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Conserved domains on  [gi|16128591|ref|NP_415141|]
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putative Zn(2(+))-dependent alcohol dehydrogenase YbdR [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

zinc-dependent alcohol dehydrogenase( domain architecture ID 10169674)

zinc-dependent alcohol dehydrogenase such as glutathione-dependent formaldehyde dehydrogenase converts formaldehyde and NAD(P) to formate and NAD(P)H; 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
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
1-388 0e+00

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: 613.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08283   1 MKALVWHGKGDVRVEEVPDPKIEDPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGPEVRNLKVGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCFFCRLQQYAACENTNAGKGAAlnKKQIPAPAALFGYSHLYGGVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd08283  81 RVVVPFTIACGECFYCKRGLYSQCDNTNPSAEMA--KLYGHAGAGIFGYSHLTGGYAGGQAEYVRVPFADVGPFKIPDDL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 161 SDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPINFDE 240
Cdd:cd08283 159 SDEKALFLSDILPTGYHAAELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLGAETINFEE 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 241 DSDPAQSIIEQTaGHRGVDAVIDAVGFEAKGSTTETVLTN-LKLEGSSGKALRQCIAAVRRGGIVSVPGVYAGFIHGFLF 319
Cdd:cd08283 239 VDDVVEALRELT-GGRGPDVCIDAVGMEAHGSPLHKAEQAlLKLETDRPDALREAIQAVRKGGTVSIIGVYGGTVNKFPI 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128591 320 GDAFDKGLSFKMGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEECRKVILVP 388
Cdd:cd08283 318 GAAMNKGLTLRMGQTHVQRYLPRLLELIESGELDPSFIITHRLPLEDAPEAYKIFDKKEDGCIKVVLKP 386
 
Name Accession Description Interval E-value
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
1-388 0e+00

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: 613.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08283   1 MKALVWHGKGDVRVEEVPDPKIEDPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGPEVRNLKVGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCFFCRLQQYAACENTNAGKGAAlnKKQIPAPAALFGYSHLYGGVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd08283  81 RVVVPFTIACGECFYCKRGLYSQCDNTNPSAEMA--KLYGHAGAGIFGYSHLTGGYAGGQAEYVRVPFADVGPFKIPDDL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 161 SDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPINFDE 240
Cdd:cd08283 159 SDEKALFLSDILPTGYHAAELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLGAETINFEE 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 241 DSDPAQSIIEQTaGHRGVDAVIDAVGFEAKGSTTETVLTN-LKLEGSSGKALRQCIAAVRRGGIVSVPGVYAGFIHGFLF 319
Cdd:cd08283 239 VDDVVEALRELT-GGRGPDVCIDAVGMEAHGSPLHKAEQAlLKLETDRPDALREAIQAVRKGGTVSIIGVYGGTVNKFPI 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128591 320 GDAFDKGLSFKMGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEECRKVILVP 388
Cdd:cd08283 318 GAAMNKGLTLRMGQTHVQRYLPRLLELIESGELDPSFIITHRLPLEDAPEAYKIFDKKEDGCIKVVLKP 386
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
1-389 4.21e-132

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: 382.95  E-value: 4.21e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:COG1063   1 MKALVLHGPGDLRLEEVPDP-EPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCFFCRLQQYAACENTNAgkgaalnkkqipapaalFGYSHlyggVPGGQAEYVRVPKGNVgpFKVPPLL 160
Cdd:COG1063  80 RVVVEPNIPCGECRYCRRGRYNLCENLQF-----------------LGIAG----RDGGFAEYVRVPAANL--VKVPDGL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 161 SDDkALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGA-IPINFD 239
Cdd:COG1063 137 SDE-AAALVEPLAVALHAVERAGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELAR-ELGAdAVVNPR 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 240 EDsDPAQSIIEQTAGhRGVDAVIDAVGFEAkgsttetvltnlklegssgkALRQCIAAVRRGGIVSVPGVYAGFIhGFLF 319
Cdd:COG1063 215 EE-DLVEAVRELTGG-RGADVVIEAVGAPA--------------------ALEQALDLVRPGGTVVLVGVPGGPV-PIDL 271
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 320 GDAFDKGLSFKMGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEECRKVILVPG 389
Cdd:COG1063 272 NALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPLITHRFPLDDAPEAFEAAADRADGAIKVVLDPD 341
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
1-388 7.04e-44

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 155.75  E-value: 7.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    1 MKALTYHGPHH----VQVEnVPDPGVeqaDDIILRITATAICGSDLHLY--------RGKIPQVkhgdiFGHEFMGEVVE 68
Cdd:PRK05396   1 MKALVKLKAEPglwlTDVP-VPEPGP---NDVLIKVKKTAICGTDVHIYnwdewaqkTIPVPMV-----VGHEFVGEVVE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   69 TGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACENTnagKGAALNkkqipapaalfgyshlyggVPGGQAEYVRVPK 148
Cdd:PRK05396  72 VGSEVTGFKVGDRVSGEGHIVCGHCRNCRAGRRHLCRNT---KGVGVN-------------------RPGAFAEYLVIPA 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  149 GNVgpFKVPPLLSDDKALFLsDILPTAWQAAKNAQIQqGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAA 228
Cdd:PRK05396 130 FNV--WKIPDDIPDDLAAIF-DPFGNAVHTALSFDLV-GEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELAR 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  229 dRYGA-IPINFDEDsDPAQSIIEQTAGHrGVDavidaVGFEAKGsttetvltnlklegsSGKALRQCIAAVRRGGIVSVP 307
Cdd:PRK05396 206 -KMGAtRAVNVAKE-DLRDVMAELGMTE-GFD-----VGLEMSG---------------APSAFRQMLDNMNHGGRIAML 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  308 GVYAGFIhGFLFGDAFDKGLSFK------MGQThvhaWLgELLPLIEKGL-LKPeeIVTHYMPFEEAARGYEIFekREEE 380
Cdd:PRK05396 263 GIPPGDM-AIDWNKVIFKGLTIKgiygreMFET----WY-KMSALLQSGLdLSP--IITHRFPIDDFQKGFEAM--RSGQ 332

                 ....*...
gi 16128591  381 CRKVILVP 388
Cdd:PRK05396 333 SGKVILDW 340
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
26-151 1.74e-38

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: 134.27  E-value: 1.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    26 DDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACE 105
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYNLCP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 16128591   106 NtnagkgaalnkkqipapAALFGYshlygGVPGGQAEYVRVPKGNV 151
Cdd:pfam08240  81 N-----------------GRFLGY-----DRDGGFAEYVVVPERNL 104
adh_fam_2 TIGR02822
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
8-212 5.16e-12

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


Pssm-ID: 131869 [Multi-domain]  Cd Length: 329  Bit Score: 66.48  E-value: 5.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591     8 GPHHVQVENVPDPGveqADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFV 87
Cdd:TIGR02822  13 GPLRFVERPVPRPG---PGELLVRVRACGVCRTDLHVSEGDLPVHRPRVTPGHEVVGEVAGRGADAGGFAVGDRVGIAWL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    88 -IACGDCFFCRLQQYAACENTNagkgaalnkkqipapaalfgyshlYGG--VPGGQAEYVRVPKGNVgpFKVPPLLSDDK 164
Cdd:TIGR02822  90 rRTCGVCRYCRRGAENLCPASR------------------------YTGwdTDGGYAEYTTVPAAFA--YRLPTGYDDVE 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 16128591   165 --ALFLSDILptAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAE 212
Cdd:TIGR02822 144 laPLLCAGII--GYRALLRASLPPGGRLGLYGFGGSAHLTAQVALAQGAT 191
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
41-354 7.27e-11

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 62.41  E-value: 7.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591     41 DLHLYRGKIPqvkHGDIFGHEFMGEVVETGKDVKNLQKGDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqi 120
Cdd:smart00829  12 DVLIALGLYP---GEAVLGGECAGVVTRVGPGVTGLAVGDRVM------------------------------------- 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    121 papaalfgyshlyGGVPGGQAEYVRVPKGNVgpFKVPPLLSDDKALFLSDILPTAWQAAKN-AQIQQGSSVAVY-GAGPV 198
Cdd:smart00829  52 -------------GLAPGAFATRVVTDARLV--VPIPDGWSFEEAATVPVVFLTAYYALVDlARLRPGESVLIHaAAGGV 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    199 GLLTIACARLLGAEqIFVVDHHPYRLHFaADRYGaIPIN--FD-EDSDPAQSIIEQTAGhRGVDAVIDAVgfeakgstte 275
Cdd:smart00829 117 GQAAIQLARHLGAE-VFATAGSPEKRDF-LRALG-IPDDhiFSsRDLSFADEILRATGG-RGVDVVLNSL---------- 182
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    276 tvltnlklegsSGKALRQCIAAVRRGGIvsvpgvyagFI---------HGFLFGDAFDKGLSF------KM--GQTHVHA 338
Cdd:smart00829 183 -----------SGEFLDASLRCLAPGGR---------FVeigkrdirdNSQLAMAPFRPNVSYhavdldALeeGPDRIRE 242
                          330
                   ....*....|....*.
gi 16128591    339 WLGELLPLIEKGLLKP 354
Cdd:smart00829 243 LLAEVLELFAEGVLRP 258
 
Name Accession Description Interval E-value
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
1-388 0e+00

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: 613.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08283   1 MKALVWHGKGDVRVEEVPDPKIEDPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGPEVRNLKVGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCFFCRLQQYAACENTNAGKGAAlnKKQIPAPAALFGYSHLYGGVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd08283  81 RVVVPFTIACGECFYCKRGLYSQCDNTNPSAEMA--KLYGHAGAGIFGYSHLTGGYAGGQAEYVRVPFADVGPFKIPDDL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 161 SDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPINFDE 240
Cdd:cd08283 159 SDEKALFLSDILPTGYHAAELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLGAETINFEE 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 241 DSDPAQSIIEQTaGHRGVDAVIDAVGFEAKGSTTETVLTN-LKLEGSSGKALRQCIAAVRRGGIVSVPGVYAGFIHGFLF 319
Cdd:cd08283 239 VDDVVEALRELT-GGRGPDVCIDAVGMEAHGSPLHKAEQAlLKLETDRPDALREAIQAVRKGGTVSIIGVYGGTVNKFPI 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128591 320 GDAFDKGLSFKMGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEECRKVILVP 388
Cdd:cd08283 318 GAAMNKGLTLRMGQTHVQRYLPRLLELIESGELDPSFIITHRLPLEDAPEAYKIFDKKEDGCIKVVLKP 386
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
1-388 1.77e-172

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: 485.63  E-value: 1.77e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd05278   1 MKALVYLGPGKIGLEEVPDPKIQGPHDAIVRVTATSICGSDLHIYRGGVPGAKHGMILGHEFVGEVVEVGSDVKRLKPGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCFFCRLQQYAACENTNAGKGaalnkkqipapaalfgyshLYGGVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd05278  81 RVSVPCITFCGRCRFCRRGYHAHCENGLWGWK-------------------LGNRIDGGQAEYVRVPYADMNLAKIPDGL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 161 SDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPINFDE 240
Cdd:cd05278 142 PDEDALMLSDILPTGFHGAELAGIKPGSTVAVIGAGPVGLCAVAGARLLGAARIIAVDSNPERLDLAKEAGATDIINPKN 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 241 DsDPAQSIIEQTaGHRGVDAVIDAVGFEAkgsttetvltnlklegssgkALRQCIAAVRRGGIVSVPGVYAGFIHGFLFG 320
Cdd:cd05278 222 G-DIVEQILELT-GGRGVDCVIEAVGFEE--------------------TFEQAVKVVRPGGTIANVGVYGKPDPLPLLG 279
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128591 321 DAFDKGLSFKMGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEECRKVILVP 388
Cdd:cd05278 280 EWFGKNLTFKTGLVPVRARMPELLDLIEEGKIDPSKLITHRFPLDDILKAYRLFDNKPDGCIKVVIRP 347
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
1-389 4.21e-132

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: 382.95  E-value: 4.21e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:COG1063   1 MKALVLHGPGDLRLEEVPDP-EPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCFFCRLQQYAACENTNAgkgaalnkkqipapaalFGYSHlyggVPGGQAEYVRVPKGNVgpFKVPPLL 160
Cdd:COG1063  80 RVVVEPNIPCGECRYCRRGRYNLCENLQF-----------------LGIAG----RDGGFAEYVRVPAANL--VKVPDGL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 161 SDDkALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGA-IPINFD 239
Cdd:COG1063 137 SDE-AAALVEPLAVALHAVERAGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELAR-ELGAdAVVNPR 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 240 EDsDPAQSIIEQTAGhRGVDAVIDAVGFEAkgsttetvltnlklegssgkALRQCIAAVRRGGIVSVPGVYAGFIhGFLF 319
Cdd:COG1063 215 EE-DLVEAVRELTGG-RGADVVIEAVGAPA--------------------ALEQALDLVRPGGTVVLVGVPGGPV-PIDL 271
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 320 GDAFDKGLSFKMGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEECRKVILVPG 389
Cdd:COG1063 272 NALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPLITHRFPLDDAPEAFEAAADRADGAIKVVLDPD 341
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
1-388 7.07e-127

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: 369.66  E-value: 7.07e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08284   1 MKAVVFKGPGDVRVEEVPIPQIQDPTDAIVKVTAAAICGSDLHIYRGHIP-STPGFVLGHEFVGEVVEVGPEVRTLKVGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCFFCRLQQYAACENTNagkgaalnkkqipapaaLFGYShLYGGVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd08284  80 RVVSPFTIACGECFYCRRGQSGRCAKGG-----------------LFGYA-GSPNLDGAQAEYVRVPFADGTLLKLPDGL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 161 SDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRyGAIPINFDE 240
Cdd:cd08284 142 SDEAALLLGDILPTGYFGAKRAQVRPGDTVAVIGCGPVGLCAVLSAQVLGAARVFAVDPVPERLERAAAL-GAEPINFED 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 241 DsDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVPGVYAGfiHGFLF- 319
Cdd:cd08284 221 A-EPVERVREATEG-RGADVVLEAVG--------------------GAAALDLAFDLVRPGGVISSVGVHTA--EEFPFp 276
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 320 -GDAFDKGLSFKMGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEecRKVILVP 388
Cdd:cd08284 277 gLDAYNKNLTLRFGRCPVRSLFPELLPLLESGRLDLEFLIDHRMPLEEAPEAYRLFDKRKV--LKVVLDP 344
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
1-388 1.08e-117

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: 347.66  E-value: 1.08e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08282   1 MKAVVYGGPGNVAVEDVPDPKIEHPTDAIVRITTTAICGSDLHMYRGRTG-AEPGLVLGHEAMGEVEEVGSAVESLKVGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCFFCRLQQYAACENTNAGkgaalnkkqipAPAALFGYSHLyGGVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd08282  80 RVVVPFNVACGRCRNCKRGLTGVCLTVNPG-----------RAGGAYGYVDM-GPYGGGQAEYLRVPYADFNLLKLPDRD 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 161 SDDKA---LFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGAIPIN 237
Cdd:cd08282 148 GAKEKddyLMLSDIFPTGWHGLELAGVQPGDTVAVFGAGPVGLMAAYSAILRGASRVYVVDHVPERLDLAE-SIGAIPID 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 238 FdEDSDPAQSIIEQTAGhrGVDAVIDAVGFEAkgsttetvlTNLKLEGSSGKALRQCIAAVRRGGIVSVPGVYAGF---- 313
Cdd:cd08282 227 F-SDGDPVEQILGLEPG--GVDRAVDCVGYEA---------RDRGGEAQPNLVLNQLIRVTRPGGGIGIVGVYVAEdpga 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 314 -----IHG---FLFGDAFDKGLSFKMGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEecRKVI 385
Cdd:cd08282 295 gdaaaKQGelsFDFGLLWAKGLSFGTGQAPVKKYNRQLRDLILAGRAKPSFVVSHVISLEDAPEAYARFDKRLE--TKVV 372

                ...
gi 16128591 386 LVP 388
Cdd:cd08282 373 IKP 375
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
1-386 6.45e-78

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: 244.85  E-value: 6.45e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08286   1 MKALVYHGPGKISWEDRPKPTIQEPTDAIVKMLKTTICGTDLHILKGDVPTVTPGRILGHEGVGVVEEVGSAVTNFKVGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCFFCRLQQYAACENTnagkgaalnkkqipapAALFGYShlyggVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd08286  81 RVLISCISSCGTCGYCRKGLYSHCESG----------------GWILGNL-----IDGTQAEYVRIPHADNSLYKLPEGV 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 161 SDDKALFLSDILPTAWQ-AAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHfAADRYGAIPINFD 239
Cdd:cd08286 140 DEEAAVMLSDILPTGYEcGVLNGKVKPGDTVAIVGAGPVGLAALLTAQLYSPSKIIMVDLDDNRLE-VAKKLGATHTVNS 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 240 EDSDPAQSIIEQTAGhRGVDAVIDAVGFEAkgsTTETvltnlklegssgkalrqCIAAVRRGGIVSVPGVyagfiHG--- 316
Cdd:cd08286 219 AKGDAIEQVLELTDG-RGVDVVIEAVGIPA---TFEL-----------------CQELVAPGGHIANVGV-----HGkpv 272
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128591 317 -FLFGDAFDKGLSFKMGQTHVHAWlGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEK-REEECRKVIL 386
Cdd:cd08286 273 dLHLEKLWIKNITITTGLVDTNTT-PMLLKLVSSGKLDPSKLVTHRFKLSEIEKAYDTFSAaAKHKALKVII 343
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
1-388 4.69e-76

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: 239.90  E-value: 4.69e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIfGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08287   1 MRATVIHGPGDIRVEEVPDPVIEEPTDAVIRVVATCVCGSDLWPYRGVSPTRAPAPI-GHEFVGVVEEVGSEVTSVKPGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkkqipapAALFGyshlyGGVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd08287  80 FVIAPFAISDGTCPFCRAGFTTSCVH-----------------GGFWG-----AFVDGGQGEYVRVPLADGTLVKVPGSP 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 161 SDDKALF-----LSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGAIP 235
Cdd:cd08287 138 SDDEDLLpsllaLSDVMGTGHHAAVSAGVRPGSTVVVVGDGAVGLCAVLAAKRLGAERIIAMSRHEDRQALAR-EFGATD 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 236 INFDEDSDPAQSIIEQTAGHrGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVPGVYAGFIh 315
Cdd:cd08287 217 IVAERGEEAVARVRELTGGV-GADAVLECVG--------------------TQESMEQAIAIARPGGRVGYVGVPHGGV- 274
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128591 316 GFLFGDAFDKGLSFKMGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKReeECRKVILVP 388
Cdd:cd08287 275 ELDVRELFFRNVGLAGGPAPVRRYLPELLDDVLAGRINPGRVFDLTLPLDEVAEGYRAMDER--RAIKVLLRP 345
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
1-386 6.09e-65

