPAPGAGEVLIRVEAIGLNRADAMFRRGAYIEpPPLPARLGYEAAGVVEAVGAGVTGFAVGDRVSVIP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  94 TAECGVckmctsgktnlcsavretqgkglmpdgttrfykdgepiYHymgcsTFSEYTVLPEISLAKVNKEAPLEEVCLLG 173
Cdd:cd08268    90 AADLGQ--------------------------------------YG-----TYAEYALVPAAAVVKLPDGLSFVEAAALW 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 174 CGVTTGMGAVMNTAKVEEGATVAIFGL-GGIGLSAVigaQMAKA--SRIIAIDINESKFELAKKLGATDCINPKDYDkpI 250
Cdd:cd08268   127 MQYLTAYGALVELAGLRPGDSVLITAAsSSVGLAAI---QIANAagATVIATTRTSEKRDALLALGAAHVIVTDEED--L 201
                         250       260
                  ....*....|....*....|.
gi 2539978014 251 QDVIVELTDG-GVDYSFECIG 270
Cdd:cd08268   202 VAEVLRITGGkGVDVVFDPVG 222
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
9-372 2.23e-16

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: 79.16  E-value: 2.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAI--AWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGE-DPEGVFPAILGHEGGGIVEQIGEGVTSVQV 85
Cdd:cd08253     2 RAIRyhEFGAPDVLRLGDLPVPTPGPGEVLVRVHASGVNPVDTYIRAGAyPGLPPLPYVPGSDGAGVVEAVGEGVDGLKV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  86 GDHViplYTaecgvckmctsgkTNLCSAVRetQGkglmpdgttrfykdgepiyhymgcsTFSEYTVLPEISLAKVNKEAP 165
Cdd:cd08253    82 GDRV---WL-------------TNLGWGRR--QG-------------------------TAAEYVVVPADQLVPLPDGVS 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 166 LEEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFG-LGGIGLSAVigaQMAKAS--RIIAIDINESKFELAKKLGATDCIN 242
Cdd:cd08253   119 FEQGAALGIPALTAYRALFHRAGAKAGETVLVHGgSGAVGHAAV---QLARWAgaRVIATASSAEGAELVRQAGADAVFN 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 243 PKDYDkpIQDVIVELTDG-GVDYSFECIGNVDvMRSALECCHKGwGESVIIGVAGAGQEISTRPFQLVTGRVwRGSAFGG 321
Cdd:cd08253   196 YRAED--LADRILAATAGqGVDVIIEVLANVN-LAKDLDVLAPG-GRIVVYGSGGLRGTIPINPLMAKEASI-RGVLLYT 270
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2539978014 322 VKgRSELPGYVERYLAG--DIPLQDFITHTMPLEDINEAFDLMHKGESIRTVI 372
Cdd:cd08253   271 AT-PEERAAAAEAIAAGlaDGALRPVIAREYPLEEAAAAHEAVESGGAIGKVV 322
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
20-365 3.99e-16

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


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 78.46  E-value: 3.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  20 LSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDP-EGVFPAILGHEGGGIVEQIGEGVTSVQVGDHVIPLytaecg 98
Cdd:cd08273    15 LKVVEADLPEPAAGEVVVKVEASGVSFADVQMRRGLYPdQPPLPFTPGYDLVGRVDALGSGVTGFEVGDRVAAL------ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  99 vckmctsgktnlcsavreTQGKGlmpdgttrfykdgepiyhymgcstFSEYTVLPEISLAKVNKEAPLEE-VCLlgcgVT 177
Cdd:cd08273    89 ------------------TRVGG------------------------NAEYINLDAKYLVPVPEGVDAAEaVCL----VL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 178 TGM---GAVMNTAKVEEGATVAIFGL-GGIGLSAVIGAQMAKAsRIIAIDiNESKFELAKKLGATdcinPKDYDKpiQDV 253
Cdd:cd08273   123 NYVtayQMLHRAAKVLTGQRVLIHGAsGGVGQALLELALLAGA-EVYGTA-SERNHAALRELGAT----PIDYRT--KDW 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 254 I-VELTDGGVDYSFECIGNvDVMRSALECCHKGwGESVIIGVAGA--GQEISTRPFQLVTGRVWRGSAFGGvkGRSELPG 330
Cdd:cd08273   195 LpAMLTPGGVDVVFDGVGG-ESYEESYAALAPG-GTLVCYGGNSSllQGRRSLAALGSLLARLAKLKLLPT--GRRATFY 270
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2539978014 331 YVERYLAGDIPL--QDF---------------ITHTMPLEDINEAFDLMHKG 365
Cdd:cd08273   271 YVWRDRAEDPKLfrQDLtelldllakgkirpkIAKRLPLSEVAEAHRLLESG 322
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
16-247 6.95e-16

