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Conserved domains on  [gi|1352184135|gb|AVI55151|]
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glutathione-dependent formaldehyde dehydrogenase [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 1352184135   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08283     1 MKALVWHGKGDVRVEEVPDPKIEDPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGPEVRNLKVGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACENTNAGKGAAlnKKQIPAPAALFGYSHLYGGVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd08283    81 RVVVPFTIACGECFYCKRGLYSQCDNTNPSAEMA--KLYGHAGAGIFGYSHLTGGYAGGQAEYVRVPFADVGPFKIPDDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 161 SDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPINFDE 240
Cdd:cd08283   159 SDEKALFLSDILPTGYHAAELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLGAETINFEE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 241 DSDPAQSIIEQTaGHRGVDAVIDAVGFEAKGSTTETVLTN-LKLEGSSGKALRQCIAAVRRGGIVSVPGVYAGFIHGFLF 319
Cdd:cd08283   239 VDDVVEALRELT-GGRGPDVCIDAVGMEAHGSPLHKAEQAlLKLETDRPDALREAIQAVRKGGTVSIIGVYGGTVNKFPI 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08283     1 MKALVWHGKGDVRVEEVPDPKIEDPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGPEVRNLKVGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACENTNAGKGAAlnKKQIPAPAALFGYSHLYGGVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd08283    81 RVVVPFTIACGECFYCKRGLYSQCDNTNPSAEMA--KLYGHAGAGIFGYSHLTGGYAGGQAEYVRVPFADVGPFKIPDDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 161 SDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPINFDE 240
Cdd:cd08283   159 SDEKALFLSDILPTGYHAAELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLGAETINFEE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 241 DSDPAQSIIEQTaGHRGVDAVIDAVGFEAKGSTTETVLTN-LKLEGSSGKALRQCIAAVRRGGIVSVPGVYAGFIHGFLF 319
Cdd:cd08283   239 VDDVVEALRELT-GGRGPDVCIDAVGMEAHGSPLHKAEQAlLKLETDRPDALREAIQAVRKGGTVSIIGVYGGTVNKFPI 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:COG1063     1 MKALVLHGPGDLRLEEVPDP-EPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACENTNAgkgaalnkkqipapaalFGYSHlyggVPGGQAEYVRVPKGNVgpFKVPPLL 160
Cdd:COG1063    80 RVVVEPNIPCGECRYCRRGRYNLCENLQF-----------------LGIAG----RDGGFAEYVRVPAANL--VKVPDGL 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 161 SDDkALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGA-IPINFD 239
Cdd:COG1063   137 SDE-AAALVEPLAVALHAVERAGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELAR-ELGAdAVVNPR 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 240 EDsDPAQSIIEQTAGhRGVDAVIDAVGFEAkgsttetvltnlklegssgkALRQCIAAVRRGGIVSVPGVYAGFIhGFLF 319
Cdd:COG1063   215 EE-DLVEAVRELTGG-RGADVVIEAVGAPA--------------------ALEQALDLVRPGGTVVLVGVPGGPV-PIDL 271
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135   1 MKALTYHGPHH----VQVEnVPDPGVeqaDDIILRITATAICGSDLHLY--------RGKIPQVkhgdiFGHEFMGEVVE 68
Cdd:PRK05396    1 MKALVKLKAEPglwlTDVP-VPEPGP---NDVLIKVKKTAICGTDVHIYnwdewaqkTIPVPMV-----VGHEFVGEVVE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  69 TGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACENTnagKGAALNkkqipapaalfgyshlyggVPGGQAEYVRVPK 148
Cdd:PRK05396   72 VGSEVTGFKVGDRVSGEGHIVCGHCRNCRAGRRHLCRNT---KGVGVN-------------------RPGAFAEYLVIPA 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 149 GNVgpFKVPPLLSDDKALFLsDILPTAWQAAKNAQIQqGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAA 228
Cdd:PRK05396  130 FNV--WKIPDDIPDDLAAIF-DPFGNAVHTALSFDLV-GEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELAR 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 229 dRYGA-IPINFDEDsDPAQSIIEQTAGHrGVDavidaVGFEAKGsttetvltnlklegsSGKALRQCIAAVRRGGIVSVP 307
Cdd:PRK05396  206 -KMGAtRAVNVAKE-DLRDVMAELGMTE-GFD-----VGLEMSG---------------APSAFRQMLDNMNHGGRIAML 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 308 GVYAGFIhGFLFGDAFDKGLSFK------MGQThvhaWLgELLPLIEKGL-LKPeeIVTHYMPFEEAARGYEIFekREEE 380
Cdd:PRK05396  263 GIPPGDM-AIDWNKVIFKGLTIKgiygreMFET----WY-KMSALLQSGLdLSP--IITHRFPIDDFQKGFEAM--RSGQ 332

                  ....*...
gi 1352184135 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 1352184135  26 DDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACE 105
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYNLCP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1352184135 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 1352184135   8 GPHHVQVENVPDPGveqADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFV 87
Cdd:TIGR02822  13 GPLRFVERPVPRPG---PGELLVRVRACGVCRTDLHVSEGDLPVHRPRVTPGHEVVGEVAGRGADAGGFAVGDRVGIAWL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  88 -IACGDCFFCRLQQYAACENTNagkgaalnkkqipapaalfgyshlYGG--VPGGQAEYVRVPKGNVgpFKVPPLLSDDK 164
Cdd:TIGR02822  90 rRTCGVCRYCRRGAENLCPASR------------------------YTGwdTDGGYAEYTTVPAAFA--YRLPTGYDDVE 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135   41 DLHLYRGKIPqvkHGDIFGHEFMGEVVETGKDVKNLQKGDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqi 120
Cdd:smart00829  12 DVLIALGLYP---GEAVLGGECAGVVTRVGPGVTGLAVGDRVM------------------------------------- 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  121 papaalfgyshlyGGVPGGQAEYVRVPKGNVgpFKVPPLLSDDKALFLSDILPTAWQAAKN-AQIQQGSSVAVY-GAGPV 198
Cdd:smart00829  52 -------------GLAPGAFATRVVTDARLV--VPIPDGWSFEEAATVPVVFLTAYYALVDlARLRPGESVLIHaAAGGV 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  199 GLLTIACARLLGAEqIFVVDHHPYRLHFaADRYGaIPIN--FD-EDSDPAQSIIEQTAGhRGVDAVIDAVgfeakgstte 275
Cdd:smart00829 117 GQAAIQLARHLGAE-VFATAGSPEKRDF-LRALG-IPDDhiFSsRDLSFADEILRATGG-RGVDVVLNSL---------- 182
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  276 tvltnlklegsSGKALRQCIAAVRRGGIvsvpgvyagFI---------HGFLFGDAFDKGLSF------KM--GQTHVHA 338
Cdd:smart00829 183 -----------SGEFLDASLRCLAPGGR---------FVeigkrdirdNSQLAMAPFRPNVSYhavdldALeeGPDRIRE 242
                          330
                   ....*....|....*.