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 210.93  E-value: 6.09e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVkHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08236   1 MKALVLTGPGDLRYEDIPKP-EPGPGEVLVKVKACGICGSDIPRYLGTGAYH-PPLVLGHEFSGTVEEVGSGVDDLAVGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCFFCRLQQYAACENTNagkgaalnkkqipapaaLFGySHLyggvPGGQAEYVRVPKGNVgpFKVPPLL 160
Cdd:cd08236  79 RVAVNPLLPCGKCEYCKKGEYSLCSNYD-----------------YIG-SRR----DGAFAEYVSVPARNL--IKIPDHV 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 161 SDDKALFLsDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADrYGAiPINFDE 240
Cdd:cd08236 135 DYEEAAMI-EPAAVALHAVRLAGITLGDTVVVIGAGTIGLLAIQWLKILGAKRVIAVDIDDEKLAVARE-LGA-DDTINP 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 241 DSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVsvpgVYAG------FI 314
Cdd:cd08236 212 KEEDVEKVRELTEG-RGADLVIEAAG--------------------SPATIEQALALARPGGKV----VLVGipygdvTL 266
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128591 315 HGFLFGDAFDKGLSFKMGQTHVHAWLG-----ELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEECRKVIL 386
Cdd:cd08236 267 SEEAFEKILRKELTIQGSWNSYSAPFPgdewrTALDLLASGKIKVEPLITHRLPLEDGPAAFERLADREEFSGKVLL 343
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
1-385 6.09e-64

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 208.04  E-value: 6.09e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHH-VQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKG 79
Cdd:COG1064   1 MKAAVLTEPGGpLELEEVPRPEPG-PGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGVTGFKVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  80 DRVVIPFVIACGDCFFCR--LQQYaaCENtnagkgaalnkkqipapAALFGYSHlyggvPGGQAEYVRVPKGNVgpFKVP 157
Cdd:COG1064  80 DRVGVGWVDSCGTCEYCRsgRENL--CEN-----------------GRFTGYTT-----DGGYAEYVVVPARFL--VKLP 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 158 PLLSDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFA----ADRYGA 233
Cdd:COG1064 134 DGLDPAEAAPLLCAGITAYRALRRAGVGPGDRVAVIGAGGLGHLAVQIAKALGAE-VIAVDRSPEKLELArelgADHVVN 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 234 IpinfdEDSDPAQSIieqtAGHRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVPGVYAGF 313
Cdd:COG1064 213 S-----SDEDPVEAV----RELTGADVVIDTVG--------------------APATVNAALALLRRGGRLVLVGLPGGP 263
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128591 314 IHGFLFgDAFDKGLSFK----MGQTHvhawLGELLPLIEKGLLKPEeiVTHYmPFEEAARGYEIFEKREEECRKVI 385
Cdd:COG1064 264 IPLPPF-DLILKERSIRgsliGTRAD----LQEMLDLAAEGKIKPE--VETI-PLEEANEALERLRAGKVRGRAVL 331
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
1-387 9.22e-63

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: 205.07  E-value: 9.22e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYRGKiPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08234   1 MKALVYEGPGELEVEEVPVPEP-GPDEVLIKVAACGICGTDLHIYEGE-FGAAPPLVPGHEFAGVVVAVGSKVTGFKVGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCFFCRLQQYAACENTNAgkgaalnkkqipapaalfgyshlYG-GVPGGQAEYVRVPKGNVgpFKVPPL 159
Cdd:cd08234  79 RVAVDPNIYCGECFYCRRGRPNLCENLTA-----------------------VGvTRNGGFAEYVVVPAKQV--YKIPDN 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 160 LSDDKALFLsDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPINFD 239
Cdd:cd08234 134 LSFEEAALA-EPLSCAVHGLDLLGIKPGDSVLVFGAGPIGLLLAQLLKLNGASRVTVAEPNEEKLELAKKLGATETVDPS 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 240 EDSDPAQSIIeqtaGHRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVPGVYAgfiHGFLF 319
Cdd:cd08234 213 REDPEAQKED----NPYGFDVVIEATG--------------------VPKTLEQAIEYARRGGTVLVFGVYA---PDARV 265
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128591 320 G----DAFDKGLSFK--MGQTHVHawlGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEecRKVILV 387
Cdd:cd08234 266 SispfEIFQKELTIIgsFINPYTF---PRAIALLESGKIDVKGLVSHRLPLEEVPEALEGMRSGGA--LKVVVV 334
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
1-379 9.97e-62

L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176197 [Multi-domain]  Cd Length: 343  Bit Score: 202.83  E-value: 9.97e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPGVEQaDDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08235   1 MKAAVLHGPNDVRLEEVPVPEPGP-GEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGDGVTGFKVGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkkqipapaaLFGYSHLYggvPGGQAEYVRVPKGNV---GPFKVP 157
Cdd:cd08235  80 RVFVAPHVPCGECHYCLRGNENMCPN-------------------YKKFGNLY---DGGFAEYVRVPAWAVkrgGVLKLP 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 158 PLLSDDKALfLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPIN 237
Cdd:cd08235 138 DNVSFEEAA-LVEPLACCINAQRKAGIKPGDTVLVIGAGPIGLLHAMLAKASGARKVIVSDLNEFRLEFAKKLGADYTID 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 238 FDEDsDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSvpgVYAGFIHGF 317
Cdd:cd08235 217 AAEE-DLVEKVRELTDG-RGADVVIVATG--------------------SPEAQAQALELVRKGGRIL---FFGGLPKGS 271
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128591 318 LFgdAFDKGLsFKMGQTHVHAWLG-------ELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREE 379
Cdd:cd08235 272 TV--NIDPNL-IHYREITITGSYAaspedykEALELIASGKIDVKDLITHRFPLEDIEEAFELAADGKS 337
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
1-386 6.43e-61

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: 200.49  E-value: 6.43e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08261   1 MKALVCEKPGRLEVVDIPEPVPG-AGEVLVRVKRVGICGSDLHIYHGRNPFASYPRILGHELSGEVVEVGEGVAGLKVGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCFFCRLQQYAACENTNagkgaalnkkqipapaaLFGySHlyggVPGGQAEYVRVPKGNVgpfKVPPLL 160
Cdd:cd08261  80 RVVVDPYISCGECYACRKGRPNCCENLQ-----------------VLG-VH----RDGGFAEYIVVPADAL---LVPEGL 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 161 SDDKALfLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGAIPINFDE 240
Cdd:cd08261 135 SLDQAA-LVEPLAIGAHAVRRAGVTAGDTVLVVGAGPIGLGVIQVAKARGAR-VIVVDIDDERLEFARELGADDTINVGD 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 241 DsDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVsvpgVYAGFIHGFLfg 320
Cdd:cd08261 213 E-DVAARLRELTDG-EGADVVIDATG--------------------NPASMEEAVELVAHGGRV----VLVGLSKGPV-- 264
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128591 321 dAFDkGLSFKMGQTHVHA---WLGELLP----LIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEECRKVIL 386
Cdd:cd08261 265 -TFP-DPEFHKKELTILGsrnATREDFPdvidLLESGKVDPEALITHRFPFEDVPEAFDLWEAPPGGVIKVLI 335
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
1-388 6.69e-61

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: 200.93  E-value: 6.69e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08285   1 MKAFAMLGIGKVGWIEKPIP-VCGPNDAIVRPTAVAPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGSEVKDFKPGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCffcrlqqyaacentnagkgaalnkkqipaPAALFGYSHLYGGVPGG----------QAEYVRVPKGN 150
Cdd:cd08285  80 RVIVPAITPDWRS-----------------------------VAAQRGYPSQSGGMLGGwkfsnfkdgvFAEYFHVNDAD 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 151 VGPFKVPPLLSDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHfAADR 230
Cdd:cd08285 131 ANLAPLPDGLTDEQAVMLPDMMSTGFHGAELANIKLGDTVAVFGIGPVGLMAVAGARLRGAGRIIAVGSRPNRVE-LAKE 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 231 YGAIPI-NFDEdSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsTTETvltnlklegssgkaLRQCIAAVRRGGIVSVPGV 309
Cdd:cd08285 210 YGATDIvDYKN-GDVVEQILKLTGG-KGVDAVIIAGG------GQDT--------------FEQALKVLKPGGTISNVNY 267
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 310 YAGFIHGFLFGDAFDKGLSFKMGQTHV----HAWLGELLPLIEKGLLKPEE-IVTHYMPFEEAARGYEIFEKREEECRKV 384
Cdd:cd08285 268 YGEDDYLPIPREEWGVGMGHKTINGGLcpggRLRMERLASLIEYGRVDPSKlLTHHFFGFDDIEEALMLMKDKPDDLIKP 347

                ....
gi 16128591 385 ILVP 388
Cdd:cd08285 348 VIIF 351
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
1-359 5.46e-59

(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: 195.84  E-value: 5.46e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYRGK---IPQVKHGDI--------FGHEFMGEVVET 69
Cdd:cd08233   1 MKAARYHGRKDIRVEEVPEPPV-KPGEVKIKVAWCGICGSDLHEYLDGpifIPTEGHPHLtgetapvtLGHEFSGVVVEV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  70 GKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkkqipapaalFGYSHLyGGVPGGQAEYVRVPKG 149
Cdd:cd08233  80 GSGVTGFKVGDRVVVEPTIKCGTCGACKRGLYNLCDS--------------------LGFIGL-GGGGGGFAEYVVVPAY 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 150 NVgpFKVPPLLSDDKALfLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAD 229
Cdd:cd08233 139 HV--HKLPDNVPLEEAA-LVEPLAVAWHAVRRSGFKPGDTALVLGAGPIGLLTILALKAAGASKIIVSEPSEARRELAEE 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 230 RYGAIPINFDEDsDPAQSIIEQTAGhRGVDAVIDAVGFEAkgsttetvltnlklegssgkALRQCIAAVRRGGIVSVPGV 309
Cdd:cd08233 216 LGATIVLDPTEV-DVVAEVRKLTGG-GGVDVSFDCAGVQA--------------------TLDTAIDALRPRGTAVNVAI 273
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 16128591 310 YAGFIhGFLFGDAFDKGLSFKMGQTHVHAWLGELLPLIEKGLLKPEEIVT 359
Cdd:cd08233 274 WEKPI-SFNPNDLVLKEKTLTGSICYTREDFEEVIDLLASGKIDAEPLIT 322
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
27-330 8.49e-59

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: 192.92  E-value: 8.49e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  27 DIILRITATAICGSDLHLYRGK-IPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRlqqyaace 105
Cdd:cd05188   1 EVLVRVEAAGLCGTDLHIRRGGyPPPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNLGCGTCELCR-------- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 106 ntnagkgaalnkkqipapAALFGYSHLYGGVPGGQAEYVRVPKGNVgpFKVPPLLSDDKALFLSDILPTAWQAAKNA-QI 184
Cdd:cd05188  73 ------------------ELCPGGGILGEGLDGGFAEYVVVPADNL--VPLPDGLSLEEAALLPEPLATAYHALRRAgVL 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 185 QQGSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGAIPINFDEDSDPAQsiiEQTAGHRGVDAVIDA 264
Cdd:cd05188 133 KPGDTVLVLGAGGVGLLAAQLAKAAGAR-VIVTDRSDEKLELAKELGADHVIDYKEEDLEEE---LRLTGGGGADVVIDA 208
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128591 265 VGFEAkgsttetvltnlklegssgkALRQCIAAVRRGGIVSVPGVYAGFIHGFLFGDAFDKGLSFK 330
Cdd:cd05188 209 VGGPE--------------------TLAQALRLLRPGGRIVVVGGTSGGPPLDDLRRLLFKELTII 254
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
1-388 6.05e-55

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: 184.83  E-value: 6.05e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIF-GHEFMGEVVETGKDVKNLQKG 79
Cdd:cd08239   1 MRGAVFPGDRTVELREFPVP-VPGPGEVLLRVKASGLCGSDLHYYYHGHRAPAYQGVIpGHEPAGVVVAVGPGVTHFRVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  80 DRVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkkqipaPAALFGYSHlyggvPGGQAEYVRVPKGNVgpFKVPPL 159
Cdd:cd08239  80 DRVMVYHYVGCGACRNCRRGWMQLCTS----------------KRAAYGWNR-----DGGHAEYMLVPEKTL--IPLPDD 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 160 LSDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADrYGAIPInFD 239
Cdd:cd08239 137 LSFADGALLLCGIGTAYHALRRVGVSGRDTVLVVGAGPVGLGALMLARALGAEDVIGVDPSPERLELAKA-LGADFV-IN 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 240 EDSDPAQSIIEQTAGhRGVDAVIDAVGFEAkgsttetvltnlklegssgkALRQCIAAVRRGGIVSVPGVYAGFihgflf 319
Cdd:cd08239 215 SGQDDVQEIRELTSG-AGADVAIECSGNTA--------------------ARRLALEAVRPWGRLVLVGEGGEL------ 267
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128591 320 gdAFDKGLSFKMGQTHVHA-W------LGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKReeECRKVILVP 388
Cdd:cd08239 268 --TIEVSNDLIRKQRTLIGsWyfsvpdMEECAEFLARHKLEVDRLVTHRFGLDQAPEAYALFAQG--ESGKVVFVF 339
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
1-388 6.56e-53

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: 179.74  E-value: 6.56e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKAL--TYHGPHHVQVE-NVPDPGveqADDIILRITATAICGSDLHLY--------RGKIPQvkhgdIFGHEFMGEVVET 69
Cdd:cd05281   1 MKAIvkTKAGPGAELVEvPVPKPG---PGEVLIKVLAASICGTDVHIYewdewaqsRIKPPL-----IFGHEFAGEVVEV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  70 GKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACENTnagkgaalnkKQIpapaalfgyshlygGV--PGGQAEYVRVP 147
Cdd:cd05281  73 GEGVTRVKVGDYVSAETHIVCGKCYQCRTGNYHVCQNT----------KIL--------------GVdtDGCFAEYVVVP 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 148 KGNVgpFKVPPLLSDDKALfLSDILPTAWQAAKNAQIQqGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFA 227
Cdd:cd05281 129 EENL--WKNDKDIPPEIAS-IQEPLGNAVHTVLAGDVS-GKSVLITGCGPIGLMAIAVAKAAGASLVIASDPNPYRLELA 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 228 ADRYGAIPINFDEDsDPAQsIIEQTAGHrGVDAVIDAVGFEakgsttetvltnlklegssgKALRQCIAAVRRGGIVSVP 307
Cdd:cd05281 205 KKMGADVVINPREE-DVVE-VKSVTDGT-GVDVVLEMSGNP--------------------KAIEQGLKALTPGGRVSIL 261
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 308 GVYAGFIHGFLFGDAFDKGLSF------KMGQT--HVHAWLgellpliEKGLLKPEEIVTHYMPFEEAARGYEIFekREE 379
Cdd:cd05281 262 GLPPGPVDIDLNNLVIFKGLTVqgitgrKMFETwyQVSALL-------KSGKVDLSPVITHKLPLEDFEEAFELM--RSG 332

                ....*....
gi 16128591 380 ECRKVILVP 388
Cdd:cd05281 333 KCGKVVLYP 341
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
3-388 2.15e-52

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: 178.46  E-value: 2.15e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   3 ALTYHGPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYR-GKI--PQVKHGDIFGHEFMGEVVETGKDVKNLQKG 79
Cdd:cd05285   1 AAVLHGPGDLRLEERPIPEP-GPGEVLVRVRAVGICGSDVHYYKhGRIgdFVVKEPMVLGHESAGTVVAVGSGVTHLKVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  80 DRVVIPFVIACGDCFFCRLQQYAACENtnaGKGAAlnkkqipAPaalfgyshlygGVPGGQAEYVRVPKGNVgpFKVPPL 159
Cdd:cd05285  80 DRVAIEPGVPCRTCEFCKSGRYNLCPD---MRFAA-------TP-----------PVDGTLCRYVNHPADFC--HKLPDN 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 160 LSDDK-ALF--LSdilpTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGA--- 233
Cdd:cd05285 137 VSLEEgALVepLS----VGVHACRRAGVRPGDTVLVFGAGPIGLLTAAVAKAFGATKVVVTDIDPSRLEFAK-ELGAtht 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 234 IPINFDEDSDPAQSIIEQTAGhRGVDAVIDAVGFEakgsttetvltnlklegssgKALRQCIAAVRRGGIVSVPGVYAGF 313
Cdd:cd05285 212 VNVRTEDTPESAEKIAELLGG-KGPDVVIECTGAE--------------------SCIQTAIYATRPGGTVVLVGMGKPE 270
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128591 314 IHgFLFGDAFDKGLSFKMGQTHVHAWlgellP----LIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEECRKVILVP 388
Cdd:cd05285 271 VT-LPLSAASLREIDIRGVFRYANTY-----PtaieLLASGKVDVKPLITHRFPLEDAVEAFETAAKGKKGVIKVVIEG 343
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
1-372 2.59e-47

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: 165.08  E-value: 2.59e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHV-QVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKG 79
Cdd:cd08260   1 MRAAVYEEFGEPlEIREVPDPEPP-PDGVVVEVEACGVCRSDWHGWQGHDPDVTLPHVPGHEFAGVVVEVGEDVSRWRVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  80 DRVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkKQIPapaalfGYSHlyggvPGGQAEYVRVPKGNVGPFKVPPL 159
Cdd:cd08260  80 DRVTVPFVLGCGTCPYCRAGDSNVCEH-----------QVQP------GFTH-----PGSFAEYVAVPRADVNLVRLPDD 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 160 LSDDKALFLSDILPTAWQA-AKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAeQIFVVDHHPYRLHFaADRYGAIP-IN 237
Cdd:cd08260 138 VDFVTAAGLGCRFATAFRAlVHQARVKPGEWVAVHGCGGVGLSAVMIASALGA-RVIAVDIDDDKLEL-ARELGAVAtVN 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 238 FDEDSDPAQSIIEQTAGhrGVDAVIDAVGFEAkgsttetvltnlklegssgkALRQCIAAVRRGG-IVSVpgvyagfihG 316
Cdd:cd08260 216 ASEVEDVAAAVRDLTGG--GAHVSVDALGIPE--------------------TCRNSVASLRKRGrHVQV---------G 264
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 317 FLFGDafDKGLSFKMGQthVHAW--------------LGELLPLIEKGLLKPEEIVTHYMPFEEAARGYE 372
Cdd:cd08260 265 LTLGE--EAGVALPMDR--VVAReleivgshgmpahrYDAMLALIASGKLDPEPLVGRTISLDEAPDALA 330
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
1-386 3.85e-47