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: 78.23  E-value: 6.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  16 PNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEdPEGVFPA-----------ILGHEGGGIVEQIGEGVTSVQ 84
Cdd:cd08246    26 PAQAIQLEDVPVPELGPGEVLVAVMAAGVNYNNVWAALGE-PVSTFAArqrrgrdepyhIGGSDASGIVWAVGEGVKNWK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  85 VGDHVIPlytaecgvckmctsgktnLCSAVRETQGKGLMPDGTtrfYKDGEPIYHY-MGCSTFSEYTVLPEISLAKVNKE 163
Cdd:cd08246   105 VGDEVVV------------------HCSVWDGNDPERAGGDPM---FDPSQRIWGYeTNYGSFAQFALVQATQLMPKPKH 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 164 APLEE-VCLLGCGVTT-GMGAVMNTAKVEEGATVAIFG-LGGIGLSAVigaQMAKAS--RIIAIDINESKFELAKKLGAT 238
Cdd:cd08246   164 LSWEEaAAYMLVGATAyRMLFGWNPNTVKPGDNVLIWGaSGGLGSMAI---QLARAAgaNPVAVVSSEEKAEYCRALGAE 240

                  ....*....
gi 2539978014 239 DCINPKDYD 247
Cdd:cd08246   241 GVINRRDFD 249
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
11-280 4.74e-15

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: 74.97  E-value: 4.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  11 AIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPegvFPAILGHEGGGIVEQIGEG--VTSVQVGDH 88
Cdd:cd08242     3 ALVLDGGLDLRVEDLPKPEPPPGEALVRVLLAGICNTDLEIYKGYYP---FPGVPGHEFVGIVEEGPEAelVGKRVVGEI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  89 VIPlytaeCGVCKMCTSGKTNLCSaVRETQGkglMPDgttrfyKDGepiyhymgcsTFSEYTVLPEISLAKVNKEAPLEE 168
Cdd:cd08242    80 NIA-----CGRCEYCRRGLYTHCP-NRTVLG---IVD------RDG----------AFAEYLTLPLENLHVVPDLVPDEQ 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 169 VCLlgcgvTTGMGAVMNT---AKVEEGATVAIFGLGGIGLSAvigAQMAKAS--RIIAIDINESKFELAKKLGATDCinp 243
Cdd:cd08242   135 AVF-----AEPLAAALEIleqVPITPGDKVAVLGDGKLGLLI---AQVLALTgpDVVLVGRHSEKLALARRLGVETV--- 203
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2539978014 244 kdydkpiQDVIVELTDGGVDYSFECIGNVDVMRSALE 280
Cdd:cd08242   204 -------LPDEAESEGGGFDVVVEATGSPSGLELALR 233
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
9-374 1.40e-14

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: 74.18  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTD----AFTLsGEDPEGVFPAILGHEGGGIVEQIGEGvTSVQ 84
Cdd:cd08230     2 KAIAVKPGKPGVRVVDIPEPEPTPGEVLVRTLEVGVCGTDreivAGEY-GTAPPGEDFLVLGHEALGVVEEVGDG-SGLS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  85 VGDHVIPLYTAECGVCKMCTSGKTNLCSA--VRETQGKGLmpDGttrfykdgepiyhYMgcstfSEYTVLPEISLAKVNK 162
Cdd:cd08230    80 PGDLVVPTVRRPPGKCLNCRIGRPDFCETgeYTERGIKGL--HG-------------FM-----REYFVDDPEYLVKVPP 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 163 EapLEEVCLLGCGVTTGMGAVMNTAKVE------EGATVAIFGLGGIG-LSAVIGAQMAKASRIIAI-DINESKFELAKK 234
Cdd:cd08230   140 S--LADVGVLLEPLSVVEKAIEQAEAVQkrlptwNPRRALVLGAGPIGlLAALLLRLRGFEVYVLNRrDPPDPKADIVEE 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 235 LGATdcinpkDYDKPIQDVIVELTDGGVDYSFECIGNVDVMRSALECCHKGwGESVIIGVAGAGQEISTRPFQLVTGRVW 314
Cdd:cd08230   218 LGAT------YVNSSKTPVAEVKLVGEFDLIIEATGVPPLAFEALPALAPN-GVVILFGVPGGGREFEVDGGELNRDLVL 290
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2539978014 315 RGSA-FGGVKG-RSELPGYVERYLAGDIP----LQDFITHTMPLEDINEAFDLMHKGEsIRTVIHF 374
Cdd:cd08230   291 GNKAlVGSVNAnKRHFEQAVEDLAQWKYRwpgvLERLITRRVPLEEFAEALTEKPDGE-IKVVIEW 355
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
35-297 1.81e-14