gi 1352184135  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 1352184135   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08283     1 MKALVWHGKGDVRVEEVPDPKIEDPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGPEVRNLKVGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACENTNAGKGAAlnKKQIPAPAALFGYSHLYGGVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd08283    81 RVVVPFTIACGECFYCKRGLYSQCDNTNPSAEMA--KLYGHAGAGIFGYSHLTGGYAGGQAEYVRVPFADVGPFKIPDDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 161 SDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPINFDE 240
Cdd:cd08283   159 SDEKALFLSDILPTGYHAAELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLGAETINFEE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 241 DSDPAQSIIEQTaGHRGVDAVIDAVGFEAKGSTTETVLTN-LKLEGSSGKALRQCIAAVRRGGIVSVPGVYAGFIHGFLF 319
Cdd:cd08283   239 VDDVVEALRELT-GGRGPDVCIDAVGMEAHGSPLHKAEQAlLKLETDRPDALREAIQAVRKGGTVSIIGVYGGTVNKFPI 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd05278     1 MKALVYLGPGKIGLEEVPDPKIQGPHDAIVRVTATSICGSDLHIYRGGVPGAKHGMILGHEFVGEVVEVGSDVKRLKPGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACENTNAGKGaalnkkqipapaalfgyshLYGGVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd05278    81 RVSVPCITFCGRCRFCRRGYHAHCENGLWGWK-------------------LGNRIDGGQAEYVRVPYADMNLAKIPDGL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 161 SDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPINFDE 240
Cdd:cd05278   142 PDEDALMLSDILPTGFHGAELAGIKPGSTVAVIGAGPVGLCAVAGARLLGAARIIAVDSNPERLDLAKEAGATDIINPKN 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 241 DsDPAQSIIEQTaGHRGVDAVIDAVGFEAkgsttetvltnlklegssgkALRQCIAAVRRGGIVSVPGVYAGFIHGFLFG 320
Cdd:cd05278   222 G-DIVEQILELT-GGRGVDCVIEAVGFEE--------------------TFEQAVKVVRPGGTIANVGVYGKPDPLPLLG 279
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:COG1063     1 MKALVLHGPGDLRLEEVPDP-EPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACENTNAgkgaalnkkqipapaalFGYSHlyggVPGGQAEYVRVPKGNVgpFKVPPLL 160
Cdd:COG1063    80 RVVVEPNIPCGECRYCRRGRYNLCENLQF-----------------LGIAG----RDGGFAEYVRVPAANL--VKVPDGL 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 161 SDDkALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGA-IPINFD 239
Cdd:COG1063   137 SDE-AAALVEPLAVALHAVERAGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELAR-ELGAdAVVNPR 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 240 EDsDPAQSIIEQTAGhRGVDAVIDAVGFEAkgsttetvltnlklegssgkALRQCIAAVRRGGIVSVPGVYAGFIhGFLF 319
Cdd:COG1063   215 EE-DLVEAVRELTGG-RGADVVIEAVGAPA--------------------ALEQALDLVRPGGTVVLVGVPGGPV-PIDL 271
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08284     1 MKAVVFKGPGDVRVEEVPIPQIQDPTDAIVKVTAAAICGSDLHIYRGHIP-STPGFVLGHEFVGEVVEVGPEVRTLKVGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACENTNagkgaalnkkqipapaaLFGYShLYGGVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd08284    80 RVVSPFTIACGECFYCRRGQSGRCAKGG-----------------LFGYA-GSPNLDGAQAEYVRVPFADGTLLKLPDGL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 161 SDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRyGAIPINFDE 240
Cdd:cd08284   142 SDEAALLLGDILPTGYFGAKRAQVRPGDTVAVIGCGPVGLCAVLSAQVLGAARVFAVDPVPERLERAAAL-GAEPINFED 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 241 DsDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVPGVYAGfiHGFLF- 319
Cdd:cd08284   221 A-EPVERVREATEG-RGADVVLEAVG--------------------GAAALDLAFDLVRPGGVISSVGVHTA--EEFPFp 276
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08282     1 MKAVVYGGPGNVAVEDVPDPKIEHPTDAIVRITTTAICGSDLHMYRGRTG-AEPGLVLGHEAMGEVEEVGSAVESLKVGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACENTNAGkgaalnkkqipAPAALFGYSHLyGGVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd08282    80 RVVVPFNVACGRCRNCKRGLTGVCLTVNPG-----------RAGGAYGYVDM-GPYGGGQAEYLRVPYADFNLLKLPDRD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 161 SDDKA---LFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGAIPIN 237
Cdd:cd08282   148 GAKEKddyLMLSDIFPTGWHGLELAGVQPGDTVAVFGAGPVGLMAAYSAILRGASRVYVVDHVPERLDLAE-SIGAIPID 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 238 FdEDSDPAQSIIEQTAGhrGVDAVIDAVGFEAkgsttetvlTNLKLEGSSGKALRQCIAAVRRGGIVSVPGVYAGF---- 313
Cdd:cd08282   227 F-SDGDPVEQILGLEPG--GVDRAVDCVGYEA---------RDRGGEAQPNLVLNQLIRVTRPGGGIGIVGVYVAEdpga 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 314 -----IHG---FLFGDAFDKGLSFKMGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKREEecRKVI 385
Cdd:cd08282   295 gdaaaKQGelsFDFGLLWAKGLSFGTGQAPVKKYNRQLRDLILAGRAKPSFVVSHVISLEDAPEAYARFDKRLE--TKVV 372

                  ...
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08286     1 MKALVYHGPGKISWEDRPKPTIQEPTDAIVKMLKTTICGTDLHILKGDVPTVTPGRILGHEGVGVVEEVGSAVTNFKVGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACENTnagkgaalnkkqipapAALFGYShlyggVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd08286    81 RVLISCISSCGTCGYCRKGLYSHCESG----------------GWILGNL-----IDGTQAEYVRIPHADNSLYKLPEGV 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 161 SDDKALFLSDILPTAWQ-AAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHfAADRYGAIPINFD 239
Cdd:cd08286   140 DEEAAVMLSDILPTGYEcGVLNGKVKPGDTVAIVGAGPVGLAALLTAQLYSPSKIIMVDLDDNRLE-VAKKLGATHTVNS 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 240 EDSDPAQSIIEQTAGhRGVDAVIDAVGFEAkgsTTETvltnlklegssgkalrqCIAAVRRGGIVSVPGVyagfiHG--- 316
Cdd:cd08286   219 AKGDAIEQVLELTDG-RGVDVVIEAVGIPA---TFEL-----------------CQELVAPGGHIANVGV-----HGkpv 272
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIfGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08287     1 MRATVIHGPGDIRVEEVPDPVIEEPTDAVIRVVATCVCGSDLWPYRGVSPTRAPAPI-GHEFVGVVEEVGSEVTSVKPGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkkqipapAALFGyshlyGGVPGGQAEYVRVPKGNVGPFKVPPLL 160
Cdd:cd08287    80 FVIAPFAISDGTCPFCRAGFTTSCVH-----------------GGFWG-----AFVDGGQGEYVRVPLADGTLVKVPGSP 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 161 SDDKALF-----LSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGAIP 235