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: 164.89  E-value: 3.85e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRG---------KIPQVKHGDIFGHEFMGEVVETGK 71
Cdd:cd08256   1 MRAVVCHGPQDYRLEEVPVP-RPGPGEILVKVEACGICAGDIKCYHGapsfwgdenQPPYVKPPMIPGHEFVGRVVELGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  72 DVKN--LQKGDRVVIPFVIACGDCFFCRLQQYAACENTNagkgaalnkkqipapaaLFGYSHlygGVPGGQAEYVRVPKG 149
Cdd:cd08256  80 GAEErgVKVGDRVISEQIVPCWNCRFCNRGQYWMCQKHD-----------------LYGFQN---NVNGGMAEYMRFPKE 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 150 NVGpFKVPPLLSDDKALFLsDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAd 229
Cdd:cd08256 140 AIV-HKVPDDIPPEDAILI-EPLACALHAVDRANIKFDDVVVLAGAGPLGLGMIGAARLKNPKKLIVLDLKDERLALAR- 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 230 RYGA-IPINFDEDSDPAQsIIEQTAGHrGVDAVIDAVGFEakgsttetvltnlklegssgKALRQCIAAVRRGGIvsvpg 308
Cdd:cd08256 217 KFGAdVVLNPPEVDVVEK-IKELTGGY-GCDIYIEATGHP--------------------SAVEQGLNMIRKLGR----- 269
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 309 vyagFIHGFLFGDAF---------DKGLSFkMGqTHVHAWLGEL-LPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKRE 378
Cdd:cd08256 270 ----FVEFSVFGDPVtvdwsiigdRKELDV-LG-SHLGPYCYPIaIDLIASGRLPTDGIVTHQFPLEDFEEAFELMARGD 343

                ....*...
gi 16128591 379 EECrKVIL 386
Cdd:cd08256 344 DSI-KVVL 350
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
13-372 1.15e-46

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 163.71  E-value: 1.15e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  13 QVENV--PDPGveqADDIILRITATAICGSDLHLYRGKIPQVKHGdIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIAC 90
Cdd:COG1062   5 EIEEVelDEPR---PGEVLVRIVAAGLCHSDLHVRDGDLPVPLPA-VLGHEGAGVVEEVGPGVTGVAPGDHVVLSFIPSC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  91 GDCFFCRLQQYAACENtnagkGAALNKK--QIPAPAALfgysHLYGGVP-------GGQAEYVRVPKGNVgpFKVPPLLS 161
Cdd:COG1062  81 GHCRYCASGRPALCEA-----GAALNGKgtLPDGTSRL----SSADGEPvghffgqSSFAEYAVVPERSV--VKVDKDVP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 162 DDKALFLSDILPTAWQAAKN-AQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGAIP-INfD 239
Cdd:COG1062 150 LELAALLGCGVQTGAGAVLNtAKVRPGDTVAVFGLGGVGLSAVQGARIAGASRIIAVDPVPEKLELAR-ELGATHtVN-P 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 240 EDSDPAQSIIEQTAGhrGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGG---IVSVPGVYAGF-IH 315
Cdd:COG1062 228 ADEDAVEAVRELTGG--GVDYAFETTG--------------------NPAVIRQALEALRKGGtvvVVGLAPPGAEIsLD 285
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 316 GFlfgDAFDKGLSFK---MGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYE 372
Cdd:COG1062 286 PF---QLLLTGRTIRgsyFGGAVPRRDIPRLVDLYRAGRLPLDELITRRYPLDEINEAFD 342
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
1-386 2.03e-45

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: 160.40  E-value: 2.03e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHH-VQVENV--PDPGveqADDIILRITATAICGSDLHLYRGKIPQVKHGdIFGHEFMGEVVETGKDVKNLQ 77
Cdd:cd08279   1 MRAAVLHEVGKpLEIEEVelDDPG---PGEVLVRIAAAGLCHSDLHVVTGDLPAPLPA-VLGHEGAGVVEEVGPGVTGVK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  78 KGDRVVIPFVIACGDCFFCRLQQYAACENtnagkGAALNKKQIPAPAalfgYSHLYGGVPGGQ-------AEYVRVPKGN 150
Cdd:cd08279  77 PGDHVVLSWIPACGTCRYCSRGQPNLCDL-----GAGILGGQLPDGT----RRFTADGEPVGAmcglgtfAEYTVVPEAS 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 151 VGpfKVPPLLSDDKALFLSDILPTAWQAAKN-AQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAd 229
Cdd:cd08279 148 VV--KIDDDIPLDRAALLGCGVTTGVGAVVNtARVRPGDTVAVIGCGGVGLNAIQGARIAGASRIIAVDPVPEKLELAR- 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 230 RYGAIPINFDEDSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsTTETVltnlklegssgkalRQCIAAVRRGG---IVSV 306
Cdd:cd08279 225 RFGATHTVNASEDDAVEAVRDLTDG-RGADYAFEAVG------RAATI--------------RQALAMTRKGGtavVVGM 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 307 PGVYAGF-IHGFLFGdAFDKGL-SFKMGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFeKREEECRKV 384
Cdd:cd08279 284 GPPGETVsLPALELF-LSEKRLqGSLYGSANPRRDIPRLLDLYRAGRLKLDELVTRRYSLDEINEAFADM-LAGENARGV 361

                ..
gi 16128591 385 IL 386
Cdd:cd08279 362 IV 363
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
2-312 2.18e-45

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: 160.50  E-value: 2.18e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   2 KALTYHGPHH-VQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKN----- 75
Cdd:cd08231   2 RAAVLTGPGKpLEIREVPLPDLE-PGAVLVRVRLAGVCGSDVHTVAGRRPRVPLPIILGHEGVGRVVALGGGVTTdvage 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  76 -LQKGDRVVIPFVIACGDCFFCRLQQYAACEN-TNAGkgaalnkkqipaPAALFGYSHLYGGVpggqAEYVRVPKGnVGP 153
Cdd:cd08231  81 pLKVGDRVTWSVGAPCGRCYRCLVGDPTKCENrKKYG------------HEASCDDPHLSGGY----AEHIYLPPG-TAI 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 154 FKVPPLLSDDKALFLSDILPTAWQAAKNAQIQQ-GSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYG 232
Cdd:cd08231 144 VRVPDNVPDEVAAPANCALATVLAALDRAGPVGaGDTVVVQGAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAR-EFG 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 233 AIP-INFDEDSDP-AQSIIEQTAGHRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVPGVY 310
Cdd:cd08231 223 ADAtIDIDELPDPqRRAIVRDITGGRGADVVIEASG--------------------HPAAVPEGLELLRRGGTYVLVGSV 282

                ..
gi 16128591 311 AG 312
Cdd:cd08231 283 AP 284
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
1-386 4.24e-45

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


Pssm-ID: 176224 [Multi-domain]  Cd Length: 367  Bit Score: 159.84  E-value: 4.24e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHH-VQVENVPDPGvEQADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKN---L 76
Cdd:cd08263   1 MKAAVLKGPNPpLTIEEIPVPR-PKEGEILIRVAACGVCHSDLHVLKGELP-FPPPFVLGHEISGEVVEVGPNVENpygL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  77 QKGDRVVIPFVIACGDCFFCRLQQYAACEN---TNAGKGAALNkkqipAPAALFG--YSHLYGGVPGGQAEYVRVPKGNV 151
Cdd:cd08263  79 SVGDRVVGSFIMPCGKCRYCARGKENLCEDffaYNRLKGTLYD-----GTTRLFRldGGPVYMYSMGGLAEYAVVPATAL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 152 gpFKVPPLLSDDKALFLSDILPTAWQAAKNAQIQQ-GSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdR 230
Cdd:cd08263 154 --APLPESLDYTESAVLGCAGFTAYGALKHAADVRpGETVAVIGVGGVGSSAIQLAKAFGASPIIAVDVRDEKLAKAK-E 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 231 YGAIPINFDEDSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsTTETVLTNLKLEGSSGKALRQCIAA------------V 298
Cdd:cd08263 231 LGATHTVNAAKEDAVAAIREITGG-RGVDVVVEALG------KPETFKLALDVVRDGGRAVVVGLAPggataeipitrlV 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 299 RRGgiVSVPGVYAgfihgflfgdafdkglsfkmGQTHVHawLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKRE 378
Cdd:cd08263 304 RRG--IKIIGSYG--------------------ARPRQD--LPELVGLAASGKLDPEALVTHKYKLEEINEAYENLRKGL 359

                ....*...
gi 16128591 379 EECRKVIL 386
Cdd:cd08263 360 IHGRAIVE 367
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
1-388 7.04e-44

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 155.75  E-value: 7.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    1 MKALTYHGPHH----VQVEnVPDPGVeqaDDIILRITATAICGSDLHLY--------RGKIPQVkhgdiFGHEFMGEVVE 68
Cdd:PRK05396   1 MKALVKLKAEPglwlTDVP-VPEPGP---NDVLIKVKKTAICGTDVHIYnwdewaqkTIPVPMV-----VGHEFVGEVVE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   69 TGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACENTnagKGAALNkkqipapaalfgyshlyggVPGGQAEYVRVPK 148
Cdd:PRK05396  72 VGSEVTGFKVGDRVSGEGHIVCGHCRNCRAGRRHLCRNT---KGVGVN-------------------RPGAFAEYLVIPA 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  149 GNVgpFKVPPLLSDDKALFLsDILPTAWQAAKNAQIQqGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAA 228
Cdd:PRK05396 130 FNV--WKIPDDIPDDLAAIF-DPFGNAVHTALSFDLV-GEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELAR 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  229 dRYGA-IPINFDEDsDPAQSIIEQTAGHrGVDavidaVGFEAKGsttetvltnlklegsSGKALRQCIAAVRRGGIVSVP 307
Cdd:PRK05396 206 -KMGAtRAVNVAKE-DLRDVMAELGMTE-GFD-----VGLEMSG---------------APSAFRQMLDNMNHGGRIAML 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  308 GVYAGFIhGFLFGDAFDKGLSFK------MGQThvhaWLgELLPLIEKGL-LKPeeIVTHYMPFEEAARGYEIFekREEE 380
Cdd:PRK05396 263 GIPPGDM-AIDWNKVIFKGLTIKgiygreMFET----WY-KMSALLQSGLdLSP--IITHRFPIDDFQKGFEAM--RSGQ 332

                 ....*...
gi 16128591  381 CRKVILVP 388
Cdd:PRK05396 333 SGKVILDW 340
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
1-311 3.00e-42

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: 150.54  E-value: 3.00e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKAL--TYHGPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQK 78
Cdd:cd08258   1 MKALvkTGPGPGNVELREVPEPEP-GPGEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEVGPDVEGWKV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  79 GDRVVI-PFVIACGDCFFCRLQQYAACEntnagkgaalNKKqipapaaLFGYshlygGVPGGQAEYVRVPKGNVgpFKVP 157
Cdd:cd08258  80 GDRVVSeTTFSTCGRCPYCRRGDYNLCP----------HRK-------GIGT-----QADGGFAEYVLVPEESL--HELP 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 158 PLLSDDKALfLSDILPTAWQA-AKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFV-VDHHPYRLHfAADRYGAIP 235
Cdd:cd08258 136 ENLSLEAAA-LTEPLAVAVHAvAERSGIRPGDTVVVFGPGPIGLLAAQVAKLQGATVVVVgTEKDEVRLD-VAKELGADA 213
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128591 236 INFDEDsDPAQSIIEQTAGHrGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVPGVYA 311
Cdd:cd08258 214 VNGGEE-DLAELVNEITDGD-GADVVIECSG--------------------AVPALEQALELLRKGGRIVQVGIFG 267
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
1-388 1.18e-39

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: 144.70  E-value: 1.18e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPH--HVQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPQVKHGDI-FGHEFMGEVVETGKDVKNLQ 77
Cdd:cd08254   1 MKAWRFHKGSkgLLVLEEVPVPEPG-PGEVLVKVKAAGVCHSDLHILDGGVPTLTKLPLtLGHEIAGTVVEVGAGVTNFK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  78 KGDRVVIPFVIACGDCFFCRLQQYAACENTnagkgaalnkkqipapaalfgySHLYGGVPGGQAEYVRVPKGNVGPfkVP 157
Cdd:cd08254  80 VGDRVAVPAVIPCGACALCRRGRGNLCLNQ----------------------GMPGLGIDGGFAEYIVVPARALVP--VP 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 158 PLLSDDKALFLSDILPTAWQAAKNA-QIQQGSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAAdRYGAIPi 236
Cdd:cd08254 136 DGVPFAQAAVATDAVLTPYHAVVRAgEVKPGETVLVIGLGGLGLNAVQIAKAMGAA-VIAVDIKEEKLELAK-ELGADE- 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 237 nFDEDSDPAQSIIEQTAGHRGVDAVIDAVGFeakGSTTEtvltnlklegssgkalrQCIAAVRRGGIVSVPGVYAG--FI 314
Cdd:cd08254 213 -VLNSLDDSPKDKKAAGLGGGFDVIFDFVGT---QPTFE-----------------DAQKAVKPGGRIVVVGLGRDklTV 271
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128591 315 HGFLFGdAFDKGLSFKMGQTHVHawLGELLPLIEKGLLKPeeiVTHYMPFEEAARGYEIFEKREEECRkVILVP 388
Cdd:cd08254 272 DLSDLI-ARELRIIGSFGGTPED--LPEVLDLIAKGKLDP---QVETRPLDEIPEVLERLHKGKVKGR-VVLVP 338
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
1-385 7.16e-39

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group 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: 142.46  E-value: 7.16e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHH-VQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKG 79
Cdd:cd08259   1 MKAAILHKPNKpLQIEEVPDP-EPGPGEVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVGEGVERFKPG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  80 DRVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkkqipapAALFGYShlyggVPGGQAEYVRVPKGNVgpFKVPPL 159
Cdd:cd08259  80 DRVILYYYIPCGKCEYCLSGEENLCRN-----------------RAEYGEE-----VDGGFAEYVKVPERSL--VKLPDN 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 160 LSDDKALFLSDILPTAWQAAKNAQIQQGSSVAV-YGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGAIPINF 238
Cdd:cd08259 136 VSDESAALAACVVGTAVHALKRAGVKKGDTVLVtGAGGGVGIHAIQLAKALGAR-VIAVTRSPEKLKILKELGADYVIDG 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 239 DEDSDPAQSIIeqtaghrGVDAVIDAVgfeakGSTTetvltnlkLEGSsgkaLRqciaAVRRGGIVSVPGVYAGFIHGFL 318
Cdd:cd08259 215 SKFSEDVKKLG-------GADVVIELV-----GSPT--------IEES----LR----SLNKGGRLVLIGNVTPDPAPLR 266
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 319 FGDAFDKGLSFkmgQTHVHAWLGEL---LPLIEKGLLKPeeIVTHYMPFEEAARGYEIFEKREEECRKVI 385
Cdd:cd08259 267 PGLLILKEIRI---IGSISATKADVeeaLKLVKEGKIKP--VIDRVVSLEDINEALEDLKSGKVVGRIVL 331
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
26-151 1.74e-38

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: 134.27  E-value: 1.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    26 DDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACE 105
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYNLCP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 16128591   106 NtnagkgaalnkkqipapAALFGYshlygGVPGGQAEYVRVPKGNV 151
Cdd:pfam08240  81 N-----------------GRFLGY-----DRDGGFAEYVVVPERNL 104
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
1-388 4.09e-38

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: 140.39  E-value: 4.09e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHH-VQVENVPDPGVEQaDDIILRITATAICGSDLHLYRGkiPQVKHGD-----IFGHEFMGEVVETGKDVK 74
Cdd:cd05284   1 MKAARLYEYGKpLRLEDVPVPEPGP-GQVLVRVGGAGVCHSDLHVIDG--VWGGILPyklpfTLGHENAGWVEEVGSGVD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  75 NLQKGDRVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkkqiPAPAALfgyshlygGVPGGQAEYVRVPKGNVgpF 154
Cdd:cd05284  78 GLKEGDPVVVHPPWGCGTCRYCRRGEENYCEN--------------ARFPGI--------GTDGGFAEYLLVPSRRL--V 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 155 KVPPLLSDDKALFLSDILPTAWQAAKNA--QIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYG 232
Cdd:cd05284 134 KLPRGLDPVEAAPLADAGLTAYHAVKKAlpYLDPGSTVVVIGVGGLGHIAVQILRALTPATVIAVDRSEEALKLAE-RLG 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 233 AiPINFDEDSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVPGvYAG 312
Cdd:cd05284 213 A-DHVLNASDDVVEEVRELTGG-RGADAVIDFVG--------------------SDETLALAAKLLAKGGRYVIVG-YGG 269
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128591 313 FIHgFLFGDAFDKGLSFKMGQTHVHAWLGELLPLIEKGLLKPEeiVTHYmPFEEAARGYEIFEKREEECRKVIlVP 388
Cdd:cd05284 270 HGR-LPTSDLVPTEISVIGSLWGTRAELVEVVALAESGKVKVE--ITKF-PLEDANEALDRLREGRVTGRAVL-VP 340
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
7-373 9.51e-38

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: 139.29  E-value: 9.51e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   7 HGPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYR-GKI--PQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVV 83
Cdd:cd08232   4 HAAGDLRVEERPAPEP-GPGEVRVRVAAGGICGSDLHYYQhGGFgtVRLREPMVLGHEVSGVVEAVGPGVTGLAPGQRVA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  84 IPFVIACGDCFFCRLQQYAACENTNagkgaalnkkqipapaaLFGYSHLYGGVPGGQAEYVRVPKGNVgpFKVPPLLSDD 163
Cdd:cd08232  83 VNPSRPCGTCDYCRAGRPNLCLNMR-----------------FLGSAMRFPHVQGGFREYLVVDASQC--VPLPDGLSLR 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 164 KALFlSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGAipinfDEDSD 243
Cdd:cd08232 144 RAAL-AEPLAVALHAVNRAGDLAGKRVLVTGAGPIGALVVAAARRAGAAEIVATDLADAPLAVAR-AMGA-----DETVN 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 244 PAQSIIEQTAGHRG-VDavidaVGFEAKGSTtetvltnlklegssgKALRQCIAAVRRGGIVSVPGVYAGFIhGFLFGDA 322
Cdd:cd08232 217 LARDPLAAYAADKGdFD-----VVFEASGAP---------------AALASALRVVRPGGTVVQVGMLGGPV-PLPLNAL 275
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 16128591 323 FDKGLSFKmGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEI 373
Cdd:cd08232 276 VAKELDLR-GSFRFDDEFAEAVRLLAAGRIDVRPLITAVFPLEEAAEAFAL 325
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
1-379 9.95e-35