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 73.57  E-value: 1.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  35 VLVKIIASGVCHTDAFTLSgEDPEGVF----PAILGHEGGGIVEQIGEgvTSVQVGDHVIPLYTAECGVCKMCTSGKTNL 110
Cdd:PRK09880   30 TLVQITRGGICGSDLHYYQ-EGKVGNFvikaPMVLGHEVIGKIVHSDS--SGLKEGQTVAINPSKPCGHCKYCLSHNENQ 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 111 CsavretqgkglmpdGTTRFYkdGEPIY--HYMGcsTFSEYTVLPEISLAKVNKEAPlEEVCLLGCGVTTGMGAVmNTAK 188
Cdd:PRK09880  107 C--------------TTMRFF--GSAMYfpHVDG--GFTRYKVVDTAQCIPYPEKAD-EKVMAFAEPLAVAIHAA-HQAG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 189 VEEGATVAIFGLGGIGLSAVIGAQMAKASRIIAIDINESKFELAKKLGATDCINPKD--YDKPIQDviveltDGGVDYSF 266
Cdd:PRK09880  167 DLQGKRVFVSGVGPIGCLIVAAVKTLGAAEIVCADVSPRSLSLAREMGADKLVNPQNddLDHYKAE------KGYFDVSF 240
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2539978014 267 ECIGNVDVMRSALECChKGWGESVIIGVAGA 297
Cdd:PRK09880  241 EVSGHPSSINTCLEVT-RAKGVMVQVGMGGA 270
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
34-366 4.98e-14

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 72.60  E-value: 4.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  34 EVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDHV-IPLYTAECGVCKMCTSGKTNLCS 112
Cdd:PLN02586   39 DVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGKNVKKFKEGDRVgVGVIVGSCKSCESCDQDLENYCP 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 113 AVRETQGKglmpdgttrFYKDGEPIYhymgcSTFSEYTVLPEISLAKVNKEAPLEEVCLLGCGVTTGMGAVMNTAKVEEG 192
Cdd:PLN02586  119 KMIFTYNS---------IGHDGTKNY-----GGYSDMIVVDQHFVLRFPDNLPLDAGAPLLCAGITVYSPMKYYGMTEPG 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 193 ATVAIFGLGGIGLSAV-IGAQMAKASRIIAIDINESKfELAKKLGATDCINPKDYDKpiqdviVELTDGGVDYSFECIGN 271
Cdd:PLN02586  185 KHLGVAGLGGLGHVAVkIGKAFGLKVTVISSSSNKED-EAINRLGADSFLVSTDPEK------MKAAIGTMDYIIDTVSA 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 272 VDVMRSALECChKGWGESVIIGVAGAGQEISTrpFQLVTGR-VWRGSAFGGVKGRSELPGYVERY-LAGDIPLqdfitht 349
Cdd:PLN02586  258 VHALGPLLGLL-KVNGKLITLGLPEKPLELPI--FPLVLGRkLVGGSDIGGIKETQEMLDFCAKHnITADIEL------- 327
                         330
                  ....*....|....*..
gi 2539978014 350 MPLEDINEAFDLMHKGE 366
Cdd:PLN02586  328 IRMDEINTAMERLAKSD 344
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
21-270 5.62e-13

Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of undetermined function. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176212 [Multi-domain]  Cd Length: 329  Bit Score: 69.21  E-value: 5.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  21 SIEEVDVMLPRKGEVLVKIIASGVCHTDA-FTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDHVIplytaecgv 99
Cdd:cd08250    19 SIVDVPVPLPGPGEVLVKNRFVGINASDInFTAGRYDPGVKPPFDCGFEGVGEVVAVGEGVTDFKVGDAVA--------- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 100 ckmctsgktnlcsavretqgkglmpdgttrfykdgepiyhYMGCSTFSEYTVLPEISLAKVNKEAPlEEVCLLGCGVTTG 179
Cdd:cd08250    90 ----------------------------------------TMSFGAFAEYQVVPARHAVPVPELKP-EVLPLLVSGLTAS 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 180 MgAVMNTAKVEEGATVAIF-GLGGIGLSAVigaQMAKAS--RIIAIDINESKFELAKKLGATDCINPKDYDkpIQDVIVE 256
Cdd:cd08250   129 I-ALEEVGEMKSGETVLVTaAAGGTGQFAV---QLAKLAgcHVIGTCSSDEKAEFLKSLGCDRPINYKTED--LGEVLKK 202
                         250
                  ....*....|....
gi 2539978014 257 LTDGGVDYSFECIG 270
Cdd:cd08250   203 EYPKGVDVVYESVG 216
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
15-372 2.88e-12