Cdd:cd08287   138 SDDEDLLpsllaLSDVMGTGHHAAVSAGVRPGSTVVVVGDGAVGLCAVLAAKRLGAERIIAMSRHEDRQALAR-EFGATD 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 236 INFDEDSDPAQSIIEQTAGHrGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVPGVYAGFIh 315
Cdd:cd08287   217 IVAERGEEAVARVRELTGGV-GADAVLECVG--------------------TQESMEQAIAIARPGGRVGYVGVPHGGV- 274
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVkHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08236     1 MKALVLTGPGDLRYEDIPKP-EPGPGEVLVKVKACGICGSDIPRYLGTGAYH-PPLVLGHEFSGTVEEVGSGVDDLAVGD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACENTNagkgaalnkkqipapaaLFGySHLyggvPGGQAEYVRVPKGNVgpFKVPPLL 160
Cdd:cd08236    79 RVAVNPLLPCGKCEYCKKGEYSLCSNYD-----------------YIG-SRR----DGAFAEYVSVPARNL--IKIPDHV 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 161 SDDKALFLsDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADrYGAiPINFDE 240
Cdd:cd08236   135 DYEEAAMI-EPAAVALHAVRLAGITLGDTVVVIGAGTIGLLAIQWLKILGAKRVIAVDIDDEKLAVARE-LGA-DDTINP 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 241 DSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVsvpgVYAG------FI 314
Cdd:cd08236   212 KEEDVEKVRELTEG-RGADLVIEAAG--------------------SPATIEQALALARPGGKV----VLVGipygdvTL 266
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184135 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 1352184135   1 MKALTYHGPHH-VQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKG 79
Cdd:COG1064     1 MKAAVLTEPGGpLELEEVPRPEPG-PGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGVTGFKVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  80 DRVVIPFVIACGDCFFCR--LQQYaaCENtnagkgaalnkkqipapAALFGYSHlyggvPGGQAEYVRVPKGNVgpFKVP 157
Cdd:COG1064    80 DRVGVGWVDSCGTCEYCRsgRENL--CEN-----------------GRFTGYTT-----DGGYAEYVVVPARFL--VKLP 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 158 PLLSDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFA----ADRYGA 233
Cdd:COG1064   134 DGLDPAEAAPLLCAGITAYRALRRAGVGPGDRVAVIGAGGLGHLAVQIAKALGAE-VIAVDRSPEKLELArelgADHVVN 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 234 IpinfdEDSDPAQSIieqtAGHRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVPGVYAGF 313
Cdd:COG1064   213 S-----SDEDPVEAV----RELTGADVVIDTVG--------------------APATVNAALALLRRGGRLVLVGLPGGP 263
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYRGKiPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08234     1 MKALVYEGPGELEVEEVPVPEP-GPDEVLIKVAACGICGTDLHIYEGE-FGAAPPLVPGHEFAGVVVAVGSKVTGFKVGD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACENTNAgkgaalnkkqipapaalfgyshlYG-GVPGGQAEYVRVPKGNVgpFKVPPL 159
Cdd:cd08234    79 RVAVDPNIYCGECFYCRRGRPNLCENLTA-----------------------VGvTRNGGFAEYVVVPAKQV--YKIPDN 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 160 LSDDKALFLsDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPINFD 239
Cdd:cd08234   134 LSFEEAALA-EPLSCAVHGLDLLGIKPGDSVLVFGAGPIGLLLAQLLKLNGASRVTVAEPNEEKLELAKKLGATETVDPS 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 240 EDSDPAQSIIeqtaGHRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVPGVYAgfiHGFLF 319
Cdd:cd08234   213 REDPEAQKED----NPYGFDVVIEATG--------------------VPKTLEQAIEYARRGGTVLVFGVYA---PDARV 265
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPGVEQaDDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08235     1 MKAAVLHGPNDVRLEEVPVPEPGP-GEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGDGVTGFKVGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkkqipapaaLFGYSHLYggvPGGQAEYVRVPKGNV---GPFKVP 157
Cdd:cd08235    80 RVFVAPHVPCGECHYCLRGNENMCPN-------------------YKKFGNLY---DGGFAEYVRVPAWAVkrgGVLKLP 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 158 PLLSDDKALfLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPIN 237
Cdd:cd08235   138 DNVSFEEAA-LVEPLACCINAQRKAGIKPGDTVLVIGAGPIGLLHAMLAKASGARKVIVSDLNEFRLEFAKKLGADYTID 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 238 FDEDsDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSvpgVYAGFIHGF 317
Cdd:cd08235   217 AAEE-DLVEKVRELTDG-RGADVVIVATG--------------------SPEAQAQALELVRKGGRIL---FFGGLPKGS 271
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08261     1 MKALVCEKPGRLEVVDIPEPVPG-AGEVLVRVKRVGICGSDLHIYHGRNPFASYPRILGHELSGEVVEVGEGVAGLKVGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACENTNagkgaalnkkqipapaaLFGySHlyggVPGGQAEYVRVPKGNVgpfKVPPLL 160
Cdd:cd08261    80 RVVVDPYISCGECYACRKGRPNCCENLQ-----------------VLG-VH----RDGGFAEYIVVPADAL---LVPEGL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 161 SDDKALfLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGAIPINFDE 240
Cdd:cd08261   135 SLDQAA-LVEPLAIGAHAVRRAGVTAGDTVLVVGAGPIGLGVIQVAKARGAR-VIVVDIDDERLEFARELGADDTINVGD 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 241 DsDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVsvpgVYAGFIHGFLfg 320
Cdd:cd08261   213 E-DVAARLRELTDG-EGADVVIDATG--------------------NPASMEEAVELVAHGGRV----VLVGLSKGPV-- 264
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:cd08285     1 MKAFAMLGIGKVGWIEKPIP-VCGPNDAIVRPTAVAPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGSEVKDFKPGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCffcrlqqyaacentnagkgaalnkkqipaPAALFGYSHLYGGVPGG----------QAEYVRVPKGN 150
Cdd:cd08285    80 RVIVPAITPDWRS-----------------------------VAAQRGYPSQSGGMLGGwkfsnfkdgvFAEYFHVNDAD 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 151 VGPFKVPPLLSDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHfAADR 230
Cdd:cd08285   131 ANLAPLPDGLTDEQAVMLPDMMSTGFHGAELANIKLGDTVAVFGIGPVGLMAVAGARLRGAGRIIAVGSRPNRVE-LAKE 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 231 YGAIPI-NFDEdSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsTTETvltnlklegssgkaLRQCIAAVRRGGIVSVPGV 309
Cdd:cd08285   210 YGATDIvDYKN-GDVVEQILKLTGG-KGVDAVIIAGG------GQDT--------------FEQALKVLKPGGTISNVNY 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 310 YAGFIHGFLFGDAFDKGLSFKMGQTHV----HAWLGELLPLIEKGLLKPEE-IVTHYMPFEEAARGYEIFEKREEECRKV 384
Cdd:cd08285   268 YGEDDYLPIPREEWGVGMGHKTINGGLcpggRLRMERLASLIEYGRVDPSKlLTHHFFGFDDIEEALMLMKDKPDDLIKP 347

                  ....