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: 131.50  E-value: 9.95e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYH--GPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIP-QVKHGDIFGHEFMGEVVETGKDVKNLQ 77
Cdd:cd08297   1 MKAAVVEefGEKPYEVKDVPVP-EPGPGEVLVKLEASGVCHTDLHAALGDWPvKPKLPLIGGHEGAGVVVAVGPGVSGLK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  78 KGDRVVIPFVI-ACGDCFFCRLQQYAACENtnagkgaalnkkqipapAALFGYShlyggVPGGQAEYVRVPKGNVGPfkV 156
Cdd:cd08297  80 VGDRVGVKWLYdACGKCEYCRTGDETLCPN-----------------QKNSGYT-----VDGTFAEYAIADARYVTP--I 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 157 PPLLSDDKA--LFLSDIlpTAWQAAKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAeQIFVVDHHPYRLHFA----AD 229
Cdd:cd08297 136 PDGLSFEQAapLLCAGV--TVYKALKKAGLKPGDWVVISGAgGGLGHLGVQYAKAMGL-RVIAIDVGDEKLELAkelgAD 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 230 RYgaipINFDEdSDPAQSIIEQTAGhRGVDAVIdavgfeakgsttetVLTnlklegSSGKALRQCIAAVRRGGIVSVPGV 309
Cdd:cd08297 213 AF----VDFKK-SDDVEAVKELTGG-GGAHAVV--------------VTA------VSAAAYEQALDYLRPGGTLVCVGL 266
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128591 310 YAGfihGFLFGDAFD---KGLSFKMGQTHVHAWLGELLPLIEKGLLKPeeIVTHYmPFEEAArgyEIFEKREE 379
Cdd:cd08297 267 PPG---GFIPLDPFDlvlRGITIVGSLVGTRQDLQEALEFAARGKVKP--HIQVV-PLEDLN---EVFEKMEE 330
PRK10083 PRK10083
putative oxidoreductase; Provisional
1-386 3.03e-33

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 127.16  E-value: 3.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    1 MKALTYHGPHHVQVENVPDPGvEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:PRK10083   1 MKSIVIEKPNSLAIEERPIPQ-PAAGEVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGEGVDAARIGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   81 RVVIPFVIACGDCFFCRLQQYAACEntnagkgaalnkkqipapaalfgySHLYGGV--PGGQAEYVRVPKGNVgpFKVPP 158
Cdd:PRK10083  80 RVAVDPVISCGHCYPCSIGKPNVCT------------------------SLVVLGVhrDGGFSEYAVVPAKNA--HRIPD 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  159 LLSDDKALFLsDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTI-ACARLLGAEQIFVVDHHPYRLHFAAdRYGAipin 237
Cdd:PRK10083 134 AIADQYAVMV-EPFTIAANVTGRTGPTEQDVALIYGAGPVGLTIVqVLKGVYNVKAVIVADRIDERLALAK-ESGA---- 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  238 fDEDSDPAQSIIEQTAGHRGVDA--VIDAVGFEAkgsttetvltnlKLEgssgKALRQCIAAVRRG--GIVSVPG--VYA 311
Cdd:PRK10083 208 -DWVINNAQEPLGEALEEKGIKPtlIIDAACHPS------------ILE----EAVTLASPAARIVlmGFSSEPSeiVQQ 270
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128591  312 GFIHGFLfgDAFDKGLSFKMGQThVHAWLgellpliEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEECRKVIL 386
Cdd:PRK10083 271 GITGKEL--SIFSSRLNANKFPV-VIDWL-------SKGLIDPEKLITHTFDFQHVADAIELFEKDQRHCCKVLL 335
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
1-389 4.04e-33

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: 126.42  E-value: 4.04e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYH---GPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIP-QVKHGDIFGHEFMGEVVETGKDVKNL 76
Cdd:COG0604   1 MKAIVITefgGPEVLELEEVPVP-EPGPGEVLVRVKAAGVNPADLLIRRGLYPlPPGLPFIPGSDAAGVVVAVGEGVTGF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  77 QKGDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalfgyshlYGGVPGGQAEYVRVPKGNVGPfkV 156
Cdd:COG0604  80 KVGDRVA-------------------------------------------------GLGRGGGYAEYVVVPADQLVP--L 108
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 157 PPLLSDDKA--LFLSdiLPTAWQA-AKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVV---DHHPYRLHFAAD 229
Cdd:COG0604 109 PDGLSFEEAaaLPLA--GLTAWQAlFDRGRLKPGETVLVHGAaGGVGSAAVQLAKALGARVIATAsspEKAELLRALGAD 186
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 230 RygaiPINFDEDsDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRRGGIVSVPGV 309
Cdd:COG0604 187 H----VIDYREE-DFAERVRALTGG-RGVDVVLDTVG---------------------GDTLARSLRALAPGGRLVSIGA 239
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 310 YAGFIHGFLFGDAFDKGLS------FKMGQTHVHAWLGELLPLIEKGLLKPeeIVTHYMPFEEAARGYEIFEKREEecR- 382
Cdd:COG0604 240 ASGAPPPLDLAPLLLKGLTltgftlFARDPAERRAALAELARLLAAGKLRP--VIDRVFPLEEAAEAHRLLESGKH--Rg 315

                ....*..
gi 16128591 383 KVILVPG 389
Cdd:COG0604 316 KVVLTVD 322
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
1-378 1.67e-32

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: 125.45  E-value: 1.67e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYH---GPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYRGkIPQVKH--GDIFGHEFMGEVVETGKDVKN 75
Cdd:cd08266   1 MKAVVIRghgGPEVLEYGDLPEPEP-GPDEVLVRVKAAALNHLDLWVRRG-MPGIKLplPHILGSDGAGVVEAVGPGVTN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  76 LQKGDRVVIPFVIACGDCFFCRlqqyaacentnAGKGAALNKKQIpapaalFGYshlygGVPGGQAEYVRVPKGNVgpFK 155
Cdd:cd08266  79 VKPGQRVVIYPGISCGRCEYCL-----------AGRENLCAQYGI------LGE-----HVDGGYAEYVAVPARNL--LP 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 156 VPPLLSDDKALFLSDILPTAWQA-AKNAQIQQGSSVAVYGAGP-VGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGA 233
Cdd:cd08266 135 IPDNLSFEEAAAAPLTFLTAWHMlVTRARLRPGETVLVHGAGSgVGSAAIQIAKLFGAT-VIATAGSEDKLERAKELGAD 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 234 IPINFDEDSDPAqSIIEQTAGhRGVDAVIDAVGfeakGSTTETVLTNLKlegssgkalrqciaavRRGGIVSVpGVYAGF 313
Cdd:cd08266 214 YVIDYRKEDFVR-EVRELTGK-RGVDVVVEHVG----AATWEKSLKSLA----------------RGGRLVTC-GATTGY 270
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128591 314 IHGFLFGDAFDKGLSFkMGQTH-VHAWLGELLPLIEKGLLKPeeIVTHYMPFEEAARGYEIFEKRE 378
Cdd:cd08266 271 EAPIDLRHVFWRQLSI-LGSTMgTKAELDEALRLVFRGKLKP--VIDSVFPLEEAAEAHRRLESRE 333
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
24-386 7.61e-30

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: 118.60  E-value: 7.61e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  24 QADDIILRITATAICGSDLHLYRGKiPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAA 103
Cdd:cd08277  26 KANEVRIKMLATSVCHTDILAIEGF-KATLFPVILGHEGAGIVESVGEGVTNLKPGDKVIPLFIGQCGECSNCRSGKTNL 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 104 CENTNAGKGAALNKKQipAPAALFGYS-HLYGGVpGGQAEYVRVPKGNVGpfKVPPLLSDDKALFLSDILPTAWQAA-KN 181
Cdd:cd08277 105 CQKYRANESGLMPDGT--SRFTCKGKKiYHFLGT-STFSQYTVVDENYVA--KIDPAAPLEHVCLLGCGFSTGYGAAwNT 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 182 AQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHfAADRYGAIPINFDEDSD--PAQSIIEQTAGhrGVD 259
Cdd:cd08277 180 AKVEPGSTVAVFGLGAVGLSAIMGAKIAGASRIIGVDINEDKFE-KAKEFGATDFINPKDSDkpVSEVIREMTGG--GVD 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 260 AVIDAVGfeakgsttetvltNLKLegssgkaLRQCIAAVRRGG----IVSVPGVYAGFIHGFLFGDAFD-KGlsFKMGQT 334
Cdd:cd08277 257 YSFECTG-------------NADL-------MNEALESTKLGWgvsvVVGVPPGAELSIRPFQLILGRTwKG--SFFGGF 314
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 16128591 335 HVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFekREEECRKVIL 386
Cdd:cd08277 315 KSRSDVPKLVSKYMNKKFDLDELITHVLPFEEINKGFDLM--KSGECIRTVI 364
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
57-386 2.36e-29

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: 115.06  E-value: 2.36e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  57 IFGHEFMGEVVETGKDVKNLQKGDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalfgyshlyggV 136
Cdd:cd08255  23 PPGYSSVGRVVEVGSGVTGFKPGDRVF----------------------------------------------------C 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 137 PGGQAEYVRVPKGNVgpFKVPPLLSDDKALFLsDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFV 216
Cdd:cd08255  51 FGPHAERVVVPANLL--VPLPDGLPPERAALT-ALAATALNGVRDAEPRLGERVAVVGLGLVGLLAAQLAKAAGAREVVG 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 217 VDHHPYRLHFAAdRYGAIpinfdedsDPAQSIIEQTAGHRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIA 296
Cdd:cd08255 128 VDPDAARRELAE-ALGPA--------DPVAADTADEIGGRGADVVIEASG--------------------SPSALETALR 178
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 297 AVRRGGIVSVPGVYAGFihGFLFGDAFD-KGLSFKMGQT-----------HVHAW-LGELLPLIEKGllKPEEIVTHYMP 363
Cdd:cd08255 179 LLRDRGRVVLVGWYGLK--PLLLGEEFHfKRLPIRSSQVygigrydrprrWTEARnLEEALDLLAEG--RLEALITHRVP 254
                       330       340
                ....*....|....*....|...
gi 16128591 364 FEEAARGYEIFEKREEECRKVIL 386
Cdd:cd08255 255 FEDAPEAYRLLFEDPPECLKVVL 277
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
1-385 4.98e-29

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


Pssm-ID: 176223 [Multi-domain]  Cd Length: 341  Bit Score: 115.87  E-value: 4.98e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGpHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYR-----------GKIPQVKHGDIFGHEFMGEVVET 69
Cdd:cd08262   1 MRAAVFRD-GPLVVRDVPDP-EPGPGQVLVKVLACGICGSDLHATAhpeamvddaggPSLMDLGADIVLGHEFCGEVVDY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  70 GKDVKN-LQKGDRVV-IPFVIaCGDCFFCRLqqyaacentnagkgaalnkkqipapaalfGYShlyGGVPGGQAEYVRVP 147
Cdd:cd08262  79 GPGTERkLKVGTRVTsLPLLL-CGQGASCGI-----------------------------GLS---PEAPGGYAEYMLLS 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 148 KGNVgpFKVPPLLSDDKALfLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFA 227
Cdd:cd08262 126 EALL--LRVPDGLSMEDAA-LTEPLAVGLHAVRRARLTPGEVALVIGCGPIGLAVIAALKARGVGPIVASDFSPERRALA 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 228 AdRYGA-IPINFDEDSDPAQSIIEQTAGHRGVDAVIdavgFEAKGSTTetvltnlklegssgkALRQCIAAVRRGGIVSV 306
Cdd:cd08262 203 L-AMGAdIVVDPAADSPFAAWAAELARAGGPKPAVI----FECVGAPG---------------LIQQIIEGAPPGGRIVV 262
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128591 307 PGVYAGFIHgFLFGDAFDKGLSFKMGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEECRKVI 385
Cdd:cd08262 263 VGVCMESDN-IEPALAIRKELTLQFSLGYTPEEFADALDALAEGKVDVAPMVTGTVGLDGVPDAFEALRDPEHHCKILV 340
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
1-367 2.27e-28

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


Pssm-ID: 176258 [Multi-domain]  Cd Length: 329  Bit Score: 113.82  E-value: 2.27e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHV-----QVENVPDPGVEQaDDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKN 75
Cdd:cd08298   1 MKAMVLEKPGPIeenplRLTEVPVPEPGP-GEVLIKVEACGVCRTDLHIVEGDLPPPKLPLIPGHEIVGRVEAVGPGVTR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  76 LQKGDRV-VIPFVIACGDCFFCRLQQYAACentnagkgaalnkkqipaPAALF-GYShlyggVPGGQAEYVRVPKGNVgp 153
Cdd:cd08298  80 FSVGDRVgVPWLGSTCGECRYCRSGRENLC------------------DNARFtGYT-----VDGGYAEYMVADERFA-- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 154 FKVPPLLSDDKA--LFLSDIlpTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFA---- 227
Cdd:cd08298 135 YPIPEDYDDEEAapLLCAGI--IGYRALKLAGLKPGQRLGLYGFGASAHLALQIARYQGAE-VFAFTRSGEHQELArelg 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 228 ADRYGaipinfDEDSDPAQSIieqtaghrgvDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVP 307
Cdd:cd08298 212 ADWAG------DSDDLPPEPL----------DAAIIFAP--------------------VGALVPAALRAVKKGGRVVLA 255
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128591 308 GVYAGFIHGFLFGDAFdkglsfkMGQTHVHAWLG------ELLPLIEKGLLKPEeiVTHYmPFEEA 367
Cdd:cd08298 256 GIHMSDIPAFDYELLW-------GEKTIRSVANLtrqdgeEFLKLAAEIPIKPE--VETY-PLEEA 311
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
8-387 3.50e-28

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: 112.84  E-value: 3.50e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   8 GPHHVQVENVPDPGVEQADdIILRITATAICGSDLH-LYRGKIPQVKHGD--IFGHEFMGEVVETGKDVKNLQKGDRVVi 84
Cdd:cd08269   3 GPGRFEVEEHPRPTPGPGQ-VLVRVEGCGVCGSDLPaFNQGRPWFVYPAEpgGPGHEGWGRVVALGPGVRGLAVGDRVA- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  85 pfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalfgyshlyGGVPGGQAEYVRVPKGNVgpFKVPPLLsDDK 164
Cdd:cd08269  81 -------------------------------------------------GLSGGAFAEYDLADADHA--VPLPSLL-DGQ 108
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 165 AlFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGAIPINfdedSDP 244
Cdd:cd08269 109 A-FPGEPLGCALNVFRRGWIRAGKTVAVIGAGFIGLLFLQLAAAAGARRVIAIDRRPARLALAR-ELGATEVV----TDD 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 245 AQSIIEQTA---GHRGVDAVIDAVGFEAkgsttetvltnlklegssgkALRQCIAAVRRGGIVSVPGVYAGFIHGFLFGD 321
Cdd:cd08269 183 SEAIVERVReltGGAGADVVIEAVGHQW--------------------PLDLAGELVAERGRLVIFGYHQDGPRPVPFQT 242
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 322 AFDKGLSFKMGQTHVHAWLGELLP----LIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEECRKVILV 387
Cdd:cd08269 243 WNWKGIDLINAVERDPRIGLEGMReavkLIADGRLDLGSLLTHEFPLEELGDAFEAARRRPDGFIKGVIV 312
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
12-377 2.86e-27

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: 111.84  E-value: 2.86e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  12 VQVENVPDPgVEQADDIILRITATAICGSDLHLYR----GKI--PQV-KHGDIFGHEFMGEVVETGKDVKNLQKGDRVVI 84
Cdd:cd08265  39 LRVEDVPVP-NLKPDEILIRVKACGICGSDIHLYEtdkdGYIlyPGLtEFPVVIGHEFSGVVEKTGKNVKNFEKGDPVTA 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  85 PFVIACGDCFFCRLQQYAACENTNagkgaalnkkqipapaaLFGYSHlyggvPGGQAEYVRVPKGNVgpFKVPPLL---S 161
Cdd:cd08265 118 EEMMWCGMCRACRSGSPNHCKNLK-----------------ELGFSA-----DGAFAEYIAVNARYA--WEINELReiyS 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 162 DDKAlFLSDILPTAWQAAKNAQ------IQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIP 235
Cdd:cd08265 174 EDKA-FEAGALVEPTSVAYNGLfirgggFRPGAYVVVYGAGPIGLAAIALAKAAGASKVIAFEISEERRNLAKEMGADYV 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 236 INFDEDSD--PAQSIIEQTAGhRGVDAVIDAVGFEAKG--STTETVLTNLKlegssgkalrqcIAAVRRgGIVSVPgvya 311
Cdd:cd08265 253 FNPTKMRDclSGEKVMEVTKG-WGADIQVEAAGAPPATipQMEKSIAINGK------------IVYIGR-AATTVP---- 314
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128591 312 gfihgfLFGDAFDKGLSFKMG-QTHV-HAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKR 377
Cdd:cd08265 315 ------LHLEVLQVRRAQIVGaQGHSgHGIFPSVIKLMASGKIDMTKIITARFPLEGIMEAIKAASER 376
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
1-377 6.04e-27

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: 109.19  E-value: 6.04e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYH---GPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYRGKIPQVKHGD---IFGHEFMGEVVETGKDVK 74
Cdd:cd05289   1 MKAVRIHeygGPEVLELADVPTPEP-GPGEVLVKVHAAGVNPVDLKIREGLLKAAFPLTlplIPGHDVAGVVVAVGPGVT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  75 NLQKGDRVvipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalFGYSHLYGGvpGGQAEYVRVPKGNVgpF 154
Cdd:cd05289  80 GFKVGDEV--------------------------------------------FGMTPFTRG--GAYAEYVVVPADEL--A 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 155 KVPPLLSDDKA--LFLSDIlpTAWQA-AKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVV--DHHPYRLHFAA 228
Cdd:cd05289 112 LKPANLSFEEAaaLPLAGL--TAWQAlFELGGLKAGQTVLIHGAaGGVGSFAVQLAKARGARVIATAsaANADFLRSLGA 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 229 DrygaIPINFDEDSdpaqsiIEQTAGHRGVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRRGG-IVSVP 307
Cdd:cd05289 190 D----EVIDYTKGD------FERAAAPGGVDAVLDTVG---------------------GETLARSLALVKPGGrLVSIA 238
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 308 GVYAGFihgFLFGDAFDKGLSFKMGQTHVHawLGELLPLIEKGLLKPeeIVTHYMPFEEAARGYEIFEKR 377
Cdd:cd05289 239 GPPPAE---QAAKRRGVRAGFVFVEPDGEQ--LAELAELVEAGKLRP--VVDRVFPLEDAAEAHERLESG 301
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
24-366 1.01e-26