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: 66.84  E-value: 2.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  15 GPNQpLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSG--EDPEGvFPAILGHEGGGIVEQIGEGVTSVQVGDHVIpl 92
Cdd:cd08275    10 GLDK-LKVEKEALPEPSSGEVRVRVEACGLNFADLMARQGlyDSAPK-PPFVPGFECAGTVEAVGEGVKDFKVGDRVM-- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  93 ytaecgvckmctsgktnlcsavretqgkglmpdGTTRFykdgepiyhymgcSTFSEYTVLPEISLAKVNKEAPLEE-VCL 171
Cdd:cd08275    86 ---------------------------------GLTRF-------------GGYAEVVNVPADQVFPLPDGMSFEEaAAF 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 172 LGCGVTTGMgAVMNTAKVEEGATVAIF-GLGGIGLSAVigaQMAKASRIIAI--DINESKFELAKKLGATDCInpkdyDK 248
Cdd:cd08275   120 PVNYLTAYY-ALFELGNLRPGQSVLVHsAAGGVGLAAG---QLCKTVPNVTVvgTASASKHEALKENGVTHVI-----DY 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 249 PIQD---VIVELTDGGVDYSFECIGNVDvmrsalecCHKGW------GESVIIGVAgAGQEISTRPFQLVTGRVWRGSAF 319
Cdd:cd08275   191 RTQDyveEVKKISPEGVDIVLDALGGED--------TRKSYdllkpmGRLVVYGAA-NLVTGEKRSWFKLAKKWWNRPKV 261
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2539978014 320 ------------GGV------KGRSELPGYVER----YLAGDI-PLQDfitHTMPLEDINEAFDLMHKGESIRTVI 372
Cdd:cd08275   262 dpmklisenksvLGFnlgwlfEERELLTEVMDKllklYEEGKIkPKID---SVFPFEEVGEAMRRLQSRKNIGKVV 334
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
20-270 9.91e-12

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 65.44  E-value: 9.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  20 LSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSG--EDPEGVFPaILGHEGGGIVEQIGEGVTSVQVGDHVIplytaec 97
Cdd:PTZ00354   16 LKIGESPKPAPKRNDVLIKVSAAGVNRADTLQRQGkyPPPPGSSE-ILGLEVAGYVEDVGSDVKRFKEGDRVM------- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  98 gvckmctsgktnlcsavretqgkGLMPDGttrfykdgepiyhymgcsTFSEYTVLPEISLAKVNKEAPLEEVCLLGCGVT 177
Cdd:PTZ00354   88 -----------------------ALLPGG------------------GYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 178 TGMGAVMNTAKVEEGATVAIF-GLGGIGLSAvigAQMAK---ASRIIAIDiNESKFELAKKLGATDCINPKDyDKPIQDV 253
Cdd:PTZ00354  127 TAWQLLKKHGDVKKGQSVLIHaGASGVGTAA---AQLAEkygAATIITTS-SEEKVDFCKKLAAIILIRYPD-EEGFAPK 201
                         250
                  ....*....|....*...
gi 2539978014 254 IVELT-DGGVDYSFECIG 270
Cdd:PTZ00354  202 VKKLTgEKGVNLVLDCVG 219
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
15-358 1.48e-11

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


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 65.01  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  15 GPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSG-----EDPEG---------------VFPAILGHEGGGIVE 74
Cdd:cd08274    11 GLDKLVYRDDVPVPTPAPGEVLIRVGACGVNNTDINTREGwysteVDGATdstgageagwwggtlSFPRIQGADIVGRVV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  75 QIGEGVTSVQVGDHViplytaecgvckmctsgktnlcsavretqgkglMPDGTTRFYKDGEPI-YHYMGCST---FSEYT 150
Cdd:cd08274    91 AVGEGVDTARIGERV---------------------------------LVDPSIRDPPEDDPAdIDYIGSERdggFAEYT 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 151 VLPEISLAKVNKEAPLEEVCLLGCGVTTGMGavMNT-AKVEEGATVAIFGL-GGIGLSAVigaQMAKA--SRIIAIdINE 226
Cdd:cd08274   138 VVPAENAYPVNSPLSDVELATFPCSYSTAEN--MLErAGVGAGETVLVTGAsGGVGSALV---QLAKRrgAIVIAV-AGA 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 227 SKFELAKKLGATDCInpkDYDKPIQDVIVELTDGGVDYSFECIGNvDVMRSALECCHKGwGESVIIG-VAGAGQEISTRP 305
Cdd:cd08274   212 AKEEAVRALGADTVI---LRDAPLLADAKALGGEPVDVVADVVGG-PLFPDLLRLLRPG-GRYVTAGaIAGPVVELDLRT 286
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2539978014 306 FQLVTGRVwRGSAFGGVKGRSELPGYVERylaGDI-PLqdfITHTMPLEDINEA 358
Cdd:cd08274   287 LYLKDLTL-FGSTLGTREVFRRLVRYIEE---GEIrPV---VAKTFPLSEIREA 333
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
15-92 1.64e-11

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: 64.61  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  15 GPNQPLSIEEVDVMLPRK--GEVLVKIIASGVCHTDAFTLSGE-DPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDHVIP 91
Cdd:cd05282     7 GEPLPLVLELVSLPIPPPgpGEVLVRMLAAPINPSDLITISGAyGSRPPLPAVPGNEGVGVVVEVGSGVSGLLVGQRVLP 86