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYRGK---IPQVKHGDI--------FGHEFMGEVVET 69
Cdd:cd08233     1 MKAARYHGRKDIRVEEVPEPPV-KPGEVKIKVAWCGICGSDLHEYLDGpifIPTEGHPHLtgetapvtLGHEFSGVVVEV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  70 GKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkkqipapaalFGYSHLyGGVPGGQAEYVRVPKG 149
Cdd:cd08233    80 GSGVTGFKVGDRVVVEPTIKCGTCGACKRGLYNLCDS--------------------LGFIGL-GGGGGGFAEYVVVPAY 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 150 NVgpFKVPPLLSDDKALfLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAD 229
Cdd:cd08233   139 HV--HKLPDNVPLEEAA-LVEPLAVAWHAVRRSGFKPGDTALVLGAGPIGLLTILALKAAGASKIIVSEPSEARRELAEE 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 230 RYGAIPINFDEDsDPAQSIIEQTAGhRGVDAVIDAVGFEAkgsttetvltnlklegssgkALRQCIAAVRRGGIVSVPGV 309
Cdd:cd08233   216 LGATIVLDPTEV-DVVAEVRKLTGG-GGVDVSFDCAGVQA--------------------TLDTAIDALRPRGTAVNVAI 273
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135  27 DIILRITATAICGSDLHLYRGK-IPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRlqqyaace 105
Cdd:cd05188     1 EVLVRVEAAGLCGTDLHIRRGGyPPPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNLGCGTCELCR-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 106 ntnagkgaalnkkqipapAALFGYSHLYGGVPGGQAEYVRVPKGNVgpFKVPPLLSDDKALFLSDILPTAWQAAKNA-QI 184
Cdd:cd05188    73 ------------------ELCPGGGILGEGLDGGFAEYVVVPADNL--VPLPDGLSLEEAALLPEPLATAYHALRRAgVL 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 185 QQGSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGAIPINFDEDSDPAQsiiEQTAGHRGVDAVIDA 264
Cdd:cd05188   133 KPGDTVLVLGAGGVGLLAAQLAKAAGAR-VIVTDRSDEKLELAKELGADHVIDYKEEDLEEE---LRLTGGGGADVVIDA 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIF-GHEFMGEVVETGKDVKNLQKG 79
Cdd:cd08239     1 MRGAVFPGDRTVELREFPVP-VPGPGEVLLRVKASGLCGSDLHYYYHGHRAPAYQGVIpGHEPAGVVVAVGPGVTHFRVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  80 DRVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkkqipaPAALFGYSHlyggvPGGQAEYVRVPKGNVgpFKVPPL 159
Cdd:cd08239    80 DRVMVYHYVGCGACRNCRRGWMQLCTS----------------KRAAYGWNR-----DGGHAEYMLVPEKTL--IPLPDD 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 160 LSDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADrYGAIPInFD 239
Cdd:cd08239   137 LSFADGALLLCGIGTAYHALRRVGVSGRDTVLVVGAGPVGLGALMLARALGAEDVIGVDPSPERLELAKA-LGADFV-IN 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 240 EDSDPAQSIIEQTAGhRGVDAVIDAVGFEAkgsttetvltnlklegssgkALRQCIAAVRRGGIVSVPGVYAGFihgflf 319
Cdd:cd08239   215 SGQDDVQEIRELTSG-AGADVAIECSGNTA--------------------ARRLALEAVRPWGRLVLVGEGGEL------ 267
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184135 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 1352184135   1 MKAL--TYHGPHHVQVE-NVPDPGveqADDIILRITATAICGSDLHLY--------RGKIPQvkhgdIFGHEFMGEVVET 69
Cdd:cd05281     1 MKAIvkTKAGPGAELVEvPVPKPG---PGEVLIKVLAASICGTDVHIYewdewaqsRIKPPL-----IFGHEFAGEVVEV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  70 GKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACENTnagkgaalnkKQIpapaalfgyshlygGV--PGGQAEYVRVP 147
Cdd:cd05281    73 GEGVTRVKVGDYVSAETHIVCGKCYQCRTGNYHVCQNT----------KIL--------------GVdtDGCFAEYVVVP 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 148 KGNVgpFKVPPLLSDDKALfLSDILPTAWQAAKNAQIQqGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFA 227
Cdd:cd05281   129 EENL--WKNDKDIPPEIAS-IQEPLGNAVHTVLAGDVS-GKSVLITGCGPIGLMAIAVAKAAGASLVIASDPNPYRLELA 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 228 ADRYGAIPINFDEDsDPAQsIIEQTAGHrGVDAVIDAVGFEakgsttetvltnlklegssgKALRQCIAAVRRGGIVSVP 307
Cdd:cd05281   205 KKMGADVVINPREE-DVVE-VKSVTDGT-GVDVVLEMSGNP--------------------KAIEQGLKALTPGGRVSIL 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 308 GVYAGFIHGFLFGDAFDKGLSF------KMGQT--HVHAWLgellpliEKGLLKPEEIVTHYMPFEEAARGYEIFekREE 379
Cdd:cd05281   262 GLPPGPVDIDLNNLVIFKGLTVqgitgrKMFETwyQVSALL-------KSGKVDLSPVITHKLPLEDFEEAFELM--RSG 332

                  ....*....
gi 1352184135 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 1352184135   3 ALTYHGPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYR-GKI--PQVKHGDIFGHEFMGEVVETGKDVKNLQKG 79
Cdd:cd05285     1 AAVLHGPGDLRLEERPIPEP-GPGEVLVRVRAVGICGSDVHYYKhGRIgdFVVKEPMVLGHESAGTVVAVGSGVTHLKVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  80 DRVVIPFVIACGDCFFCRLQQYAACENtnaGKGAAlnkkqipAPaalfgyshlygGVPGGQAEYVRVPKGNVgpFKVPPL 159
Cdd:cd05285    80 DRVAIEPGVPCRTCEFCKSGRYNLCPD---MRFAA-------TP-----------PVDGTLCRYVNHPADFC--HKLPDN 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 160 LSDDK-ALF--LSdilpTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGA--- 233
Cdd:cd05285   137 VSLEEgALVepLS----VGVHACRRAGVRPGDTVLVFGAGPIGLLTAAVAKAFGATKVVVTDIDPSRLEFAK-ELGAtht 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 234 IPINFDEDSDPAQSIIEQTAGhRGVDAVIDAVGFEakgsttetvltnlklegssgKALRQCIAAVRRGGIVSVPGVYAGF 313
Cdd:cd05285   212 VNVRTEDTPESAEKIAELLGG-KGPDVVIECTGAE--------------------SCIQTAIYATRPGGTVVLVGMGKPE 270
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184135 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 1352184135   1 MKALTYHGPHHV-QVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKG 79
Cdd:cd08260     1 MRAAVYEEFGEPlEIREVPDPEPP-PDGVVVEVEACGVCRSDWHGWQGHDPDVTLPHVPGHEFAGVVVEVGEDVSRWRVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  80 DRVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkKQIPapaalfGYSHlyggvPGGQAEYVRVPKGNVGPFKVPPL 159
Cdd:cd08260    80 DRVTVPFVLGCGTCPYCRAGDSNVCEH-----------QVQP------GFTH-----PGSFAEYVAVPRADVNLVRLPDD 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 160 LSDDKALFLSDILPTAWQA-AKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAeQIFVVDHHPYRLHFaADRYGAIP-IN 237
Cdd:cd08260   138 VDFVTAAGLGCRFATAFRAlVHQARVKPGEWVAVHGCGGVGLSAVMIASALGA-RVIAVDIDDDKLEL-ARELGAVAtVN 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 238 FDEDSDPAQSIIEQTAGhrGVDAVIDAVGFEAkgsttetvltnlklegssgkALRQCIAAVRRGG-IVSVpgvyagfihG 316
Cdd:cd08260   216 ASEVEDVAAAVRDLTGG--GAHVSVDALGIPE--------------------TCRNSVASLRKRGrHVQV---------G 264
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRG---------KIPQVKHGDIFGHEFMGEVVETGK 71
Cdd:cd08256     1 MRAVVCHGPQDYRLEEVPVP-RPGPGEILVKVEACGICAGDIKCYHGapsfwgdenQPPYVKPPMIPGHEFVGRVVELGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  72 DVKN--LQKGDRVVIPFVIACGDCFFCRLQQYAACENTNagkgaalnkkqipapaaLFGYSHlygGVPGGQAEYVRVPKG 149
Cdd:cd08256    80 GAEErgVKVGDRVISEQIVPCWNCRFCNRGQYWMCQKHD-----------------LYGFQN---NVNGGMAEYMRFPKE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 150 NVGpFKVPPLLSDDKALFLsDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAd 229
Cdd:cd08256   140 AIV-HKVPDDIPPEDAILI-EPLACALHAVDRANIKFDDVVVLAGAGPLGLGMIGAARLKNPKKLIVLDLKDERLALAR- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 230 RYGA-IPINFDEDSDPAQsIIEQTAGHrGVDAVIDAVGFEakgsttetvltnlklegssgKALRQCIAAVRRGGIvsvpg 308
Cdd:cd08256   217 KFGAdVVLNPPEVDVVEK-IKELTGGY-GCDIYIEATGHP--------------------SAVEQGLNMIRKLGR----- 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 309 vyagFIHGFLFGDAF---------DKGLSFkMGqTHVHAWLGEL-LPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKRE 378
Cdd:cd08256   270 ----FVEFSVFGDPVtvdwsiigdRKELDV-LG-SHLGPYCYPIaIDLIASGRLPTDGIVTHQFPLEDFEEAFELMARGD 343

                  ....*...