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: 109.90  E-value: 1.01e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  24 QADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFViACGDCFFCRLQQYAA 103
Cdd:cd08278  26 RPDEVLVRIVATGICHTDLVVRDGGLP-TPLPAVLGHEGAGVVEAVGSAVTGLKPGDHVVLSFA-SCGECANCLSGHPAY 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 104 CENTNAGKGAALNKkqiPAPAALfgysHLYGGVPG-----GQ---AEYVRVPKGNVgpFKVPPLLsdDKALF--LSDILP 173
Cdd:cd08278 104 CENFFPLNFSGRRP---DGSTPL----SLDDGTPVhghffGQssfATYAVVHERNV--VKVDKDV--PLELLapLGCGIQ 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 174 TAWQAAKNA-QIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADrYGA-IPINfDEDSDPAQSIIEQ 251
Cdd:cd08278 173 TGAGAVLNVlKPRPGSSIAVFGAGAVGLAAVMAAKIAGCTTIIAVDIVDSRLELAKE-LGAtHVIN-PKEEDLVAAIREI 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 252 TAGhrGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGG---IVSVPGVYAGFihGFLFGDAFDKGLS 328
Cdd:cd08278 251 TGG--GVDYALDTTG--------------------VPAVIEQAVDALAPRGtlaLVGAPPPGAEV--TLDVNDLLVSGKT 306
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 16128591 329 FK---MGQTHVHAWLGELLPLIEKGLLKPEEIVTHYmPFEE 366
Cdd:cd08278 307 IRgviEGDSVPQEFIPRLIELYRQGKFPFDKLVTFY-PFED 346
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
1-312 1.99e-26

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: 108.86  E-value: 1.99e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKA---LTYHGPHHVQVENVPDPgveQADDIILRITATAICGSDLHLYRGKI------------PQVKHGDIFGHEFMGE 65
Cdd:cd08240   1 MKAaavVEPGKPLEEVEIDTPKP---PGTEVLVKVTACGVCHSDLHIWDGGYdlgggktmslddRGVKLPLVLGHEIVGE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  66 VVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACEntnagKGAALNkkqipapaalfgyshlyGGVPGGQAEYVR 145
Cdd:cd08240  78 VVAVGPDAADVKVGDKVLVYPWIGCGECPVCLAGDENLCA-----KGRALG-----------------IFQDGGYAEYVI 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 146 VPKGNVgpFKVPPLLSDDKALFL--SDIlpTAWQAAKNAQIQQGS-SVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPY 222
Cdd:cd08240 136 VPHSRY--LVDPGGLDPALAATLacSGL--TAYSAVKKLMPLVADePVVIIGAGGLGLMALALLKALGPANIIVVDIDEA 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 223 RLHfAADRYGAIPINFDEDSDPAQSIIEQTAGhrGVDAVIDAVGFEAkgsttetvltnlklegSSGKALRqciaAVRRGG 302
Cdd:cd08240 212 KLE-AAKAAGADVVVNGSDPDAAKRIIKAAGG--GVDAVIDFVNNSA----------------TASLAFD----ILAKGG 268
                       330
                ....*....|
gi 16128591 303 IVSVPGVYAG 312
Cdd:cd08240 269 KLVLVGLFGG 278
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
1-293 3.66e-26

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 108.00  E-value: 3.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDlhlyrgkIPQV-KHGDIF-----GHEFMGEVVETGKDVK 74
Cdd:PRK10309   1 MKSVVNDTDGIVRVAESPIPEIKHQDDVLVKVASSGLCGSD-------IPRIfKNGAHYypitlGHEFSGYVEAVGSGVD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   75 NLQKGDRVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkkqipapaalfgYSHLYGGVPGGQAEYVRVPKGNVgpF 154
Cdd:PRK10309  74 DLHPGDAVACVPLLPCFTCPECLRGFYSLCAK----------------------YDFIGSRRDGGNAEYIVVKRKNL--F 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  155 KVPPLLSDDKALFLSDIlPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADrYGAI 234
Cdd:PRK10309 130 ALPTDMPIEDGAFIEPI-TVGLHAFHLAQGCEGKNVIIIGAGTIGLLAIQCAVALGAKSVTAIDINSEKLALAKS-LGAM 207
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128591  235 PI-NFDEDSDPA-----------QSIIEQTAGHRGVDAVIDAVGFEAKGSTTETVLTNLKLEGSS-GKALRQ 293
Cdd:PRK10309 208 QTfNSREMSAPQiqsvlrelrfdQLILETAGVPQTVELAIEIAGPRAQLALVGTLHHDLHLTSATfGKILRK 279
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
24-372 3.82e-26

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: 108.30  E-value: 3.82e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  24 QADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAA 103
Cdd:cd05279  24 KAGEVRIKVVATGVCHTDLHVIDGKLP-TPLPVILGHEGAGIVESIGPGVTTLKPGDKVIPLFGPQCGKCKQCLNPRPNL 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 104 CENTNA--GKGA------ALNKKQIPApaalfgysHLYGGVpGGQAEYVRVPKGNVGpfKVPPLLSDDKALFLSDILPTA 175
Cdd:cd05279 103 CSKSRGtnGRGLmsdgtsRFTCKGKPI--------HHFLGT-STFAEYTVVSEISLA--KIDPDAPLEKVCLIGCGFSTG 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 176 WQAAKN-AQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGAIP-IN-FDEDSDPAQSIIEQT 252
Cdd:cd05279 172 YGAAVNtAKVTPGSTCAVFGLGGVGLSVIMGCKAAGASRIIAVDINKDKFEKAK-QLGATEcINpRDQDKPIVEVLTEMT 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 253 AGhrGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGG----IVSVP--GVYAGFIHGFLFGDAFDKG 326
Cdd:cd05279 251 DG--GVDYAFEVIG--------------------SADTLKQALDATRLGGgtsvVVGVPpsGTEATLDPNDLLTGRTIKG 308
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 16128591 327 LSFkmGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYE 372
Cdd:cd05279 309 TVF--GGWKSKDSVPKLVALYRQKKFPLDELITHVLPFEEINDGFD 352
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
9-308 4.65e-26

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: 108.23  E-value: 4.65e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   9 PHHVQVENVPDPGveqADDIILRITATAICGSDLHLYRG----KIPQVkhgdiFGHEFMGEVVETGKDVKNLQKGDRVVI 84
Cdd:cd08281  20 PLVIEEVELDPPG---PGEVLVKIAAAGLCHSDLSVINGdrprPLPMA-----LGHEAAGVVVEVGEGVTDLEVGDHVVL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  85 PFVIACGDCFFCRLQQYAACEntnagKGAALNKKqipapAALFG------------YSHLygGVpGGQAEYVRVPKGNVg 152
Cdd:cd08281  92 VFVPSCGHCRPCAEGRPALCE-----PGAAANGA-----GTLLSggrrlrlrggeiNHHL--GV-SAFAEYAVVSRRSV- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 153 pFKVPPLLSDDK-ALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADrY 231
Cdd:cd08281 158 -VKIDKDVPLEIaALFGCAVLTGVGAVVNTAGVRPGQSVAVVGLGGVGLSALLGAVAAGASQVVAVDLNEDKLALARE-L 235
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128591 232 GAIPINFDEDSDPAQSIIEQTAGhrGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVPG 308
Cdd:cd08281 236 GATATVNAGDPNAVEQVRELTGG--GVDYAFEMAG--------------------SVPALETAYEITRRGGTTVTAG 290
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
1-286 3.07e-25

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 105.12  E-value: 3.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    1 MKALTYHGPHH-VQVENV--PDPGVeqaDDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQ 77
Cdd:PRK13771   1 MKAVILPGFKQgYRIEEVpdPKPGK---DEVVIKVNYAGLCYRDLLQLQGFYPRMKYPVILGHEVVGTVEEVGENVKGFK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   78 KGDRVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkKQIpapaalfgyshlYG-GVPGGQAEYVRVPKGNVgpFKV 156
Cdd:PRK13771  78 PGDRVASLLYAPDGTCEYCRSGEEAYCKN-----------RLG------------YGeELDGFFAEYAKVKVTSL--VKV 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  157 PPLLSDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVVDHHPYR--LHFAADrYGA 233
Cdd:PRK13771 133 PPNVSDEGAVIVPCVTGMVYRGLRRAGVKKGETVLVTGAgGGVGIHAIQVAKALGAKVIAVTSSESKAkiVSKYAD-YVI 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16128591  234 IPINFDEDsdpAQSIieqtaghRGVDAVIDAVGfeakGSTTETVLTNLKLEGS 286
Cdd:PRK13771 212 VGSKFSEE---VKKI-------GGADIVIETVG----TPTLEESLRSLNMGGK 250
PLN02702 PLN02702
L-idonate 5-dehydrogenase
26-289 4.25e-25

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 105.24  E-value: 4.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   26 DDIILRITATAICGSDLHLYRG-KIPQ--VKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYA 102
Cdd:PLN02702  42 HDVRVRMKAVGICGSDVHYLKTmRCADfvVKEPMVIGHECAGIIEEVGSEVKHLVVGDRVALEPGISCWRCNLCKEGRYN 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  103 ACENTnagkgaalnkKQIPAPAalfgyshlyggVPGGQAEYVRVPkGNVGpFKVPPLLSDDKALfLSDILPTAWQAAKNA 182
Cdd:PLN02702 122 LCPEM----------KFFATPP-----------VHGSLANQVVHP-ADLC-FKLPENVSLEEGA-MCEPLSVGVHACRRA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  183 QIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADrYGAIPI----NFDEDSDPAQSIIEQTAGhRGV 258
Cdd:PLN02702 178 NIGPETNVLVMGAGPIGLVTMLAARAFGAPRIVIVDVDDERLSVAKQ-LGADEIvlvsTNIEDVESEVEEIQKAMG-GGI 255
                        250       260       270
                 ....*....|....*....|....*....|.
gi 16128591  259 DAVIDAVGFeakgstTETVLTNLKLEGSSGK 289
Cdd:PLN02702 256 DVSFDCVGF------NKTMSTALEATRAGGK 280
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
6-385 4.75e-25

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: 104.33  E-value: 4.75e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   6 YHGPHHVQVENVPDPGveqADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIP 85
Cdd:cd08245   8 AGGPLEPEEVPVPEPG---PGEVLIKIEACGVCHTDLHAAEGDWGGSKYPLVPGHEIVGEVVEVGAGVEGRKVGDRVGVG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  86 FVI-ACGDCFFCRLQQYAACENtnagkgaalnkkqipapAALFGYSHLyggvpGGQAEYVRVPKGNVGPFkvPPLLSDDK 164
Cdd:cd08245  85 WLVgSCGRCEYCRRGLENLCQK-----------------AVNTGYTTQ-----GGYAEYMVADAEYTVLL--PDGLPLAQ 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 165 A--LFLSDIlpTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGAIPINFDEDS 242
Cdd:cd08245 141 AapLLCAGI--TVYSALRDAGPRPGERVAVLGIGGLGHLAVQYARAMGFE-TVAITRSPDKRELARKLGADEVVDSGAEL 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 243 DpaqsiIEQTAGhrGVDAVIDAVgfeakgsttetvltnlklegSSGKALRQCIAAVRRGGIVSVPGVYAGFIHGFLFGDA 322
Cdd:cd08245 218 D-----EQAAAG--GADVILVTV--------------------VSGAAAEAALGGLRRGGRIVLVGLPESPPFSPDIFPL 270
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128591 323 FDKGLSFKMGQTHVHAWLGELLPLIEKGLLKPeeiVTHYMPFEEAARGYEIFEKREEECRKVI 385
Cdd:cd08245 271 IMKRQSIAGSTHGGRADLQEALDFAAEGKVKP---MIETFPLDQANEAYERMEKGDVRFRFVL 330
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
24-386 4.94e-24

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: 102.37  E-value: 4.94e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  24 QADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAA 103
Cdd:cd08301  26 QAMEVRIKILHTSLCHTDVYFWEAKGQTPLFPRILGHEAAGIVESVGEGVTDLKPGDHVLPVFTGECKECRHCKSEKSNM 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 104 CE--NTNAGKGAALNKKQIPAPAALFGYSHLYGGvpGGQAEYVRVPKGNVGpfKVPPLLSDDKALFLSDILPTAWQAA-K 180
Cdd:cd08301 106 CDllRINTDRGVMINDGKSRFSINGKPIYHFVGT--STFSEYTVVHVGCVA--KINPEAPLDKVCLLSCGVSTGLGAAwN 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 181 NAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHfAADRYGAIP-INFDEDSDPAQSII-EQTAGhrGV 258
Cdd:cd08301 182 VAKVKKGSTVAIFGLGAVGLAVAEGARIRGASRIIGVDLNPSKFE-QAKKFGVTEfVNPKDHDKPVQEVIaEMTGG--GV 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 259 DAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGG----IVSVPGVYAGF-IHGFLFgdafdkgLSfkmGQ 333
Cdd:cd08301 259 DYSFECTG--------------------NIDAMISAFECVHDGWgvtvLLGVPHKDAVFsTHPMNL-------LN---GR 308
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128591 334 THVHAWLGELLP------LIE---KGLLKPEEIVTHYMPFEEAARGYEIFekREEECRKVIL 386
Cdd:cd08301 309 TLKGTLFGGYKPktdlpnLVEkymKKELELEKFITHELPFSEINKAFDLL--LKGECLRCIL 368
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
7-227 5.18e-23

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 98.99  E-value: 5.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    7 HGPHHVQVEnvpDPGVE-QADDIILRITATAICGSDLHLYR-GKIP--QVKHGDIFGHEFMGEVVETgkDVKNLQKGDRV 82
Cdd:PRK09880  11 AGKKDVAVT---EQEIEwNNNGTLVQITRGGICGSDLHYYQeGKVGnfVIKAPMVLGHEVIGKIVHS--DSSGLKEGQTV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   83 VIPFVIACGDCFFCRLQQYAACENTNagkgaalnkkqipapaaLFGYSHLYGGVPGGQAEYVRVPKGNVGPFkvpPLLSD 162
Cdd:PRK09880  86 AINPSKPCGHCKYCLSHNENQCTTMR-----------------FFGSAMYFPHVDGGFTRYKVVDTAQCIPY---PEKAD 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128591  163 DKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFA 227
Cdd:PRK09880 146 EKVMAFAEPLAVAIHAAHQAGDLQGKRVFVSGVGPIGCLIVAAVKTLGAAEIVCADVSPRSLSLA 210
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-388 9.47e-23

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: 97.70  E-value: 9.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPqvKHGdIFGHEFMGEVVETGKdvKNLQkGD 80
Cdd:cd08242   1 MKALVLDGGLDLRVEDLPKPEPP-PGEALVRVLLAGICNTDLEIYKGYYP--FPG-VPGHEFVGIVEEGPE--AELV-GK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  81 RVVIPFVIACGDCFFCRLQQYAACENTNAgkgaalnkkqipapaalFGYShlygGVPGGQAEYVRVPKGNvgPFKVPPLL 160
Cdd:cd08242  74 RVVGEINIACGRCEYCRRGLYTHCPNRTV-----------------LGIV----DRDGAFAEYLTLPLEN--LHVVPDLV 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 161 SDDKALFlsdILPTAwqAAKNAQIQQ----GSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGAIPI 236
Cdd:cd08242 131 PDEQAVF---AEPLA--AALEILEQVpitpGDKVAVLGDGKLGLLIAQVLALTGPD-VVLVGRHSEKLALARRLGVETVL 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 237 NFDEDSDPaqsiieqtaghRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVR-RGGIV--SVPGVYAGF 313
Cdd:cd08242 205 PDEAESEG-----------GGFDVVVEATG--------------------SPSGLELALRLVRpRGTVVlkSTYAGPASF 253
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 314 -----------IHGFLFGDaFDKGlsfkmgqthvhawlgelLPLIEKGLLKPEEIVTHYMPFEEAargYEIFEK-REEEC 381
Cdd:cd08242 254 dltkavvneitLVGSRCGP-FAPA-----------------LRLLRKGLVDVDPLITAVYPLEEA---LEAFERaAEPGA 312

                ....*..
gi 16128591 382 RKVILVP 388
Cdd:cd08242 313 LKVLLRP 319
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
19-212 3.27e-22

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: 96.41  E-value: 3.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  19 DPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRV-VIPFVIACGDCFFCR 97
Cdd:cd05283  18 ERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDRVgVGCQVDSCGTCEQCK 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  98 --LQQYaaCENTnagkgaalnkkqipapaALFGYSHLYGGVP--GGQAEYVRVPKGNVgpFKVPPLLSDDKA--LFLSDI 171
Cdd:cd05283  98 sgEEQY--CPKG-----------------VVTYNGKYPDGTItqGGYADHIVVDERFV--FKIPEGLDSAAAapLLCAGI 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 16128591 172 lpTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAE 212
Cdd:cd05283 157 --TVYSPLKRNGVGPGKRVGVVGIGGLGHLAVKFAKALGAE 195
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
1-375 3.77e-22

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: 95.97  E-value: 3.77e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTY---HGPHHVQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPQVKHG-DIFGHEFMGEVVETGKDVKNL 76
Cdd:cd05276   1 MKAIVIkepGGPEVLELGEVPKPAPG-PGEVLIRVAAAGVNRADLLQRQGLYPPPPGAsDILGLEVAGVVVAVGPGVTGW 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  77 QKGDRVvipfviacgdcffcrlqqyaacentnagkgaalnkkqipapAALfgyshLYGGvpgGQAEYVRVPKGNVgpFKV 156
Cdd:cd05276  80 KVGDRV-----------------------------------------CAL-----LAGG---GYAEYVVVPAGQL--LPV 108
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 157 PPLLSDDKALFLSDILPTAWQAAKN-AQIQQGSSVAVY-GAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADrYGA- 233
Cdd:cd05276 109 PEGLSLVEAAALPEVFFTAWQNLFQlGGLKAGETVLIHgGASGVGTAAIQLAKALGAR-VIATAGSEEKLEACRA-LGAd 186
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 234 IPINFDEDsDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRRGG-IVSVpGVYAG 312
Cdd:cd05276 187 VAINYRTE-DFAEEVKEATGG-RGVDVILDMVG---------------------GDYLARNLRALAPDGrLVLI-GLLGG 242
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128591 313 FIHGFLFGDAFDKGLSFkMGQTH-----------VHAWLGELLPLIEKGLLKPeeIVTHYMPFEEAARGYEIFE 375
Cdd:cd05276 243 AKAELDLAPLLRKRLTL-TGSTLrsrsleekaalAAAFREHVWPLFASGRIRP--VIDKVFPLEEAAEAHRRME 313
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
24-366 3.97e-22

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: 96.91  E-value: 3.97e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  24 QADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAA 103
Cdd:cd08300  26 KAGEVRIKILATGVCHTDAYTLSGADPEGLFPVILGHEGAGIVESVGEGVTSVKPGDHVIPLYTPECGECKFCKSGKTNL 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 104 CENTNA--GKGAA--------LNKKQIpapaalfgySHLYGgvPGGQAEYVRVPKGNVGpfKVPPLLSDDKALFLSDILP 173
Cdd:cd08300 106 CQKIRAtqGKGLMpdgtsrfsCKGKPI---------YHFMG--TSTFSEYTVVAEISVA--KINPEAPLDKVCLLGCGVT 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 174 TAWQAAKN-AQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRlhFA-ADRYGAIP-INFDEDSDPAQS-II 249
Cdd:cd08300 173 TGYGAVLNtAKVEPGSTVAVFGLGAVGLAVIQGAKAAGASRIIGIDINPDK--FElAKKFGATDcVNPKDHDKPIQQvLV 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 250 EQTAGhrGVDAVIDAVGfeakgsttetvltNLKLegssgkaLRQCIAAVRRGGIVSV-PGVYAGF--IHGFLF------- 319
Cdd:cd08300 251 EMTDG--GVDYTFECIG-------------NVKV-------MRAALEACHKGWGTSViIGVAAAGqeISTRPFqlvtgrv 308
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 16128591 320 --GDAFDkglSFKmGQTHVHAWLGELLplieKGLLKPEEIVTHYMPFEE 366
Cdd:cd08300 309 wkGTAFG---GWK-SRSQVPKLVEDYM----KGKIKVDEFITHTMPLDE 349
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
1-378 1.80e-20