                  .
gi 2539978014  92 L 92
Cdd:cd05282    87 L 87
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
9-372 1.90e-11

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


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 64.55  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   9 KAAIAWGPNQP--LSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGvtSVQVG 86
Cdd:cd08243     2 KAIVIEQPGGPevLKLREIPIPEPKPGWVLIRVKAFGLNRSEIFTRQGHSPSVKFPRVLGIEAVGEVEEAPGG--TFTPG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  87 DHVIPLytaecgvckMctsgktnlcsavretqgkGLMpdGTTRfykDGepiyhymgcsTFSEYTVLPEISLAKVNKEAPL 166
Cdd:cd08243    80 QRVATA---------M------------------GGM--GRTF---DG----------SYAEYTLVPNEQVYAIDSDLSW 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 167 EEVCLLGCGVTTGMGAVMNTAKVEEGATVAIFG-LGGIGLSAvigAQMAKAS--RIIAIDINESKFELAKKLGATDCInp 243
Cdd:cd08243   118 AELAALPETYYTAWGSLFRSLGLQPGDTLLIRGgTSSVGLAA---LKLAKALgaTVTATTRSPERAALLKELGADEVV-- 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 244 kdYDKPIQDVIVELTDGGVDYSFECIGNVDVmRSALECCHKGwGESVIIGVAGaGQEiSTRPFQLVtgrvwrgsafggvk 323
Cdd:cd08243   193 --IDDGAIAEQLRAAPGGFDKVLELVGTATL-KDSLRHLRPG-GIVCMTGLLG-GQW-TLEDFNPM-------------- 252
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2539978014 324 grSELPGYVERYL----AGDI---PLQDF------------ITHTMPLEDINEAFDLMHKGESIRTVI 372
Cdd:cd08243   253 --DDIPSGVNLTLtgssSGDVpqtPLQELfdfvaaghldipPSKVFTFDEIVEAHAYMESNRAFGKVV 318
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
16-89 2.76e-11

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


Pssm-ID: 176252 [Multi-domain]  Cd Length: 324  Bit Score: 63.89  E-value: 2.76e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2539978014  16 PNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEG-VFPAILGHEGGGIVEQIGEGVTSVQVGDHV 89
Cdd:cd08292    12 PADVLEIGEVPKPTPGAGEVLVRTTLSPIHNHDLWTIRGTYGYKpELPAIGGSEAVGVVDAVGEGVKGLQVGQRV 86
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
34-364 4.97e-11

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 63.28  E-value: 4.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  34 EVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDHV-IPLYTAECGVCKMCTSGKTNLCS 112
Cdd:PLN02514   36 DVVIKVIYCGICHTDLHQIKNDLGMSNYPMVPGHEVVGEVVEVGSDVSKFTVGDIVgVGVIVGCCGECSPCKSDLEQYCN 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 113 AVRETQGKglmpdgttrFYKDGEPIYhymgcSTFSEYTVLPEISLAKV-NKEAPLEEVCLLGCGVTTgMGAVMNTAKVEE 191
Cdd:PLN02514  116 KRIWSYND---------VYTDGKPTQ-----GGFASAMVVDQKFVVKIpEGMAPEQAAPLLCAGVTV-YSPLSHFGLKQS 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 192 GATVAIFGLGGIGLsavIGAQMAKA--SRIIAIDINESKFELA-KKLGATDCINPKDYDKpiqdvIVELTDgGVDYSFEC 268
Cdd:PLN02514  181 GLRGGILGLGGVGH---MGVKIAKAmgHHVTVISSSDKKREEAlEHLGADDYLVSSDAAE-----MQEAAD-SLDYIIDT 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 269 IGNVDVMRSALECChKGWGESVIIGVAGAgqeistrPFQLVT-----GR-VWRGSAFGGVKGRSE-LPGYVERYLAGDIp 341
Cdd:PLN02514  252 VPVFHPLEPYLSLL-KLDGKLILMGVINT-------PLQFVTpmlmlGRkVITGSFIGSMKETEEmLEFCKEKGLTSMI- 322
                         330       340
                  ....*....|....*....|...
gi 2539978014 342 lqdfitHTMPLEDINEAFDLMHK 364
Cdd:PLN02514  323 ------EVVKMDYVNTAFERLEK 339
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
33-374 3.24e-10