gi 1352184135 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 1352184135  13 QVENV--PDPGveqADDIILRITATAICGSDLHLYRGKIPQVKHGdIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIAC 90
Cdd:COG1062     5 EIEEVelDEPR---PGEVLVRIVAAGLCHSDLHVRDGDLPVPLPA-VLGHEGAGVVEEVGPGVTGVAPGDHVVLSFIPSC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  91 GDCFFCRLQQYAACENtnagkGAALNKK--QIPAPAALfgysHLYGGVP-------GGQAEYVRVPKGNVgpFKVPPLLS 161
Cdd:COG1062    81 GHCRYCASGRPALCEA-----GAALNGKgtLPDGTSRL----SSADGEPvghffgqSSFAEYAVVPERSV--VKVDKDVP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 162 DDKALFLSDILPTAWQAAKN-AQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGAIP-INfD 239
Cdd:COG1062   150 LELAALLGCGVQTGAGAVLNtAKVRPGDTVAVFGLGGVGLSAVQGARIAGASRIIAVDPVPEKLELAR-ELGATHtVN-P 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 240 EDSDPAQSIIEQTAGhrGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGG---IVSVPGVYAGF-IH 315
Cdd:COG1062   228 ADEDAVEAVRELTGG--GVDYAFETTG--------------------NPAVIRQALEALRKGGtvvVVGLAPPGAEIsLD 285
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135   1 MKALTYHGPHH-VQVENV--PDPGveqADDIILRITATAICGSDLHLYRGKIPQVKHGdIFGHEFMGEVVETGKDVKNLQ 77
Cdd:cd08279     1 MRAAVLHEVGKpLEIEEVelDDPG---PGEVLVRIAAAGLCHSDLHVVTGDLPAPLPA-VLGHEGAGVVEEVGPGVTGVK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  78 KGDRVVIPFVIACGDCFFCRLQQYAACENtnagkGAALNKKQIPAPAalfgYSHLYGGVPGGQ-------AEYVRVPKGN 150
Cdd:cd08279    77 PGDHVVLSWIPACGTCRYCSRGQPNLCDL-----GAGILGGQLPDGT----RRFTADGEPVGAmcglgtfAEYTVVPEAS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 151 VGpfKVPPLLSDDKALFLSDILPTAWQAAKN-AQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAd 229
Cdd:cd08279   148 VV--KIDDDIPLDRAALLGCGVTTGVGAVVNtARVRPGDTVAVIGCGGVGLNAIQGARIAGASRIIAVDPVPEKLELAR- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 230 RYGAIPINFDEDSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsTTETVltnlklegssgkalRQCIAAVRRGG---IVSV 306
Cdd:cd08279   225 RFGATHTVNASEDDAVEAVRDLTDG-RGADYAFEAVG------RAATI--------------RQALAMTRKGGtavVVGM 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 307 PGVYAGF-IHGFLFGdAFDKGL-SFKMGQTHVHAWLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFeKREEECRKV 384
Cdd:cd08279   284 GPPGETVsLPALELF-LSEKRLqGSLYGSANPRRDIPRLLDLYRAGRLKLDELVTRRYSLDEINEAFADM-LAGENARGV 361

                  ..
gi 1352184135 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 1352184135   2 KALTYHGPHH-VQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKN----- 75
Cdd:cd08231     2 RAAVLTGPGKpLEIREVPLPDLE-PGAVLVRVRLAGVCGSDVHTVAGRRPRVPLPIILGHEGVGRVVALGGGVTTdvage 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  76 -LQKGDRVVIPFVIACGDCFFCRLQQYAACEN-TNAGkgaalnkkqipaPAALFGYSHLYGGVpggqAEYVRVPKGnVGP 153
Cdd:cd08231    81 pLKVGDRVTWSVGAPCGRCYRCLVGDPTKCENrKKYG------------HEASCDDPHLSGGY----AEHIYLPPG-TAI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 154 FKVPPLLSDDKALFLSDILPTAWQAAKNAQIQQ-GSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYG 232
Cdd:cd08231   144 VRVPDNVPDEVAAPANCALATVLAALDRAGPVGaGDTVVVQGAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAR-EFG 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 233 AIP-INFDEDSDP-AQSIIEQTAGHRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVPGVY 310
Cdd:cd08231   223 ADAtIDIDELPDPqRRAIVRDITGGRGADVVIEASG--------------------HPAAVPEGLELLRRGGTYVLVGSV 282

                  ..
gi 1352184135 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 1352184135   1 MKALTYHGPHH-VQVENVPDPGvEQADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKN---L 76
Cdd:cd08263     1 MKAAVLKGPNPpLTIEEIPVPR-PKEGEILIRVAACGVCHSDLHVLKGELP-FPPPFVLGHEISGEVVEVGPNVENpygL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  77 QKGDRVVIPFVIACGDCFFCRLQQYAACEN---TNAGKGAALNkkqipAPAALFG--YSHLYGGVPGGQAEYVRVPKGNV 151
Cdd:cd08263    79 SVGDRVVGSFIMPCGKCRYCARGKENLCEDffaYNRLKGTLYD-----GTTRLFRldGGPVYMYSMGGLAEYAVVPATAL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 152 gpFKVPPLLSDDKALFLSDILPTAWQAAKNAQIQQ-GSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdR 230
Cdd:cd08263   154 --APLPESLDYTESAVLGCAGFTAYGALKHAADVRpGETVAVIGVGGVGSSAIQLAKAFGASPIIAVDVRDEKLAKAK-E 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 231 YGAIPINFDEDSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsTTETVLTNLKLEGSSGKALRQCIAA------------V 298
Cdd:cd08263   231 LGATHTVNAAKEDAVAAIREITGG-RGVDVVVEALG------KPETFKLALDVVRDGGRAVVVGLAPggataeipitrlV 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 299 RRGgiVSVPGVYAgfihgflfgdafdkglsfkmGQTHVHawLGELLPLIEKGLLKPEEIVTHYMPFEEAARGYEIFEKRE 378
Cdd:cd08263   304 RRG--IKIIGSYG--------------------ARPRQD--LPELVGLAASGKLDPEALVTHKYKLEEINEAYENLRKGL 359

                  ....*...
gi 1352184135 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 1352184135   1 MKALTYHGPHH----VQVEnVPDPGVeqaDDIILRITATAICGSDLHLY--------RGKIPQVkhgdiFGHEFMGEVVE 68
Cdd:PRK05396    1 MKALVKLKAEPglwlTDVP-VPEPGP---NDVLIKVKKTAICGTDVHIYnwdewaqkTIPVPMV-----VGHEFVGEVVE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  69 TGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACENTnagKGAALNkkqipapaalfgyshlyggVPGGQAEYVRVPK 148
Cdd:PRK05396   72 VGSEVTGFKVGDRVSGEGHIVCGHCRNCRAGRRHLCRNT---KGVGVN-------------------RPGAFAEYLVIPA 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 149 GNVgpFKVPPLLSDDKALFLsDILPTAWQAAKNAQIQqGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAA 228
Cdd:PRK05396  130 FNV--WKIPDDIPDDLAAIF-DPFGNAVHTALSFDLV-GEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELAR 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 229 dRYGA-IPINFDEDsDPAQSIIEQTAGHrGVDavidaVGFEAKGsttetvltnlklegsSGKALRQCIAAVRRGGIVSVP 307
Cdd:PRK05396  206 -KMGAtRAVNVAKE-DLRDVMAELGMTE-GFD-----VGLEMSG---------------APSAFRQMLDNMNHGGRIAML 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 308 GVYAGFIhGFLFGDAFDKGLSFK------MGQThvhaWLgELLPLIEKGL-LKPeeIVTHYMPFEEAARGYEIFekREEE 380
Cdd:PRK05396  263 GIPPGDM-AIDWNKVIFKGLTIKgiygreMFET----WY-KMSALLQSGLdLSP--IITHRFPIDDFQKGFEAM--RSGQ 332

                  ....*...