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: 91.41  E-value: 1.80e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKAL---TYHGPHHVQVENV-PDPGVEqaDDIILRITATAICGSDLHLYRGKIpQVKHGDIF--GHEFMGEVVETGKDVK 74
Cdd:cd08241   1 MKAVvckELGGPEDLVLEEVpPEPGAP--GEVRIRVEAAGVNFPDLLMIQGKY-QVKPPLPFvpGSEVAGVVEAVGEGVT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  75 NLQKGDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqipapAALFGyshlyggvpGGQAEYVRVPKGNVgpF 154
Cdd:cd08241  78 GFKVGDRVV----------------------------------------ALTGQ---------GGFAEEVVVPAAAV--F 106
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 155 KVPPLLSDDKALFLSDILPTAWQAAKN-AQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVVdHHPYRLHFAAdRYG 232
Cdd:cd08241 107 PLPDGLSFEEAAALPVTYGTAYHALVRrARLQPGETVLVLGAaGGVGLAAVQLAKALGARVIAAA-SSEEKLALAR-ALG 184
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 233 A-IPINFDEDsDPAQSIIEQTAGhRGVDAVIDAVGfeakGSTTEtvltnlklegssgKALRqCIAavRRGGIVSVpGVYA 311
Cdd:cd08241 185 AdHVIDYRDP-DLRERVKALTGG-RGVDVVYDPVG----GDVFE-------------ASLR-SLA--WGGRLLVI-GFAS 241
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 312 GFI---------------HGFLFGDafdkglsFKMGQTHVHAW-LGELLPLIEKGLLKPEeiVTHYMPFEEAARGYEIFE 375
Cdd:cd08241 242 GEIpqipanllllknisvVGVYWGA-------YARREPELLRAnLAELFDLLAEGKIRPH--VSAVFPLEQAAEALRALA 312

                ...
gi 16128591 376 KRE 378
Cdd:cd08241 313 DRK 315
PLN02740 PLN02740
Alcohol dehydrogenase-like
30-375 4.98e-19

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 87.93  E-value: 4.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   30 LRITATAICGSDLHLYRGKIP-QVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACEN-- 106
Cdd:PLN02740  40 IKILYTSICHTDLSAWKGENEaQRAYPRILGHEAAGIVESVGEGVEDLKAGDHVIPIFNGECGDCRYCKRDKTNLCETyr 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  107 --------TNAGkGAALNKKQIPAPAALFGYSHLYggvpggqAEYVRVPKGNVgpFKVPPLLSDDKALFLSDILPTAWQA 178
Cdd:PLN02740 120 vdpfksvmVNDG-KTRFSTKGDGQPIYHFLNTSTF-------TEYTVLDSACV--VKIDPNAPLKKMSLLSCGVSTGVGA 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  179 AKN-AQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRlhFAADRYGAIP--INFDEDSDPAQSII-EQTAG 254
Cdd:PLN02740 190 AWNtANVQAGSSVAIFGLGAVGLAVAEGARARGASKIIGVDINPEK--FEKGKEMGITdfINPKDSDKPVHERIrEMTGG 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  255 hrGVDavidaVGFEAKGSTtetvltnlklegssgKALRQCIAAVRRG-GIVSVPGVYAG---------------FIHGFL 318
Cdd:PLN02740 268 --GVD-----YSFECAGNV---------------EVLREAFLSTHDGwGLTVLLGIHPTpkmlplhpmelfdgrSITGSV 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16128591  319 FGDafdkglsFKmGQTHvhawLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFE 375
Cdd:PLN02740 326 FGD-------FK-GKSQ----LPNLAKQCMQGVVNLDGFITHELPFEKINEAFQLLE 370
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
4-376 2.94e-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: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 85.01  E-value: 2.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   4 LTYHGPH---HVQVENVPDPGveqADDIILRITATAICGSDLHLYRGKIPQVKHGDIF-GHEFMGEVVETGKDVKNLQKG 79
Cdd:cd08273   6 VTRRGGPevlKVVEADLPEPA---AGEVVVKVEASGVSFADVQMRRGLYPDQPPLPFTpGYDLVGRVDALGSGVTGFEVG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  80 DRVvipfviacgdcffcrlqqyaacentnagkgAALNKKqipapaalfgyshlyggvpGGQAEYVRVPKGNVGPfkVPPL 159
Cdd:cd08273  83 DRV------------------------------AALTRV-------------------GGNAEYINLDAKYLVP--VPEG 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 160 LSDDKALFLSDILPTAWQAAKN-AQIQQGSSVAVYGA-GPVGLLTIACARLLGAeQIFVVDhhPYRLHFAADRYGAIPIN 237
Cdd:cd08273 112 VDAAEAVCLVLNYVTAYQMLHRaAKVLTGQRVLIHGAsGGVGQALLELALLAGA-EVYGTA--SERNHAALRELGATPID 188
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 238 FDEDSDPAQSIIEqtaghRGVDAVIDAVGFEakgsttetvltnlklegssgkALRQCIAAVRRGGIVSVPGVYAGFIHGF 317
Cdd:cd08273 189 YRTKDWLPAMLTP-----GGVDVVFDGVGGE---------------------SYEESYAALAPGGTLVCYGGNSSLLQGR 242
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 318 L-------FGDAFDKGLSFKMG-QTH---VHAW-----------LGELLPLIEKGLLKPeeIVTHYMPFEEAARGYEIFE 375
Cdd:cd08273 243 RslaalgsLLARLAKLKLLPTGrRATfyyVWRDraedpklfrqdLTELLDLLAKGKIRP--KIAKRLPLSEVAEAHRLLE 320

                .
gi 16128591 376 K 376
Cdd:cd08273 321 S 321
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
1-266 4.31e-18

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: 84.33  E-value: 4.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYH--GPHHVQVENVPDPGVEQaDDIILRITATAICGSDLHLYRG-KIPQVKHgdIFGHEFMGEVVETGKDVKNLQ 77
Cdd:cd08264   1 MKALVFEksGIENLKVEDVKDPKPGP-GEVLIRVKMAGVNPVDYNVINAvKVKPMPH--IPGAEFAGVVEEVGDHVKGVK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  78 KGDRVVIPFVIACGDCFFCRLQQYAACENTNAGkGAALNkkqipapaalfgyshlyggvpGGQAEYVRVPKGNVgpFKVP 157
Cdd:cd08264  78 KGDRVVVYNRVFDGTCDMCLSGNEMLCRNGGII-GVVSN---------------------GGYAEYIVVPEKNL--FKIP 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 158 PLLSDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVVDHHPYRlhfaadRYGAIPI 236
Cdd:cd08264 134 DSISDELAASLPVAALTAYHALKTAGLGPGETVVVFGAsGNTGIFAVQLAKMMGAEVIAVSRKDWLK------EFGADEV 207
                       250       260       270
                ....*....|....*....|....*....|
gi 16128591 237 nfdEDSDPAQSiiEQTAGHRGVDAVIDAVG 266
Cdd:cd08264 208 ---VDYDEVEE--KVKEITKMADVVINSLG 232
PLN02827 PLN02827
Alcohol dehydrogenase-like
24-389 7.78e-18

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 84.57  E-value: 7.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   24 QADDIILRITATAICGSDLHLYRGK--IPQvkhgdIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQY 101
Cdd:PLN02827  36 QPLEIRIKVVSTSLCRSDLSAWESQalFPR-----IFGHEASGIVESIGEGVTEFEKGDHVLTVFTGECGSCRHCISGKS 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  102 AACENTNAGKGAALNKKQIPAPAALFGYSHLYGGVpGGQAEYVRVPKGNVgpFKVPPLLSDDKALFLSDILPTAWQAAKN 181
Cdd:PLN02827 111 NMCQVLGLERKGVMHSDQKTRFSIKGKPVYHYCAV-SSFSEYTVVHSGCA--VKVDPLAPLHKICLLSCGVAAGLGAAWN 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  182 -AQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPINFDEDSDPAQSIIEQTAGHrGVDa 260
Cdd:PLN02827 188 vADVSKGSSVVIFGLGTVGLSVAQGAKLRGASQIIGVDINPEKAEKAKTFGVTDFINPNDLSEPIQQVIKRMTGG-GAD- 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  261 vidaVGFEAKGSTtetvltnlkleGSSGKALRQCI----AAVRRGGIVSVPGVYAGFihGFLFGDAFDKGLSFkmGQTHV 336
Cdd:PLN02827 266 ----YSFECVGDT-----------GIATTALQSCSdgwgLTVTLGVPKAKPEVSAHY--GLFLSGRTLKGSLF--GGWKP 326
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16128591  337 HAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFekREEEC-RKVILVPG 389
Cdd:PLN02827 327 KSDLPSLVDKYMNKEIMIDEFITHNLSFDEINKAFELM--REGKClRCVIHMPK 378
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
7-372 4.80e-17

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: 81.52  E-value: 4.80e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   7 HGPHHVQVENVPDPGVEQaddIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIP- 85
Cdd:cd08296  10 GGPLELVERDVPLPGPGE---VLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVGEGVSRWKVGDRVGVGw 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  86 FVIACGDCFFCRLQQYAACENtnagkgaalnkKQIPapaalfGYShlyggVPGGQAEYVRVPKGNVGPfkVPPLLSDDKA 165
Cdd:cd08296  87 HGGHCGTCDACRRGDFVHCEN-----------GKVT------GVT-----RDGGYAEYMLAPAEALAR--IPDDLDAAEA 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 166 --LFLSDIlpTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIfVVDHHPYRLHFA----ADRYgaipINFD 239
Cdd:cd08296 143 apLLCAGV--TTFNALRNSGAKPGDLVAVQGIGGLGHLAVQYAAKMGFRTV-AISRGSDKADLArklgAHHY----IDTS 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 240 EDsDPAQSIieQTAGhrGVDAVIDAVGFeakGSTTETVLTNLKLEGssgkalRQCIAAVRRGGIVSVPGVYAGF---IHG 316
Cdd:cd08296 216 KE-DVAEAL--QELG--GAKLILATAPN---AKAISALVGGLAPRG------KLLILGAAGEPVAVSPLQLIMGrksIHG 281
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16128591 317 FLFGDAFD--KGLSFkmgqthvhAWLGELLPLIEKgllkpeeivthyMPFEEAARGYE 372
Cdd:cd08296 282 WPSGTALDseDTLKF--------SALHGVRPMVET------------FPLEKANEAYD 319
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-377 5.01e-17

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 81.45  E-value: 5.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKAL---TYHGPHHVQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIP-QVKHGDIFGHEFMGEVVETGKDVKNL 76
Cdd:cd08272   1 MKALvleSFGGPEVFELREVPRPQPG-PGQVLVRVHASGVNPLDTKIRRGGAAaRPPLPAILGCDVAGVVEAVGEGVTRF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  77 QKGDRVvipfviacgdcFFCrlqqyaacentNAGkgaalnkkqipapaalfgyshlYGGVPGGQAEYVRVPKGNVGPfkV 156
Cdd:cd08272  80 RVGDEV-----------YGC-----------AGG----------------------LGGLQGSLAEYAVVDARLLAL--K 113
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 157 PPLLSDDKALFLSDILPTAWQAAKN-AQIQQGSSVAVY-GAGPVGLLTIACARLLGAEQIFVVDhhPYRLHFaADRYGAI 234
Cdd:cd08272 114 PANLSMREAAALPLVGITAWEGLVDrAAVQAGQTVLIHgGAGGVGHVAVQLAKAAGARVYATAS--SEKAAF-ARSLGAD 190
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 235 PINfDEDSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRR-GGIVSVPGVYAGF 313
Cdd:cd08272 191 PII-YYRETVVEYVAEHTGG-RGFDVVFDTVG---------------------GETLDASFEAVALyGRVVSILGGATHD 247
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128591 314 IhgflfGDAFDKGLSF-----------KMGQTHVHAWLGELLPLIEKGLLKPeEIVTHYMPFEEAARGYEIFEKR 377
Cdd:cd08272 248 L-----APLSFRNATYsgvftllplltGEGRAHHGEILREAARLVERGQLRP-LLDPRTFPLEEAAAAHARLESG 316
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
1-354 5.07e-17

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: 81.48  E-value: 5.07e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHH--VQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKNLQK 78
Cdd:cd08249   1 QKAAVLTGPGGglLVVVDVPVPKPG-PDEVLVKVKAVALNPVDWKHQDYGFI-PSYPAILGCDFAGTVVEVGSGVTRFKV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  79 GDRVvipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalFGYSHLYGGVP---GGQAEYVRVPKGNVgpFK 155
Cdd:cd08249  79 GDRV--------------------------------------------AGFVHGGNPNDprnGAFQEYVVADADLT--AK 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 156 VPPLLSDDKA-------------LFLSDILPTAWQAAKNAqiQQGSSVAVYGAG-PVGLLTIACARLLGAEqIFVV---D 218
Cdd:cd08249 113 IPDNISFEEAatlpvglvtaalaLFQKLGLPLPPPKPSPA--SKGKPVLIWGGSsSVGTLAIQLAKLAGYK-VITTaspK 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 219 HHPYrlhfaADRYGAIPInFD-EDSDPAQSIIEQTAGHrgVDAVIDAVGfeakgsttetvltnlklEGSSGKALRQCIAA 297
Cdd:cd08249 190 NFDL-----VKSLGADAV-FDyHDPDVVEDIRAATGGK--LRYALDCIS-----------------TPESAQLCAEALGR 244
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128591 298 VRRGGIVSV--PGVYAGFIHGFLFGDAFDKGLSFKMGQTHVHAW-LGELLP-LIEKGLLKP 354
Cdd:cd08249 245 SGGGKLVSLlpVPEETEPRKGVKVKFVLGYTVFGEIPEDREFGEvFWKYLPeLLEEGKLKP 305
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
37-306 1.10e-16

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 80.46  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   37 ICGSDLHlyrgkipqVKHGD-------IFGHEFMGEVVETGKDVKNLQKGDRVVIP-FVIACGDCFFCRLQQYAACENT- 107
Cdd:PRK09422  37 VCHTDLH--------VANGDfgdktgrILGHEGIGIVKEVGPGVTSLKVGDRVSIAwFFEGCGHCEYCTTGRETLCRSVk 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  108 NAgkgaalnkkqipapaalfGYShlyggVPGGQAEYVRVPKGNVgpFKVPPLLSDDKALFLSDILPTAWQAAKNAQIQQG 187
Cdd:PRK09422 109 NA------------------GYT-----VDGGMAEQCIVTADYA--VKVPEGLDPAQASSITCAGVTTYKAIKVSGIKPG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  188 SSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPINFDEDSDPAQSIIEQTAGHRGvdAVIDAVgf 267
Cdd:PRK09422 164 QWIAIYGAGGLGNLALQYAKNVFNAKVIAVDINDDKLALAKEVGADLTINSKRVEDVAKIIQEKTGGAHA--AVVTAV-- 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 16128591  268 eakgsttetvltnlklegsSGKALRQCIAAVRRGG-IVSV 306
Cdd:PRK09422 240 -------------------AKAAFNQAVDAVRAGGrVVAV 260
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-377 2.08e-16

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


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 79.50  E-value: 2.08e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYH---GPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYRGKIP-QVKHGDIFGHEFMGEVVETGKDVKNL 76
Cdd:cd08276   1 MKAWRLSgggGLDNLKLVEEPVPEP-GPGEVLVRVHAVSLNYRDLLILNGRYPpPVKDPLIPLSDGAGEVVAVGEGVTRF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  77 QKGDRVVIpfviacgdCFFcrlQQYAACENTNAGKGAAlnkkqipapaalfgyshLYGGVPGGQAEYVRVPKGnvGPFKV 156
Cdd:cd08276  80 KVGDRVVP--------TFF---PNWLDGPPTAEDEASA-----------------LGGPIDGVLAEYVVLPEE--GLVRA 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 157 PPLLSDDKAlflsDILP----TAWQA-AKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIfvvdhhpyrlhfA---- 227
Cdd:cd08276 130 PDHLSFEEA----ATLPcaglTAWNAlFGLGPLKPGDTVLVQGTGGVSLFALQFAKAAGARVI------------Atsss 193
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 228 ---ADRYGAIP----INFDEDSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRR 300
Cdd:cd08276 194 dekLERAKALGadhvINYRTTPDWGEEVLKLTGG-RGVDHVVEVGG---------------------PGTLAQSIKAVAP 251
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128591 301 GGIVSVPGVYAGFIHGFLFGDAFDKGLSFKMGQTHVHAWLGELLPLIEKGLLKPeeIVTHYMPFEEAARGYEIFEKR 377
Cdd:cd08276 252 GGVISLIGFLSGFEAPVLLLPLLTKGATLRGIAVGSRAQFEAMNRAIEAHRIRP--VIDRVFPFEEAKEAYRYLESG 326
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-377 4.28e-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: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 78.41  E-value: 4.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVEN--VPDPGVEqADDIILRITATAICGSDLHLYRGKIP---QVKHGDIFGHEFMGEVVETGKDVKN 75
Cdd:cd08267   1 VVYTRYGSPEVLLLLEveVPIPTPK-PGEVLVKVHAASVNPVDWKLRRGPPKlllGRPFPPIPGMDFAGEVVAVGSGVTR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  76 LQKGDRVvipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalFGYSHLYGGvpGGQAEYVRVPKGNVgpFK 155
Cdd:cd08267  80 FKVGDEV--------------------------------------------FGRLPPKGG--GALAEYVVAPESGL--AK 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 156 VPPLLSDD--KALFLSDIlpTAWQA-AKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFV-----VDhhpyrlhF 226
Cdd:cd08267 112 KPEGVSFEeaAALPVAGL--TALQAlRDAGKVKPGQRVLINGAsGGVGTFAVQIAKALGAHVTGVcstrnAE-------L 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 227 AADrYGAipinfDEDSD-PAQSIIEQTAGHRGVDAVIDAVgfeakGSTTETVLTNLKLEGSSGKalrqciaAVRRGGIVS 305
Cdd:cd08267 183 VRS-LGA-----DEVIDyTTEDFVALTAGGEKYDVIFDAV-----GNSPFSLYRASLALKPGGR-------YVSVGGGPS 244
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128591 306 VPGVYAGFIHGFLFGdaFDKGLSFKMGqTHVHAWLGELLPLIEKGLLKPeEIVTHYmPFEEAARGYEIFEKR 377
Cdd:cd08267 245 GLLLVLLLLPLTLGG--GGRRLKFFLA-KPNAEDLEQLAELVEEGKLKP-VIDSVY-PLEDAPEAYRRLKSG 311
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
1-267 5.43e-16