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


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 60.70  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  33 GEVLVKIIASGVCHTDAFTLSGEDP-----EGVFPAILGHEGGGIVEQIGEGVTSVQVGDHVIPLYTaecgvckmctsgk 107
Cdd:cd08290    30 NEVLVKMLAAPINPADINQIQGVYPikpptTPEPPAVGGNEGVGEVVKVGSGVKSLKPGDWVIPLRP------------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 108 tnlcsavretqgkglmpdgttrfykdgepiyhymGCSTFSEYTVLPEISLAKVNKEAPLEEVCLLGCGVTTGMGAVMNTA 187
Cdd:cd08290    97 ----------------------------------GLGTWRTHAVVPADDLIKVPNDVDPEQAATLSVNPCTAYRLLEDFV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 188 KVEEGATVAIFG-LGGIGLsAVIgaQMAKASRIIAI-------DINESKFELaKKLGATDCINPKD-YDKPIQDVIVELT 258
Cdd:cd08290   143 KLQPGDWVIQNGaNSAVGQ-AVI--QLAKLLGIKTInvvrdrpDLEELKERL-KALGADHVLTEEElRSLLATELLKSAP 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 259 DGGVDYSFECIG--NVDVMRSALEcchKGwGESVIIGV-AGAGQEISTRP--FQLVTGRVWRGSAFGGVKGRSELPGYVE 333
Cdd:cd08290   219 GGRPKLALNCVGgkSATELARLLS---PG-GTMVTYGGmSGQPVTVPTSLliFKDITLRGFWLTRWLKRANPEEKEDMLE 294
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2539978014 334 R----YLAGDIPLQDF-ITHTMPLEDINEAFDL-MHKGESIRTVIHF 374
Cdd:cd08290   295 ElaelIREGKLKAPPVeKVTDDPLEEFKDALANaLKGGGGGKQVLVM 341
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
33-372 3.45e-10

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: 60.28  E-value: 3.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  33 GEVLVKIIASGVCHTDAFTLSGEDPEGvfPAILGHEGGGIVEQIGEGVTSVQVGDHViplytaeCGVCKMCtsgktnlcs 112
Cdd:cd05195     1 DEVEVEVKAAGLNFRDVLVALGLLPGD--ETPLGLECSGIVTRVGSGVTGLKVGDRV-------MGLAPGA--------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 113 avretqgkglmpdgttrfykdgepiyhymgcstFSEYTVLPEISLAKVNKEAPLEEVCLLGCGVTTGMGAVMNTAKVEEG 192
Cdd:cd05195    63 ---------------------------------FATHVRVDARLVVKIPDSLSFEEAATLPVAYLTAYYALVDLARLQKG 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 193 ATVAIF-GLGGIGLSAVIGAQMAKAsRIIAIDINESKFELAKKL-GATDCInPKDYDKPIQDVIVELTDG-GVDYSFECI 269
Cdd:cd05195   110 ESVLIHaAAGGVGQAAIQLAQHLGA-EVFATVGSEEKREFLRELgGPVDHI-FSSRDLSFADGILRATGGrGVDVVLNSL 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 270 GNvDVMRSALECCHKGwGESVIIGVAG--AGQEISTRPFQlvtgrvwRGSAFGGV------KGRSELPGY-----VERYL 336
Cdd:cd05195   188 SG-ELLRASWRCLAPF-GRFVEIGKRDilSNSKLGMRPFL-------RNVSFSSVdldqlaRERPELLREllrevLELLE 258
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2539978014 337 AGDI-PLQdfiTHTMPLEDINEAFDLMHKGESI-RTVI 372
Cdd:cd05195   259 AGVLkPLP---PTVVPSASEIDAFRLMQSGKHIgKVVL 293
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
26-372 2.06e-09

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: 58.21  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  26 DVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPE-GVFPAILGHEGGGIVEQIGEGVTSVQVGDHVIplytaecgvckmCT 104
Cdd:cd08251     1 EVAPPGPGEVRIQVRAFSLNFGDLLCVRGLYPTmPPYPFTPGFEASGVVRAVGPHVTRLAVGDEVI------------AG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 105 SGKTnlcsavretqgkglmpdgttrfykdgepiyhyMGCStfSEYTVLPEISLakVNKEAPL--EEVC-LLGCGVTtgMG 181
Cdd:cd08251    69 TGES--------------------------------MGGH--ATLVTVPEDQV--VRKPASLsfEEACaLPVVFLT--VI 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 182 AVMNTAKVEEGATVAI-FGLGGIGLSAVIGAQMAKASrIIAIDINESKFELAKKLGATDCINPKDYDkpIQDVIVELTDG 260
Cdd:cd08251   111 DAFARAGLAKGEHILIqTATGGTGLMAVQLARLKGAE-IYATASSDDKLEYLKQLGVPHVINYVEED--FEEEIMRLTGG 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 261 -GVDYSFECIGNvDVMRSALECCHKGwGESVIIGVAGAgqeISTRPFQLvtGRVWRGSAFGGVKGRSEL---PGYVERYL 336
Cdd:cd08251   188 rGVDVVINTLSG-EAIQKGLNCLAPG-GRYVEIAMTAL---KSAPSVDL--SVLSNNQSFHSVDLRKLLlldPEFIADYQ 260
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2539978014 337 A--------GDipLQDFITHTMPLEDINEAFDLMHKGESIRTVI 372
Cdd:cd08251   261 AemvslveeGE--LRPTVSRIFPFDDIGEAYRYLSDRENIGKVV 302
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
32-366 3.47e-09