gi 1352184135 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 1352184135   1 MKAL--TYHGPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQK 78
Cdd:cd08258     1 MKALvkTGPGPGNVELREVPEPEP-GPGEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEVGPDVEGWKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  79 GDRVVI-PFVIACGDCFFCRLQQYAACEntnagkgaalNKKqipapaaLFGYshlygGVPGGQAEYVRVPKGNVgpFKVP 157
Cdd:cd08258    80 GDRVVSeTTFSTCGRCPYCRRGDYNLCP----------HRK-------GIGT-----QADGGFAEYVLVPEESL--HELP 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 158 PLLSDDKALfLSDILPTAWQA-AKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFV-VDHHPYRLHfAADRYGAIP 235
Cdd:cd08258   136 ENLSLEAAA-LTEPLAVAVHAvAERSGIRPGDTVVVFGPGPIGLLAAQVAKLQGATVVVVgTEKDEVRLD-VAKELGADA 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184135 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 1352184135   1 MKALTYHGPH--HVQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPQVKHGDI-FGHEFMGEVVETGKDVKNLQ 77
Cdd:cd08254     1 MKAWRFHKGSkgLLVLEEVPVPEPG-PGEVLVKVKAAGVCHSDLHILDGGVPTLTKLPLtLGHEIAGTVVEVGAGVTNFK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  78 KGDRVVIPFVIACGDCFFCRLQQYAACENTnagkgaalnkkqipapaalfgySHLYGGVPGGQAEYVRVPKGNVGPfkVP 157
Cdd:cd08254    80 VGDRVAVPAVIPCGACALCRRGRGNLCLNQ----------------------GMPGLGIDGGFAEYIVVPARALVP--VP 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 158 PLLSDDKALFLSDILPTAWQAAKNA-QIQQGSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAAdRYGAIPi 236
Cdd:cd08254   136 DGVPFAQAAVATDAVLTPYHAVVRAgEVKPGETVLVIGLGGLGLNAVQIAKAMGAA-VIAVDIKEEKLELAK-ELGADE- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 237 nFDEDSDPAQSIIEQTAGHRGVDAVIDAVGFeakGSTTEtvltnlklegssgkalrQCIAAVRRGGIVSVPGVYAG--FI 314
Cdd:cd08254   213 -VLNSLDDSPKDKKAAGLGGGFDVIFDFVGT---QPTFE-----------------DAQKAVKPGGRIVVVGLGRDklTV 271
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184135 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 1352184135   1 MKALTYHGPHH-VQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKG 79
Cdd:cd08259     1 MKAAILHKPNKpLQIEEVPDP-EPGPGEVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVGEGVERFKPG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  80 DRVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkkqipapAALFGYShlyggVPGGQAEYVRVPKGNVgpFKVPPL 159
Cdd:cd08259    80 DRVILYYYIPCGKCEYCLSGEENLCRN-----------------RAEYGEE-----VDGGFAEYVKVPERSL--VKLPDN 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 160 LSDDKALFLSDILPTAWQAAKNAQIQQGSSVAV-YGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGAIPINF 238
Cdd:cd08259   136 VSDESAALAACVVGTAVHALKRAGVKKGDTVLVtGAGGGVGIHAIQLAKALGAR-VIAVTRSPEKLKILKELGADYVIDG 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 239 DEDSDPAQSIIeqtaghrGVDAVIDAVgfeakGSTTetvltnlkLEGSsgkaLRqciaAVRRGGIVSVPGVYAGFIHGFL 318
Cdd:cd08259   215 SKFSEDVKKLG-------GADVVIELV-----GSPT--------IEES----LR----SLNKGGRLVLIGNVTPDPAPLR 266
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135  26 DDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACE 105
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYNLCP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1352184135 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 1352184135   1 MKALTYHGPHH-VQVENVPDPGVEQaDDIILRITATAICGSDLHLYRGkiPQVKHGD-----IFGHEFMGEVVETGKDVK 74
Cdd:cd05284     1 MKAARLYEYGKpLRLEDVPVPEPGP-GQVLVRVGGAGVCHSDLHVIDG--VWGGILPyklpfTLGHENAGWVEEVGSGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  75 NLQKGDRVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkkqiPAPAALfgyshlygGVPGGQAEYVRVPKGNVgpF 154
Cdd:cd05284    78 GLKEGDPVVVHPPWGCGTCRYCRRGEENYCEN--------------ARFPGI--------GTDGGFAEYLLVPSRRL--V 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 155 KVPPLLSDDKALFLSDILPTAWQAAKNA--QIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYG 232
Cdd:cd05284   134 KLPRGLDPVEAAPLADAGLTAYHAVKKAlpYLDPGSTVVVIGVGGLGHIAVQILRALTPATVIAVDRSEEALKLAE-RLG 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 233 AiPINFDEDSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVPGvYAG 312
Cdd:cd05284   213 A-DHVLNASDDVVEEVRELTGG-RGADAVIDFVG--------------------SDETLALAAKLLAKGGRYVIVG-YGG 269
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184135 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 1352184135   7 HGPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYR-GKI--PQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVV 83
Cdd:cd08232     4 HAAGDLRVEERPAPEP-GPGEVRVRVAAGGICGSDLHYYQhGGFgtVRLREPMVLGHEVSGVVEAVGPGVTGLAPGQRVA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  84 IPFVIACGDCFFCRLQQYAACENTNagkgaalnkkqipapaaLFGYSHLYGGVPGGQAEYVRVPKGNVgpFKVPPLLSDD 163
Cdd:cd08232    83 VNPSRPCGTCDYCRAGRPNLCLNMR-----------------FLGSAMRFPHVQGGFREYLVVDASQC--VPLPDGLSLR 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 164 KALFlSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGAipinfDEDSD 243
Cdd:cd08232   144 RAAL-AEPLAVALHAVNRAGDLAGKRVLVTGAGPIGALVVAAARRAGAAEIVATDLADAPLAVAR-AMGA-----DETVN 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 244 PAQSIIEQTAGHRG-VDavidaVGFEAKGSTtetvltnlklegssgKALRQCIAAVRRGGIVSVPGVYAGFIhGFLFGDA 322
Cdd:cd08232   217 LARDPLAAYAADKGdFD-----VVFEASGAP---------------AALASALRVVRPGGTVVQVGMLGGPV-PLPLNAL 275
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1352184135 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 1352184135   1 MKALTYH--GPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIP-QVKHGDIFGHEFMGEVVETGKDVKNLQ 77
Cdd:cd08297     1 MKAAVVEefGEKPYEVKDVPVP-EPGPGEVLVKLEASGVCHTDLHAALGDWPvKPKLPLIGGHEGAGVVVAVGPGVSGLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  78 KGDRVVIPFVI-ACGDCFFCRLQQYAACENtnagkgaalnkkqipapAALFGYShlyggVPGGQAEYVRVPKGNVGPfkV 156
Cdd:cd08297    80 VGDRVGVKWLYdACGKCEYCRTGDETLCPN-----------------QKNSGYT-----VDGTFAEYAIADARYVTP--I 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 157 PPLLSDDKA--LFLSDIlpTAWQAAKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAeQIFVVDHHPYRLHFA----AD 229