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: 78.80  E-value: 5.43e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPH-HVQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPQVKHGD---IFGHEFMGEVVETGKDvKNL 76
Cdd:cd08230   1 MKAIAVKPGKpGVRVVDIPEPEPT-PGEVLVRTLEVGVCGTDREIVAGEYGTAPPGEdflVLGHEALGVVEEVGDG-SGL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  77 QKGDRVViPFVI-ACGDCFFCRLQQYAACEN---TNAG-KGAalnkkqipapaalfgyshlyggvPGGQAEYVRVPKGNV 151
Cdd:cd08230  79 SPGDLVV-PTVRrPPGKCLNCRIGRPDFCETgeyTERGiKGL-----------------------HGFMREYFVDDPEYL 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 152 gpFKVPPLLSDDKALF--LSDILpTAWQAAKNAQ----IQQGSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLH 225
Cdd:cd08230 135 --VKVPPSLADVGVLLepLSVVE-KAIEQAEAVQkrlpTWNPRRALVLGAGPIGLLAALLLRLRGFE-VYVLNRRDPPDP 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 16128591 226 FA--ADRYGAIPINFDEDSdpaqsiIEQTAGHRGVDAVIDAVGF 267
Cdd:cd08230 211 KAdiVEELGATYVNSSKTP------VAEVKLVGEFDLIIEATGV 248
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
26-368 6.84e-16

enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176179 [Multi-domain]  Cd Length: 293  Bit Score: 77.61  E-value: 6.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  26 DDIILRITATAICGSDLHLYRGKIPQVKHGdiFGHEFMGEVVETGKDVKNLQKGDRVVipfviacgdcffcrlqqyaace 105
Cdd:cd05195   1 DEVEVEVKAAGLNFRDVLVALGLLPGDETP--LGLECSGIVTRVGSGVTGLKVGDRVM---------------------- 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 106 ntnagkgaalnkkqipapaalfgyshlyGGVPGGQAEYVRVPKGNVgpFKVPPLLSDDKAlflsDILP----TAWQAAKN 181
Cdd:cd05195  57 ----------------------------GLAPGAFATHVRVDARLV--VKIPDSLSFEEA----ATLPvaylTAYYALVD 102
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 182 -AQIQQGSSVAVY-GAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGAIP-INFDEDSDPAQSIIEQTAGhRGV 258
Cdd:cd05195 103 lARLQKGESVLIHaAAGGVGQAAIQLAQHLGAE-VFATVGSEEKREFLRELGGPVDhIFSSRDLSFADGILRATGG-RGV 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 259 DAVIDAVgfeakgsttetvltnlklegsSGKALRQCIAAVRRGG-IVSVpGVYAGFIHGFLFGDAFDKGLSF-------- 329
Cdd:cd05195 181 DVVLNSL---------------------SGELLRASWRCLAPFGrFVEI-GKRDILSNSKLGMRPFLRNVSFssvdldql 238
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 16128591 330 -KMGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAA 368
Cdd:cd05195 239 aRERPELLRELLREVLELLEAGVLKPLPPTVVPSASEIDA 278
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
1-266 2.89e-15

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 76.22  E-value: 2.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    1 MKALT---YHGPHHVQVENVPDPGVEQaDDIILRITATAICGSDLHLYRGKIPQVK-HGDIFGHEFMGEVVETGKDVKNL 76
Cdd:PTZ00354   2 MRAVTlkgFGGVDVLKIGESPKPAPKR-NDVLIKVSAAGVNRADTLQRQGKYPPPPgSSEILGLEVAGYVEDVGSDVKRF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   77 QKGDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaALFGyshlyggvPGGQAEYVRVPKGNVgpFKV 156
Cdd:PTZ00354  81 KEGDRVM-----------------------------------------ALLP--------GGGYAEYAVAHKGHV--MHI 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  157 PPLLSDDKALFLSDILPTAWQAAK-NAQIQQGSSVAVY-GAGPVGLLTIACARLLGAEQIfVVDHHPYRLHFAaDRYGAI 234
Cdd:PTZ00354 110 PQGYTFEEAAAIPEAFLTAWQLLKkHGDVKKGQSVLIHaGASGVGTAAAQLAEKYGAATI-ITTSSEEKVDFC-KKLAAI 187
                        250       260       270
                 ....*....|....*....|....*....|...
gi 16128591  235 P-INFDEDSDPAQSIIEQTaGHRGVDAVIDAVG 266
Cdd:PTZ00354 188 IlIRYPDEEGFAPKVKKLT-GEKGVNLVLDCVG 219
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
24-266 2.11e-14

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


Pssm-ID: 176259 [Multi-domain]  Cd Length: 373  Bit Score: 73.89  E-value: 2.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  24 QADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAA 103
Cdd:cd08299  31 KAHEVRIKIVATGICRSDDHVVSGKLV-TPFPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFVPQCGKCRACLNPESNL 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 104 CENTNAGKGAAL----------NKKQIpapaalfgysHLYGGVpGGQAEYVRVPKGNVGpfKVPPLLSDDKALFLSDILP 173
Cdd:cd08299 110 CLKNDLGKPQGLmqdgtsrftcKGKPI----------HHFLGT-STFSEYTVVDEIAVA--KIDAAAPLEKVCLIGCGFS 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 174 TAWQAA-KNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRlhFA-ADRYGAIP-INFDEDSDPAQSII- 249
Cdd:cd08299 177 TGYGAAvNTAKVTPGSTCAVFGLGGVGLSAIMGCKAAGASRIIAVDINKDK--FAkAKELGATEcINPQDYKKPIQEVLt 254
                       250
                ....*....|....*..
gi 16128591 250 EQTAGhrGVDAVIDAVG 266
Cdd:cd08299 255 EMTDG--GVDFSFEVIG 269
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-388 3.82e-14

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: 73.10  E-value: 3.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKA--LTYHGP----HHVQVENVPDPGveqADDIILRITATAICGSDLHLYRG-------------------------KI 49
Cdd:cd08274   1 MRAvlLTGHGGldklVYRDDVPVPTPA---PGEVLIRVGACGVNNTDINTREGwystevdgatdstgageagwwggtlSF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  50 PQVKHGDIFGHefmgeVVETGKDVKNLQKGDRVVIPFVIacgdcffcrlqqYAACENTnagkgaalnkkqiPAPAALFGy 129
Cdd:cd08274  78 PRIQGADIVGR-----VVAVGEGVDTARIGERVLVDPSI------------RDPPEDD-------------PADIDYIG- 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 130 shlyGGVPGGQAEYVRVPKGNVgpFKVPPLLSDDK-ALFlsdilPTAWQAAKN----AQIQQGSSVAVYGA-GPVGLLTI 203
Cdd:cd08274 127 ----SERDGGFAEYTVVPAENA--YPVNSPLSDVElATF-----PCSYSTAENmlerAGVGAGETVLVTGAsGGVGSALV 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 204 ACARLLGAEQIFVV--DHHPYRLHFAADRYgaipINFDEDSDPAqsiiEQTAGHRGVDAVIDAVGfeakGSTTETVLTNL 281
Cdd:cd08274 196 QLAKRRGAIVIAVAgaAKEEAVRALGADTV----ILRDAPLLAD----AKALGGEPVDVVADVVG----GPLFPDLLRLL 263
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 282 KLEGssgkalRQCIAAVRRGGIVSVPgvyagfihgflFGDAFDKGLSFkMGQTHV-HAWLGELLPLIEKGLLKPeeIVTH 360
Cdd:cd08274 264 RPGG------RYVTAGAIAGPVVELD-----------LRTLYLKDLTL-FGSTLGtREVFRRLVRYIEEGEIRP--VVAK 323
                       410       420
                ....*....|....*....|....*...
gi 16128591 361 YMPFEEAARGYEIFEKReEECRKVILVP 388
Cdd:cd08274 324 TFPLSEIREAQAEFLEK-RHVGKLVLVP 350
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
1-312 5.05e-13

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: 69.56  E-value: 5.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYH---GPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDvkNLQ 77
Cdd:cd08243   1 MKAIVIEqpgGPEVLKLREIPIP-EPKPGWVLIRVKAFGLNRSEIFTRQGHSPSVKFPRVLGIEAVGEVEEAPGG--TFT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  78 KGDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqipapAALFGYSHLYggvPGGQAEYVRVPKGNVGPFKVP 157
Cdd:cd08243  78 PGQRVA----------------------------------------TAMGGMGRTF---DGSYAEYTLVPNEQVYAIDSD 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 158 plLSDDKALFLSDILPTAWQAAKNA-QIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVVdHHPYR----LHFAADRY 231
Cdd:cd08243 115 --LSWAELAALPETYYTAWGSLFRSlGLQPGDTLLIRGGtSSVGLAALKLAKALGATVTATT-RSPERaallKELGADEV 191
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 232 gaipinFDEDSDPAQSIIEQTAghrGVDAVIDAVGfeakgstTETVLTNLKlegssgkalrqciaAVRRGGIVSVPGVYA 311
Cdd:cd08243 192 ------VIDDGAIAEQLRAAPG---GFDKVLELVG-------TATLKDSLR--------------HLRPGGIVCMTGLLG 241

                .
gi 16128591 312 G 312
Cdd:cd08243 242 G 242
adh_fam_2 TIGR02822
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
8-212 5.16e-12

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


Pssm-ID: 131869 [Multi-domain]  Cd Length: 329  Bit Score: 66.48  E-value: 5.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591     8 GPHHVQVENVPDPGveqADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFV 87
Cdd:TIGR02822  13 GPLRFVERPVPRPG---PGELLVRVRACGVCRTDLHVSEGDLPVHRPRVTPGHEVVGEVAGRGADAGGFAVGDRVGIAWL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    88 -IACGDCFFCRLQQYAACENTNagkgaalnkkqipapaalfgyshlYGG--VPGGQAEYVRVPKGNVgpFKVPPLLSDDK 164
Cdd:TIGR02822  90 rRTCGVCRYCRRGAENLCPASR------------------------YTGwdTDGGYAEYTTVPAAFA--YRLPTGYDDVE 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 16128591   165 --ALFLSDILptAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAE 212
Cdd:TIGR02822 144 laPLLCAGII--GYRALLRASLPPGGRLGLYGFGGSAHLTAQVALAQGAT 191
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-376 6.11e-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: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 66.08  E-value: 6.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYH---GPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGK-IPQVKHGDIFGHEFMGEVVETGKDVKNL 76
Cdd:cd08268   1 MRAVRFHqfgGPEVLRIEELPVP-APGAGEVLIRVEAIGLNRADAMFRRGAyIEPPPLPARLGYEAAGVVEAVGAGVTGF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  77 QKGDRVVIpfviacgdcffcrlqqyaacentnagkgaalnkkqipAPAALFGYSHLYGgvpggqaEYVRVPKGNVgpFKV 156
Cdd:cd08268  80 AVGDRVSV-------------------------------------IPAADLGQYGTYA-------EYALVPAAAV--VKL 113
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 157 PPLLSDDKALFLSDILPTAWQA-AKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVVDHhPYRLHFAADrYGAI 234
Cdd:cd08268 114 PDGLSFVEAAALWMQYLTAYGAlVELAGLRPGDSVLITAAsSSVGLAAIQIANAAGATVIATTRT-SEKRDALLA-LGAA 191
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 235 PINFDEDSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRRGGIVSVPGVYAGFI 314
Cdd:cd08268 192 HVIVTDEEDLVAEVLRITGG-KGVDVVFDPVG---------------------GPQFAKLADALAPGGTLVVYGALSGEP 249
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 315 HGFLFGDAFDKGLSFK--------MGQTHVHAWLGELLPLIEKGLLKPeeIVTHYMPFEEAARGYEIFEK 376
Cdd:cd08268 250 TPFPLKAALKKSLTFRgysldeitLDPEARRRAIAFILDGLASGALKP--VVDRVFPFDDIVEAHRYLES 317
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
2-388 1.88e-11

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: 64.77  E-value: 1.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   2 KALTYH---GPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKNLQK 78
Cdd:cd05286   1 KAVRIHktgGPEVLEYEDVPVP-EPGPGEVLVRNTAIGVNFIDTYFRSGLYP-LPLPFVLGVEGAGVVEAVGPGVTGFKV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  79 GDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalfgyshlYGGVPGGQAEYVRVPKGNVgpFKVPP 158
Cdd:cd05286  79 GDRVA-------------------------------------------------YAGPPGAYAEYRVVPASRL--VKLPD 107
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 159 LLSDDKA--LFLSDIlpTAWQAAKNA-QIQQGSSVAVYG-AGPVGLLTIACARLLGAEQIFVVDHhPYRLHFAADrYGAI 234
Cdd:cd05286 108 GISDETAaaLLLQGL--TAHYLLRETyPVKPGDTVLVHAaAGGVGLLLTQWAKALGATVIGTVSS-EEKAELARA-AGAD 183
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 235 -PINFDEDsDPAQSIIEQTAGhRGVDAVIDAVGfeakGSTtetvltnlkLEGSsgkalrqcIAAVRRGGIVSVPGVYAGF 313
Cdd:cd05286 184 hVINYRDE-DFVERVREITGG-RGVDVVYDGVG----KDT---------FEGS--------LDSLRPRGTLVSFGNASGP 240
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 314 IHGFLFGDAFDKGLSFK----MGQTHVHAWL----GELLPLIEKGLLKPeEIVTHYmPFEEAARGYEIFEKReeecR--- 382
Cdd:cd05286 241 VPPFDLLRLSKGSLFLTrpslFHYIATREELlaraAELFDAVASGKLKV-EIGKRY-PLADAAQAHRDLESR----Kttg 314

                ....*.
gi 16128591 383 KVILVP 388
Cdd:cd05286 315 KLLLIP 320
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
9-387 2.39e-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: 64.22  E-value: 2.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   9 PHHVQVENVP-DPGVEQADDIILRITATAICGSDLHL----YRGKIPQvkhGDIFGHEFMGEVVETGKDVKNLQKGDRVv 83
Cdd:cd05282   9 PLPLVLELVSlPIPPPGPGEVLVRMLAAPINPSDLITisgaYGSRPPL---PAVPGNEGVGVVVEVGSGVSGLLVGQRV- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  84 ipfviacgdcffcrlqqyaacentnagkgaalnkkqIPAPAAlfgyshlyggvpGGQAEYVRVPKGNVgpFKVPPLLSDD 163
Cdd:cd05282  85 ------------------------------------LPLGGE------------GTWQEYVVAPADDL--IPVPDSISDE 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 164 KALFLSdILP-TAW-QAAKNAQIQQGSSVAVYGAGP-VGLLTIACARLLGAEQIFVV--DHHPYRLhfaaDRYGAIPINF 238
Cdd:cd05282 115 QAAMLY-INPlTAWlMLTEYLKLPPGDWVIQNAANSaVGRMLIQLAKLLGFKTINVVrrDEQVEEL----KALGADEVID 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 239 DEDSDPAQSIIEQTaGHRGVDAVIDAVGfeakgsttetvltnlkleGSSGKALrqcIAAVRRGGIVSVPGVYAG----FI 314
Cdd:cd05282 190 SSPEDLAQRVKEAT-GGAGARLALDAVG------------------GESATRL---ARSLRPGGTLVNYGLLSGepvpFP 247
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 315 HGFLFGDAFD-KG--LSFKMGQTHVHAW---LGELLPLIEKGLLKPEeiVTHYMPFEEAArgyEIFEKREEECR--KVIL 386
Cdd:cd05282 248 RSVFIFKDITvRGfwLRQWLHSATKEAKqetFAEVIKLVEAGVLTTP--VGAKFPLEDFE---EAVAAAEQPGRggKVLL 322

                .
gi 16128591 387 V 387
Cdd:cd05282 323 T 323
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
197-330 3.19e-11

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 60.31  E-value: 3.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   197 PVGLLTIACARLLGAEqIFVVDHHPYRLHFAAdRYGAIPINFDEDSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttet 276
Cdd:pfam00107   1 GVGLAAIQLAKAAGAK-VIAVDGSEEKLELAK-ELGADHVINPKETDLVEEIKELTGG-KGVDVVFDCVG---------- 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 16128591   277 vltnlklegsSGKALRQCIAAVRRGGIVsvpgVYAGFIHG---FLFGDAFDKGLSFK 330
Cdd:pfam00107  68 ----------SPATLEQALKLLRPGGRV----VVVGLPGGplpLPLAPLLLKELTIL 110
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
25-160 4.46e-11

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 63.66  E-value: 4.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   25 ADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVI-ACGDCFFCR--LQQY 101
Cdd:PLN02514  34 PEDVVIKVIYCGICHTDLHQIKNDLGMSNYPMVPGHEVVGEVVEVGSDVSKFTVGDIVGVGVIVgCCGECSPCKsdLEQY 113
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  102 aaCentnagkgaalNKKqipapaaLFGYSHLY-GGVP--GGQAE--------YVRVPKGnVGPFKVPPLL 160
Cdd:PLN02514 114 --C-----------NKR-------IWSYNDVYtDGKPtqGGFASamvvdqkfVVKIPEG-MAPEQAAPLL 162
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
41-354 7.27e-11

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 62.41  E-value: 7.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591     41 DLHLYRGKIPqvkHGDIFGHEFMGEVVETGKDVKNLQKGDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqi 120
Cdd:smart00829  12 DVLIALGLYP---GEAVLGGECAGVVTRVGPGVTGLAVGDRVM------------------------------------- 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    121 papaalfgyshlyGGVPGGQAEYVRVPKGNVgpFKVPPLLSDDKALFLSDILPTAWQAAKN-AQIQQGSSVAVY-GAGPV 198
Cdd:smart00829  52 -------------GLAPGAFATRVVTDARLV--VPIPDGWSFEEAATVPVVFLTAYYALVDlARLRPGESVLIHaAAGGV 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    199 GLLTIACARLLGAEqIFVVDHHPYRLHFaADRYGaIPIN--FD-EDSDPAQSIIEQTAGhRGVDAVIDAVgfeakgstte 275
Cdd:smart00829 117 GQAAIQLARHLGAE-VFATAGSPEKRDF-LRALG-IPDDhiFSsRDLSFADEILRATGG-RGVDVVLNSL---------- 182
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591    276 tvltnlklegsSGKALRQCIAAVRRGGIvsvpgvyagFI---------HGFLFGDAFDKGLSF------KM--GQTHVHA 338
Cdd:smart00829 183 -----------SGEFLDASLRCLAPGGR---------FVeigkrdirdNSQLAMAPFRPNVSYhavdldALeeGPDRIRE 242
                          330
                   ....*....|....*.
gi 16128591    339 WLGELLPLIEKGLLKP 354
Cdd:smart00829 243 LLAEVLELFAEGVLRP 258
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-286 2.76e-10