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 57.73  E-value: 3.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  32 KGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDHV-IPLYTAECGVCKMCTSGKTNL 110
Cdd:PLN02178   31 ENDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVGKNVTKFKEGDRVgVGVIIGSCQSCESCNQDLENY 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 111 CSAVRETQgKGLMPDGTTrfykdgepiyhymGCSTFSEYTVLPEISLAKVNKEAPLEEVCLLGC-GVTTGMGAVMNTAKV 189
Cdd:PLN02178  111 CPKVVFTY-NSRSSDGTR-------------NQGGYSDVIVVDHRFVLSIPDGLPSDSGAPLLCaGITVYSPMKYYGMTK 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 190 EEGATVAIFGLGGIGLSAV-IGAQMAKASRIIAIDiNESKFELAKKLGATDCINPKDYDKpIQDVIveltdGGVDYSFEC 268
Cdd:PLN02178  177 ESGKRLGVNGLGGLGHIAVkIGKAFGLRVTVISRS-SEKEREAIDRLGADSFLVTTDSQK-MKEAV-----GTMDFIIDT 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 269 IGNVDVMRSALECChKGWGESVIIGVAGAGQEISTrpFQLVTGR-VWRGSAFGGVKGRSELPGYVERY-LAGDIPLqdfi 346
Cdd:PLN02178  250 VSAEHALLPLFSLL-KVSGKLVALGLPEKPLDLPI--FPLVLGRkMVGGSQIGGMKETQEMLEFCAKHkIVSDIEL---- 322
                         330       340
                  ....*....|....*....|
gi 2539978014 347 thtMPLEDINEAFDLMHKGE 366
Cdd:PLN02178  323 ---IKMSDINSAMDRLAKSD 339
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
13-358 5.04e-09

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


Pssm-ID: 176206 [Multi-domain]  Cd Length: 324  Bit Score: 56.99  E-value: 5.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  13 AWGPNQPLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGEDPEG---VFPAILGHEGGGIVEQIGEGVTSVQVGDHV 89
Cdd:cd08244     8 EFGPPEVLVPEDVPDPVPGPGQVRIAVAAAGVHFVDTQLRSGWGPGPfppELPYVPGGEVAGVVDAVGPGVDPAWLGRRV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  90 IplytaecGVCKMCTSGKTNLcsAVRETQGKGLMPDGTtrfykdgepiyhymgcstfseytvlpeislakvnkeAPLEEV 169
Cdd:cd08244    88 V-------AHTGRAGGGYAEL--AVADVDSLHPVPDGL------------------------------------DLEAAV 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 170 CLLGCGVTTgMGaVMNTAKVEEGATVAIFGL-GGIGLSAVigaQMAKA--SRIIAIDINESKFELAKKLGATDCInpkDY 246
Cdd:cd08244   123 AVVHDGRTA-LG-LLDLATLTPGDVVLVTAAaGGLGSLLV---QLAKAagATVVGAAGGPAKTALVRALGADVAV---DY 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 247 DKP--IQDVIVELTDGGVDYSFECIGNvDVMRSALECCHKGwGESVIIGVAgAGQEISTRPFQLVTGRVWRGSAFGGVKG 324
Cdd:cd08244   195 TRPdwPDQVREALGGGGVTVVLDGVGG-AIGRAALALLAPG-GRFLTYGWA-SGEWTALDEDDARRRGVTVVGLLGVQAE 271
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2539978014 325 RSELPGYVERYL--AGDIPLQDFITHTMPLEDINEA 358
Cdd:cd08244   272 RGGLRALEARALaeAAAGRLVPVVGQTFPLERAAEA 307
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
13-89 8.01e-08

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


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 53.30  E-value: 8.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  13 AWGPNQPLSIEE----VDVMLPRKG----EVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQ 84
Cdd:cd08252     3 AIGFTQPLPITDpdslIDIELPKPVpggrDLLVRVEAVSVNPVDTKVRAGGAPVPGQPKILGWDASGVVEAVGSEVTLFK 82