Cdd:cd08297   136 PDGLSFEQAapLLCAGV--TVYKALKKAGLKPGDWVVISGAgGGLGHLGVQYAKAMGL-RVIAIDVGDEKLELAkelgAD 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 230 RYgaipINFDEdSDPAQSIIEQTAGhRGVDAVIdavgfeakgsttetVLTnlklegSSGKALRQCIAAVRRGGIVSVPGV 309
Cdd:cd08297   213 AF----VDFKK-SDDVEAVKELTGG-GGAHAVV--------------VTA------VSAAAYEQALDYLRPGGTLVCVGL 266
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPGvEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGD 80
Cdd:PRK10083    1 MKSIVIEKPNSLAIEERPIPQ-PAAGEVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGEGVDAARIGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACEntnagkgaalnkkqipapaalfgySHLYGGV--PGGQAEYVRVPKGNVgpFKVPP 158
Cdd:PRK10083   80 RVAVDPVISCGHCYPCSIGKPNVCT------------------------SLVVLGVhrDGGFSEYAVVPAKNA--HRIPD 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 159 LLSDDKALFLsDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTI-ACARLLGAEQIFVVDHHPYRLHFAAdRYGAipin 237
Cdd:PRK10083  134 AIADQYAVMV-EPFTIAANVTGRTGPTEQDVALIYGAGPVGLTIVqVLKGVYNVKAVIVADRIDERLALAK-ESGA---- 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 238 fDEDSDPAQSIIEQTAGHRGVDA--VIDAVGFEAkgsttetvltnlKLEgssgKALRQCIAAVRRG--GIVSVPG--VYA 311
Cdd:PRK10083  208 -DWVINNAQEPLGEALEEKGIKPtlIIDAACHPS------------ILE----EAVTLASPAARIVlmGFSSEPSeiVQQ 270
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184135 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 1352184135   1 MKALTYH---GPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIP-QVKHGDIFGHEFMGEVVETGKDVKNL 76
Cdd:COG0604     1 MKAIVITefgGPEVLELEEVPVP-EPGPGEVLVRVKAAGVNPADLLIRRGLYPlPPGLPFIPGSDAAGVVVAVGEGVTGF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  77 QKGDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalfgyshlYGGVPGGQAEYVRVPKGNVGPfkV 156
Cdd:COG0604    80 KVGDRVA-------------------------------------------------GLGRGGGYAEYVVVPADQLVP--L 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 157 PPLLSDDKA--LFLSdiLPTAWQA-AKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVV---DHHPYRLHFAAD 229
Cdd:COG0604   109 PDGLSFEEAaaLPLA--GLTAWQAlFDRGRLKPGETVLVHGAaGGVGSAAVQLAKALGARVIATAsspEKAELLRALGAD 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 230 RygaiPINFDEDsDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRRGGIVSVPGV 309
Cdd:COG0604   187 H----VIDYREE-DFAERVRALTGG-RGVDVVLDTVG---------------------GDTLARSLRALAPGGRLVSIGA 239
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 310 YAGFIHGFLFGDAFDKGLS------FKMGQTHVHAWLGELLPLIEKGLLKPeeIVTHYMPFEEAARGYEIFEKREEecR- 382
Cdd:COG0604   240 ASGAPPPLDLAPLLLKGLTltgftlFARDPAERRAALAELARLLAAGKLRP--VIDRVFPLEEAAEAHRLLESGKH--Rg 315

                  ....*..
gi 1352184135 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 1352184135   1 MKALTYH---GPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYRGkIPQVKH--GDIFGHEFMGEVVETGKDVKN 75
Cdd:cd08266     1 MKAVVIRghgGPEVLEYGDLPEPEP-GPDEVLVRVKAAALNHLDLWVRRG-MPGIKLplPHILGSDGAGVVEAVGPGVTN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  76 LQKGDRVVIPFVIACGDCFFCRlqqyaacentnAGKGAALNKKQIpapaalFGYshlygGVPGGQAEYVRVPKGNVgpFK 155
Cdd:cd08266    79 VKPGQRVVIYPGISCGRCEYCL-----------AGRENLCAQYGI------LGE-----HVDGGYAEYVAVPARNL--LP 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 156 VPPLLSDDKALFLSDILPTAWQA-AKNAQIQQGSSVAVYGAGP-VGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGA 233
Cdd:cd08266   135 IPDNLSFEEAAAAPLTFLTAWHMlVTRARLRPGETVLVHGAGSgVGSAAIQIAKLFGAT-VIATAGSEDKLERAKELGAD 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 234 IPINFDEDSDPAqSIIEQTAGhRGVDAVIDAVGfeakGSTTETVLTNLKlegssgkalrqciaavRRGGIVSVpGVYAGF 313
Cdd:cd08266   214 YVIDYRKEDFVR-EVRELTGK-RGVDVVVEHVG----AATWEKSLKSLA----------------RGGRLVTC-GATTGY 270
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184135 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 1352184135  24 QADDIILRITATAICGSDLHLYRGKiPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAA 103
Cdd:cd08277    26 KANEVRIKMLATSVCHTDILAIEGF-KATLFPVILGHEGAGIVESVGEGVTNLKPGDKVIPLFIGQCGECSNCRSGKTNL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 104 CENTNAGKGAALNKKQipAPAALFGYS-HLYGGVpGGQAEYVRVPKGNVGpfKVPPLLSDDKALFLSDILPTAWQAA-KN 181
Cdd:cd08277   105 CQKYRANESGLMPDGT--SRFTCKGKKiYHFLGT-STFSQYTVVDENYVA--KIDPAAPLEHVCLLGCGFSTGYGAAwNT 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 182 AQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHfAADRYGAIPINFDEDSD--PAQSIIEQTAGhrGVD 259
Cdd:cd08277   180 AKVEPGSTVAVFGLGAVGLSAIMGAKIAGASRIIGVDINEDKFE-KAKEFGATDFINPKDSDkpVSEVIREMTGG--GVD 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 260 AVIDAVGfeakgsttetvltNLKLegssgkaLRQCIAAVRRGG----IVSVPGVYAGFIHGFLFGDAFD-KGlsFKMGQT 334
Cdd:cd08277   257 YSFECTG-------------NADL-------MNEALESTKLGWgvsvVVGVPPGAELSIRPFQLILGRTwKG--SFFGGF 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1352184135 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 1352184135  57 IFGHEFMGEVVETGKDVKNLQKGDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalfgyshlyggV 136
Cdd:cd08255    23 PPGYSSVGRVVEVGSGVTGFKPGDRVF----------------------------------------------------C 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 137 PGGQAEYVRVPKGNVgpFKVPPLLSDDKALFLsDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFV 216
Cdd:cd08255    51 FGPHAERVVVPANLL--VPLPDGLPPERAALT-ALAATALNGVRDAEPRLGERVAVVGLGLVGLLAAQLAKAAGAREVVG 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 217 VDHHPYRLHFAAdRYGAIpinfdedsDPAQSIIEQTAGHRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIA 296
Cdd:cd08255   128 VDPDAARRELAE-ALGPA--------DPVAADTADEIGGRGADVVIEASG--------------------SPSALETALR 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 297 AVRRGGIVSVPGVYAGFihGFLFGDAFD-KGLSFKMGQT-----------HVHAW-LGELLPLIEKGllKPEEIVTHYMP 363
Cdd:cd08255   179 LLRDRGRVVLVGWYGLK--PLLLGEEFHfKRLPIRSSQVygigrydrprrWTEARnLEEALDLLAEG--RLEALITHRVP 254
                         330       340
                  ....*....|....*....|...