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: 61.14  E-value: 2.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGP---HHVQVENVPDPGVeQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQ 77
Cdd:cd08271   1 MKAWVLPKPgaaLQLTLEEIEIPGP-GAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTGWK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  78 KGDRVVIpfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalfgysHLYGGVPGGQAEYVRVPkgNVGPFKVP 157
Cdd:cd08271  80 VGDRVAY----------------------------------------------HASLARGGSFAEYTVVD--ARAVLPLP 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 158 PLLSDDKALFLSDILPTAWQA-AKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEqIFVV---DHHPYRLHFAADryg 232
Cdd:cd08271 112 DSLSFEEAAALPCAGLTAYQAlFKKLRIEAGRTILITGGaGGVGSFAVQLAKRAGLR-VITTcskRNFEYVKSLGAD--- 187
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 16128591 233 aipINFDEDSDPAQSIIEQTAGHRGVDAVIDAVGfeakGSTTETVLTNLKLEGS 286
Cdd:cd08271 188 ---HVIDYNDEDVCERIKEITGGRGVDAVLDTVG----GETAAALAPTLAFNGH 234
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
1-388 8.58e-10

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: 59.52  E-value: 8.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYH--GPHHV-QVENVPDPGVEqADDIILRITATAICGSDLHLYRGKI------PQVKHGDIfghefMGEVVETGK 71
Cdd:cd08253   1 MRAIRYHefGAPDVlRLGDLPVPTPG-PGEVLVRVHASGVNPVDTYIRAGAYpglpplPYVPGSDG-----AGVVEAVGE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  72 DVKNLQKGDRVvipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalFGYSHLYGGVPGGQAEYVRVPKGNV 151
Cdd:cd08253  75 GVDGLKVGDRV--------------------------------------------WLTNLGWGRRQGTAAEYVVVPADQL 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 152 gpFKVPPLLSDDKALFLSdiLP--TAWQAA-KNAQIQQGSSVAVYG-AGPVGLLTIACARLLGAEQIFVVDhHPYRLHFA 227
Cdd:cd08253 111 --VPLPDGVSFEQGAALG--IPalTAYRALfHRAGAKAGETVLVHGgSGAVGHAAVQLARWAGARVIATAS-SAEGAELV 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 228 ADRYGAIPINFDEDsDPAQSIIEQTAGhRGVDAVIDAvgfeakgsttetvltnlklegSSGKALRQCIAAVRRGGIVSVP 307
Cdd:cd08253 186 RQAGADAVFNYRAE-DLADRILAATAG-QGVDVIIEV---------------------LANVNLAKDLDVLAPGGRIVVY 242
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 308 G--VYAGFIHgflFGDAFDKGLS------FKMGQTHVHAWLGELLPLIEKGLLKPEeiVTHYMPFEEAARGYEIFEkREE 379
Cdd:cd08253 243 GsgGLRGTIP---INPLMAKEASirgvllYTATPEERAAAAEAIAAGLADGALRPV--IAREYPLEEAAAAHEAVE-SGG 316

                ....*....
gi 16128591 380 ECRKVILVP 388
Cdd:cd08253 317 AIGKVVLDP 325
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
1-377 8.43e-09

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: 56.85  E-value: 8.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKAL---TYHGPHH-VQVENVPDPGVEQADDIILRITATAI--------CG---SDLHLYRGKIPQVKHGDIF----GHE 61
Cdd:cd08248   1 MKAWqihSYGGIDSlLLLENARIPVIRKPNQVLIKVHAASVnpidvlmrSGygrTLLNKKRKPQSCKYSGIEFpltlGRD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  62 FMGEVVETGKDVKNLQKGDRV--VIPFVIacgdcffcrlqqyaacentnagkgaalnkkqipapaalfgyshlyggvPGG 139
Cdd:cd08248  81 CSGVVVDIGSGVKSFEIGDEVwgAVPPWS------------------------------------------------QGT 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 140 QAEYVRVPKGNVGpfKVPPLLSDDKALFLSDILPTAWQAAKNA-----QIQQGSSVAVYGA-GPVGllTIACaRLLGAEQ 213
Cdd:cd08248 113 HAEYVVVPENEVS--KKPKNLSHEEAASLPYAGLTAWSALVNVgglnpKNAAGKRVLILGGsGGVG--TFAI-QLLKAWG 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 214 IFVV-----DHHPYRLHFAADRygAIPINfdedsdpAQSIIEQTAGHRGVDAVIDAVGfeakgsttetvltnLKLEGSSG 288
Cdd:cd08248 188 AHVTttcstDAIPLVKSLGADD--VIDYN-------NEDFEEELTERGKFDVILDTVG--------------GDTEKWAL 244
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 289 KALRQCiaavrrGGIVS-VPGV-----YAGFIHGFLFG--DAFDKGLSFKMGQTHVHaW---------LGELLPLIEKGL 351
Cdd:cd08248 245 KLLKKG------GTYVTlVSPLlkntdKLGLVGGMLKSavDLLKKNVKSLLKGSHYR-WgffspsgsaLDELAKLVEDGK 317
                       410       420
                ....*....|....*....|....*.
gi 16128591 352 LKPeeIVTHYMPFEEAARGYEIFEKR 377
Cdd:cd08248 318 IKP--VIDKVFPFEEVPEAYEKVESG 341
ADH_N_assoc pfam13823
Alcohol dehydrogenase GroES-associated; This short domain is frequently found at the ...
1-23 1.81e-08

Alcohol dehydrogenase GroES-associated; This short domain is frequently found at the N-terminus of the alcohol dehydrogenase GroES-like domain, Pfam: PF08240.


Pssm-ID: 433504 [Multi-domain]  Cd Length: 23  Bit Score: 49.71  E-value: 1.81e-08
                          10        20
                  ....*....|....*....|...
gi 16128591     1 MKALTYHGPHHVQVENVPDPGVE 23
Cdd:pfam13823   1 MKAVTYQGPKDVRVEEVPDPRIE 23
sorbose_phosphate_red cd08238
L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, ...
2-264 2.33e-08

L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, catalyzes the NADPH-dependent conversion of l-sorbose 1-phosphate to d-glucitol 6-phosphate in the metabolism of L-sorbose to (also converts d-fructose 1-phosphate to d-mannitol 6-phosphate). The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176200 [Multi-domain]  Cd Length: 410  Bit Score: 55.52  E-value: 2.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   2 KALTYHGPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYR--GKIPQV-----KHGDIFGHEFMGEVVETGKDVK 74
Cdd:cd08238   4 KAWRMYGKGDLRLEKFELPEI-ADDEILVRVISDSLCFSTWKLALqgSDHKKVpndlaKEPVILGHEFAGTILKVGKKWQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  75 N-LQKGDRVVIPfviacgdcffcrlqqyaacentnagkgAALnkkQIPAPAALFGYSHLYggvPGGQAEYVRVPKgNVGP 153
Cdd:cd08238  83 GkYKPGQRFVIQ---------------------------PAL---ILPDGPSCPGYSYTY---PGGLATYHIIPN-EVME 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 154 FKVPPLLSDDKALFLSDILPTAW-QAAKNAQIQ--------------QGSSVAVYGAGPVGLLTIACARLL--GAEQIFV 216
Cdd:cd08238 129 QDCLLIYEGDGYAEASLVEPLSCvIGAYTANYHlqpgeyrhrmgikpGGNTAILGGAGPMGLMAIDYAIHGpiGPSLLVV 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16128591 217 VDHHPYRLHFAADRYGAIP---------INFDEDSDPAQSIIEQTAGHRGVDAVIDA 264
Cdd:cd08238 209 TDVNDERLARAQRLFPPEAasrgiellyVNPATIDDLHATLMELTGGQGFDDVFVFV 265
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
1-83 4.56e-08

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: 54.53  E-value: 4.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTY--HG-PHHV-QVENVPDPGVEQADDIILRITATAICGSDLHL----YRGKIPQVKHGD-IFGHEFMGEVVETGK 71
Cdd:cd08290   1 AKALVYteHGePKEVlQLESYEIPPPGPPNEVLVKMLAAPINPADINQiqgvYPIKPPTTPEPPaVGGNEGVGEVVKVGS 80
                        90
                ....*....|..
gi 16128591  72 DVKNLQKGDRVV 83
Cdd:cd08290  81 GVKSLKPGDWVI 92
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-370 7.81e-08

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


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 53.53  E-value: 7.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHG--PHHVQVENVPDPgVEQADDIILRITATAICGSDLHLyrgkIPQVKHGDIFGHEFMGEVVETGKDVKNLQK 78
Cdd:cd08270   1 MRALVVDPdaPLRLRLGEVPDP-QPAPHEALVRVAAISLNRGELKF----AAERPDGAVPGWDAAGVVERAAADGSGPAV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  79 GDRVVIpfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalfgyshlyGGVPGGQAEYVRVPKGNVGPfkVPP 158
Cdd:cd08270  76 GARVVG-------------------------------------------------LGAMGAWAELVAVPTGWLAV--LPD 104
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 159 LLSDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVVdHHPYRLHFAADRYGA-IPI 236
Cdd:cd08270 105 GVSFAQAATLPVAGVTALRALRRGGPLLGRRVLVTGAsGGVGRFAVQLAALAGAHVVAVV-GSPARAEGLRELGAAeVVV 183
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 237 NFDEDSDPAqsiieqtaghrgVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRRGGIVSVPGVYAGFIHG 316
Cdd:cd08270 184 GGSELSGAP------------VDLVVDSVG---------------------GPQLARALELLAPGGTVVSVGSSSGEPAV 230
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128591 317 F----LFGDAFDKGL-SFKMGQ-THVHAWLGELLPLIEKGLLKPE-EIVTHYMPFEEAARG 370
Cdd:cd08270 231 FnpaaFVGGGGGRRLyTFFLYDgEPLAADLARLLGLVAAGRLDPRiGWRGSWTEIDEAAEA 291
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
26-269 3.30e-07

polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176213 [Multi-domain]  Cd Length: 303  Bit Score: 51.66  E-value: 3.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  26 DDIILRITATAICGSDLHLYRGKIPQV-KHGDIFGHEFMGEVVETGKDVKNLQKGDRVVipfviacgdcffcrlqqyaac 104
Cdd:cd08251   8 GEVRIQVRAFSLNFGDLLCVRGLYPTMpPYPFTPGFEASGVVRAVGPHVTRLAVGDEVI--------------------- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 105 entnAGKGAALnkkqipapaalfgyshlyggvpGGQAEYVRVPKGNVgpFKVPPLLSDDKALFLSDILPTAWQAAKNAQI 184
Cdd:cd08251  67 ----AGTGESM----------------------GGHATLVTVPEDQV--VRKPASLSFEEACALPVVFLTVIDAFARAGL 118
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 185 QQGSSVAVYGA-GPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGAIPINFDEDsDPAQSIIEQTaGHRGVDAVID 263
Cdd:cd08251 119 AKGEHILIQTAtGGTGLMAVQLARLKGAE-IYATASSDDKLEYLKQLGVPHVINYVEE-DFEEEIMRLT-GGRGVDVVIN 195

                ....*.
gi 16128591 264 AVGFEA 269
Cdd:cd08251 196 TLSGEA 201
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
8-388 6.33e-07

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


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 51.05  E-value: 6.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   8 GPHHVQVENVPDPGVEQaDDIILRITAtaiCG---SDLHLYRGKIPQ-VKHGDIFGHEFMGEVVETGKDVKNLQKGDRVV 83
Cdd:cd08275  10 GLDKLKVEKEALPEPSS-GEVRVRVEA---CGlnfADLMARQGLYDSaPKPPFVPGFECAGTVEAVGEGVKDFKVGDRVM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  84 ipfviaCGDCFfcrlqqyaacentnagkgaalnkkqipapaalfgyshlyggvpGGQAEYVRVPKGNVgpFKVPPLLS-D 162
Cdd:cd08275  86 ------GLTRF-------------------------------------------GGYAEVVNVPADQV--FPLPDGMSfE 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 163 DKALFLSDILpTAWQAA-KNAQIQQGSSVAVYGA-GPVGLLTIACARLLgaEQIFVV-DHHPYRLHFAADRYGAIPINFd 239
Cdd:cd08275 115 EAAAFPVNYL-TAYYALfELGNLRPGQSVLVHSAaGGVGLAAGQLCKTV--PNVTVVgTASASKHEALKENGVTHVIDY- 190
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 240 EDSDPAQSIIEQTAghRGVDAVIDAVGfeakGSTTETVLTNLK------LEGSSgkalrqCIAAVRRGGIVSVPGVY--- 310
Cdd:cd08275 191 RTQDYVEEVKKISP--EGVDIVLDALG----GEDTRKSYDLLKpmgrlvVYGAA------NLVTGEKRSWFKLAKKWwnr 258
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 311 ---------------AGFIHGFLFGDafDKGLSFKMGQthvhawlgeLLPLIEKGLLKPeeIVTHYMPFEEAARGYEIFE 375
Cdd:cd08275 259 pkvdpmklisenksvLGFNLGWLFEE--RELLTEVMDK---------LLKLYEEGKIKP--KIDSVFPFEEVGEAMRRLQ 325
                       410
                ....*....|...
gi 16128591 376 KREEEcRKVILVP 388
Cdd:cd08275 326 SRKNI-GKVVLTP 337
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
26-101 1.31e-06

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 49.88  E-value: 1.31e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128591   26 DDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVI-ACGDCFFCR--LQQY 101
Cdd:PLN02586  38 EDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGKNVKKFKEGDRVGVGVIVgSCKSCESCDqdLENY 116
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
250-377 2.72e-06

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 46.55  E-value: 2.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   250 EQTAGHRGVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRRGG-IVSVPGVYAGFIHGFLFGDAFDKGLS 328
Cdd:pfam13602  15 VQATGGEGVDVVLDTVG---------------------GEAFEASLRVLPGGGrLVTIGGPPLSAGLLLPARKRGGRGVK 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16128591   329 FKMGQT---HVHAWLGELLPLIEKGLLKPeeIVTHYMPFEEAARGYEIFEKR 377
Cdd:pfam13602  74 YLFLFVrpnLGADILQELADLIEEGKLRP--VIDRVFPLEEAAEAHRYLESG 123
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
2-203 6.77e-06

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: 47.65  E-value: 6.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   2 KALTYH---GPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDI-FGHEFMGEVVETGKDVKNLQ 77
Cdd:cd08247   2 KALTFKnntSPLTITTIKLPLPNCYKDNEIVVKVHAAALNPVDLKLYNSYTFHFKVKEKgLGRDYSGVIVKVGSNVASEW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591  78 K-GDRVvipfviaCGDcffcrlqqyaacentnagkgaalnkkqipapaalfgYSHLYGGVpGGQAEYVRV-PKGNVGPF- 154
Cdd:cd08247  82 KvGDEV-------CGI------------------------------------YPHPYGGQ-GTLSQYLLVdPKKDKKSIt 117
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16128591 155 KVPPLLSDDKALFLSDILPTAWQAAKNAQIQ--QGSSVAVYGAG-PVGLLTI 203
Cdd:cd08247 118 RKPENISLEEAAAWPLVLGTAYQILEDLGQKlgPDSKVLVLGGStSVGRFAI 169
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
134-388 6.93e-06

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: 47.75  E-value: 6.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 134 GGVPGGQAEYVRVPKGNVGPfkVPPLLSDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAE 212
Cdd:cd08244  92 GRAGGGYAELAVADVDSLHP--VPDGLDLEAAVAVVHDGRTALGLLDLATLTPGDVVLVTAAaGGLGSLLVQLAKAAGAT 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 213 QIFVVdHHPYRLHFAADRYGAIPINFDEDSDPAQsiIEQTAGHRGVDAVIDAVGfeakgsttetvltnlklegssGKALR 292
Cdd:cd08244 170 VVGAA-GGPAKTALVRALGADVAVDYTRPDWPDQ--VREALGGGGVTVVLDGVG---------------------GAIGR 225
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 293 QCIAAVRRGGIVSVPGVYAGFIHGFLFGDAFDKGLSF------KMGQTHVHAWLGELLPLIEKGLLKPeeIVTHYMPFEE 366
Cdd:cd08244 226 AALALLAPGGRFLTYGWASGEWTALDEDDARRRGVTVvgllgvQAERGGLRALEARALAEAAAGRLVP--VVGQTFPLER 303
                       250       260
                ....*....|....*....|..
gi 16128591 367 AARGYEIFEKREEEcRKVILVP 388
Cdd:cd08244 304 AAEAHAALEARSTV-GKVLLLP 324
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
138-360 1.26e-04

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


Pssm-ID: 176190 [Multi-domain]  Cd Length: 329  Bit Score: 43.62  E-value: 1.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 138 GGQAEYVRVPkGNVGPFKVPPLLSDDKALFLSdIL----PTAWQAAKN-AQIQQGSSVAV-YGAGPVGLLTIACARLLGA 211
Cdd:cd05288  94 LGWQEYAVVD-GASGLRKLDPSLGLPLSAYLG-VLgmtgLTAYFGLTEiGKPKPGETVVVsAAAGAVGSVVGQIAKLLGA 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 212 ---------EQI-FVVDHhpyrLHF-AAdrygaipINFDEDsDPAQSIIEQTAGhrGVDAVIDAVGfeakGSTTETVLTN 280
Cdd:cd05288 172 rvvgiagsdEKCrWLVEE----LGFdAA-------INYKTP-DLAEALKEAAPD--GIDVYFDNVG----GEILDAALTL 233
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591 281 LKLEGssgkalRqcIAAVrrGGI-------VSVPGVYAGFIH------GFLFGDAFDkglsfkmgqtHVHAWLGELLPLI 347
Cdd:cd05288 234 LNKGG------R--IALC--GAIsqynatePPGPKNLGNIITkrltmqGFIVSDYAD----------RFPEALAELAKWL 293
                       250
                ....*....|...
gi 16128591 348 EKGLLKPEEIVTH 360
Cdd:cd05288 294 AEGKLKYREDVVE 306
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
26-96 1.39e-04

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 43.86  E-value: 1.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128591   26 DDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVI-ACGDCFFC 96
Cdd:PLN02178  32 NDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVGKNVTKFKEGDRVGVGVIIgSCQSCESC 103
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
1-82 6.03e-04

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: 41.74  E-value: 6.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128591   1 MKALTYHGPHHVQVEN------VPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVK 74
Cdd:cd08252   1 MKAIGFTQPLPITDPDslidieLPKP-VPGGRDLLVRVEAVSVNPVDTKVRAGGAPVPGQPKILGWDASGVVEAVGSEVT 79

                ....*...
gi 16128591  75 NLQKGDRV 82
Cdd:cd08252  80 LFKVGDEV 87
 
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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