                  ....*
gi 2539978014  85 VGDHV 89
Cdd:cd08252    83 VGDEV 87
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
13-270 1.41e-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: 52.61  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  13 AW-----GPNQPLS-IEEVDVMLPRK-GEVLVKIIASGVCHTDAFTLSG-----------------EDPEgvFPAILGHE 68
Cdd:cd08248     3 AWqihsyGGIDSLLlLENARIPVIRKpNQVLIKVHAASVNPIDVLMRSGygrtllnkkrkpqsckySGIE--FPLTLGRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  69 GGGIVEQIGEGVTSVQVGDHVIplytaecgvckmctsgktnlcsavretqgkglmpdGTTRFYKDGepiyhymgcsTFSE 148
Cdd:cd08248    81 CSGVVVDIGSGVKSFEIGDEVW-----------------------------------GAVPPWSQG----------THAE 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 149 YTVLPEISLAKVNKEAPLEEVCLLGCGVTTGMGAVMNTAKVEEGAT----VAIFG-LGGIGLSAVigaQMAKA--SRIIA 221
Cdd:cd08248   116 YVVVPENEVSKKPKNLSHEEAASLPYAGLTAWSALVNVGGLNPKNAagkrVLILGgSGGVGTFAI---QLLKAwgAHVTT 192
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2539978014 222 IdINESKFELAKKLGATDCInpkDYDKPiqDVIVELTD-GGVDYSFECIG 270
Cdd:cd08248   193 T-CSTDAIPLVKSLGADDVI---DYNNE--DFEEELTErGKFDVILDTVG 236
PRK10754 PRK10754
NADPH:quinone reductase;
30-90 1.65e-07

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 52.43  E-value: 1.65e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2539978014  30 PRKGEVLVKIIASGVCHTDAFTLSGEDPEGVFPAILGHEGGGIVEQIGEGVTSVQVGDHVI 90
Cdd:PRK10754   26 PAENEVQVENKAIGINYIDTYIRSGLYPPPSLPSGLGTEAAGVVSKVGSGVKHIKVGDRVV 86
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
37-236 3.06e-05

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 45.07  E-value: 3.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014   37 VKIIASGVCHTDAFTLSGEDPEgvfPAILGHEGGGIVEQIGEGVTSVQVGDHVIplytaecgvckmctsgktnlcsavre 116
Cdd:smart00829   1 IEVRAAGLNFRDVLIALGLYPG---EAVLGGECAGVVTRVGPGVTGLAVGDRVM-------------------------- 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014  117 tqgkGLMPDGttrfykdgepiyhymgcstFSEYTVLPEISLAKVNKEAPLEEVCLLGCGVTTGMGAVMNTAKVEEGATVA 196
Cdd:smart00829  52 ----GLAPGA-------------------FATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYYALVDLARLRPGESVL 108
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2539978014  197 IF-GLGGIGLSAVIGAQMAKAsRIIAIDINESKFELAKKLG 236
Cdd:smart00829 109 IHaAAGGVGQAAIQLARHLGA-EVFATAGSPEKRDFLRALG 148
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
19-80 6.54e-05

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


Pssm-ID: 176251 [Multi-domain]  Cd Length: 324  Bit Score: 44.52  E-value: 6.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2539978014  19 PLSIEEVDVMLPRKGEVLVKIIASGVCHTDAFTLSGE-DPEGVFPAILGHEGGGIVEQIGEGV 80
Cdd:cd08291    17 ELSLPEPEVPEPGPGEVLIKVEAAPINPSDLGFLKGQyGSTKALPVPPGFEGSGTVVAAGGGP 79
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
208-274 6.34e-04

AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group contains members identified in targeting of yeast membrane proteins ATPase. AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast, identified as a multicopy suppressor of pma1 mutants which cause temperature sensitive growth arrest due to the inability of ATPase to target to the cell surface. This family is homologous to the medium chain family of dehydrogenases and reductases. Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176209 [Multi-domain]  Cd Length: 352  Bit Score: 41.48  E-value: 6.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 208 VIGA---------QMAK----ASRIIAIdINESKFELAKKLGATDCINPKDYD--KPIQDVIVELTDGG-VDYSFECIGN 271
Cdd:cd08247   157 VLGGstsvgrfaiQLAKnhynIGTVVGT-CSSRSAELNKKLGADHFIDYDAHSgvKLLKPVLENVKGQGkFDLILDCVGG 235

                  ...
gi 2539978014 272 VDV 274
Cdd:cd08247   236 YDL 238
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
131-270 1.40e-03

Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176190 [Multi-domain]  Cd Length: 329  Bit Score: 40.16  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 131 YKDGEPIYHYMGcstFSEYTVLPEIS-LAKVNKEAPLEEVCLLG-CGVTtGMGA---VMNTAKVEEGATVAIFGLGGigl 205
Cdd:cd05288    84 FKVGDLVSGFLG---WQEYAVVDGASgLRKLDPSLGLPLSAYLGvLGMT-GLTAyfgLTEIGKPKPGETVVVSAAAG--- 156
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539978014 206 sAV--IGAQMAKA--SRIIAIDINESKFELAKK-LGATDCINPKDYDkpIQDVIVELTDGGVDYSFECIG 270
Cdd:cd05288   157 -AVgsVVGQIAKLlgARVVGIAGSDEKCRWLVEeLGFDAAINYKTPD--LAEALKEAAPDGIDVYFDNVG 223
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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