gi 1352184135 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 1352184135   1 MKALTYHGpHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYR-----------GKIPQVKHGDIFGHEFMGEVVET 69
Cdd:cd08262     1 MRAAVFRD-GPLVVRDVPDP-EPGPGQVLVKVLACGICGSDLHATAhpeamvddaggPSLMDLGADIVLGHEFCGEVVDY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  70 GKDVKN-LQKGDRVV-IPFVIaCGDCFFCRLqqyaacentnagkgaalnkkqipapaalfGYShlyGGVPGGQAEYVRVP 147
Cdd:cd08262    79 GPGTERkLKVGTRVTsLPLLL-CGQGASCGI-----------------------------GLS---PEAPGGYAEYMLLS 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 148 KGNVgpFKVPPLLSDDKALfLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFA 227
Cdd:cd08262   126 EALL--LRVPDGLSMEDAA-LTEPLAVGLHAVRRARLTPGEVALVIGCGPIGLAVIAALKARGVGPIVASDFSPERRALA 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 228 AdRYGA-IPINFDEDSDPAQSIIEQTAGHRGVDAVIdavgFEAKGSTTetvltnlklegssgkALRQCIAAVRRGGIVSV 306
Cdd:cd08262   203 L-AMGAdIVVDPAADSPFAAWAAELARAGGPKPAVI----FECVGAPG---------------LIQQIIEGAPPGGRIVV 262
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184135 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 1352184135   1 MKALTYHGPHHV-----QVENVPDPGVEQaDDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKN 75
Cdd:cd08298     1 MKAMVLEKPGPIeenplRLTEVPVPEPGP-GEVLIKVEACGVCRTDLHIVEGDLPPPKLPLIPGHEIVGRVEAVGPGVTR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  76 LQKGDRV-VIPFVIACGDCFFCRLQQYAACentnagkgaalnkkqipaPAALF-GYShlyggVPGGQAEYVRVPKGNVgp 153
Cdd:cd08298    80 FSVGDRVgVPWLGSTCGECRYCRSGRENLC------------------DNARFtGYT-----VDGGYAEYMVADERFA-- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 154 FKVPPLLSDDKA--LFLSDIlpTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFA---- 227
Cdd:cd08298   135 YPIPEDYDDEEAapLLCAGI--IGYRALKLAGLKPGQRLGLYGFGASAHLALQIARYQGAE-VFAFTRSGEHQELArelg 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 228 ADRYGaipinfDEDSDPAQSIieqtaghrgvDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGGIVSVP 307
Cdd:cd08298   212 ADWAG------DSDDLPPEPL----------DAAIIFAP--------------------VGALVPAALRAVKKGGRVVLA 255
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184135 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 1352184135   8 GPHHVQVENVPDPGVEQADdIILRITATAICGSDLH-LYRGKIPQVKHGD--IFGHEFMGEVVETGKDVKNLQKGDRVVi 84
Cdd:cd08269     3 GPGRFEVEEHPRPTPGPGQ-VLVRVEGCGVCGSDLPaFNQGRPWFVYPAEpgGPGHEGWGRVVALGPGVRGLAVGDRVA- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  85 pfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalfgyshlyGGVPGGQAEYVRVPKGNVgpFKVPPLLsDDK 164
Cdd:cd08269    81 -------------------------------------------------GLSGGAFAEYDLADADHA--VPLPSLL-DGQ 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 165 AlFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGAIPINfdedSDP 244
Cdd:cd08269   109 A-FPGEPLGCALNVFRRGWIRAGKTVAVIGAGFIGLLFLQLAAAAGARRVIAIDRRPARLALAR-ELGATEVV----TDD 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 245 AQSIIEQTA---GHRGVDAVIDAVGFEAkgsttetvltnlklegssgkALRQCIAAVRRGGIVSVPGVYAGFIHGFLFGD 321
Cdd:cd08269   183 SEAIVERVReltGGAGADVVIEAVGHQW--------------------PLDLAGELVAERGRLVIFGYHQDGPRPVPFQT 242
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135  12 VQVENVPDPgVEQADDIILRITATAICGSDLHLYR----GKI--PQV-KHGDIFGHEFMGEVVETGKDVKNLQKGDRVVI 84
Cdd:cd08265    39 LRVEDVPVP-NLKPDEILIRVKACGICGSDIHLYEtdkdGYIlyPGLtEFPVVIGHEFSGVVEKTGKNVKNFEKGDPVTA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  85 PFVIACGDCFFCRLQQYAACENTNagkgaalnkkqipapaaLFGYSHlyggvPGGQAEYVRVPKGNVgpFKVPPLL---S 161
Cdd:cd08265   118 EEMMWCGMCRACRSGSPNHCKNLK-----------------ELGFSA-----DGAFAEYIAVNARYA--WEINELReiyS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 162 DDKAlFLSDILPTAWQAAKNAQ------IQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIP 235
Cdd:cd08265   174 EDKA-FEAGALVEPTSVAYNGLfirgggFRPGAYVVVYGAGPIGLAAIALAKAAGASKVIAFEISEERRNLAKEMGADYV 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 236 INFDEDSD--PAQSIIEQTAGhRGVDAVIDAVGFEAKG--STTETVLTNLKlegssgkalrqcIAAVRRgGIVSVPgvya 311
Cdd:cd08265   253 FNPTKMRDclSGEKVMEVTKG-WGADIQVEAAGAPPATipQMEKSIAINGK------------IVYIGR-AATTVP---- 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184135 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 1352184135   1 MKALTYH---GPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYRGKIPQVKHGD---IFGHEFMGEVVETGKDVK 74
Cdd:cd05289     1 MKAVRIHeygGPEVLELADVPTPEP-GPGEVLVKVHAAGVNPVDLKIREGLLKAAFPLTlplIPGHDVAGVVVAVGPGVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  75 NLQKGDRVvipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalFGYSHLYGGvpGGQAEYVRVPKGNVgpF 154
Cdd:cd05289    80 GFKVGDEV--------------------------------------------FGMTPFTRG--GAYAEYVVVPADEL--A 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 155 KVPPLLSDDKA--LFLSDIlpTAWQA-AKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVV--DHHPYRLHFAA 228
Cdd:cd05289   112 LKPANLSFEEAaaLPLAGL--TAWQAlFELGGLKAGQTVLIHGAaGGVGSFAVQLAKARGARVIATAsaANADFLRSLGA 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 229 DrygaIPINFDEDSdpaqsiIEQTAGHRGVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRRGG-IVSVP 307
Cdd:cd05289   190 D----EVIDYTKGD------FERAAAPGGVDAVLDTVG---------------------GETLARSLALVKPGGrLVSIA 238
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135  24 QADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFViACGDCFFCRLQQYAA 103
Cdd:cd08278    26 RPDEVLVRIVATGICHTDLVVRDGGLP-TPLPAVLGHEGAGVVEAVGSAVTGLKPGDHVVLSFA-SCGECANCLSGHPAY 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 104 CENTNAGKGAALNKkqiPAPAALfgysHLYGGVPG-----GQ---AEYVRVPKGNVgpFKVPPLLsdDKALF--LSDILP 173
Cdd:cd08278   104 CENFFPLNFSGRRP---DGSTPL----SLDDGTPVhghffGQssfATYAVVHERNV--VKVDKDV--PLELLapLGCGIQ 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 174 TAWQAAKNA-QIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADrYGA-IPINfDEDSDPAQSIIEQ 251
Cdd:cd08278   173 TGAGAVLNVlKPRPGSSIAVFGAGAVGLAAVMAAKIAGCTTIIAVDIVDSRLELAKE-LGAtHVIN-PKEEDLVAAIREI 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 252 TAGhrGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGG---IVSVPGVYAGFihGFLFGDAFDKGLS 328
Cdd:cd08278   251 TGG--GVDYALDTTG--------------------VPAVIEQAVDALAPRGtlaLVGAPPPGAEV--TLDVNDLLVSGKT 306
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1352184135 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 1352184135   1 MKA---LTYHGPHHVQVENVPDPgveQADDIILRITATAICGSDLHLYRGKI------------PQVKHGDIFGHEFMGE 65
Cdd:cd08240     1 MKAaavVEPGKPLEEVEIDTPKP---PGTEVLVKVTACGVCHSDLHIWDGGYdlgggktmslddRGVKLPLVLGHEIVGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  66 VVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACEntnagKGAALNkkqipapaalfgyshlyGGVPGGQAEYVR 145
Cdd:cd08240    78 VVAVGPDAADVKVGDKVLVYPWIGCGECPVCLAGDENLCA-----KGRALG-----------------IFQDGGYAEYVI 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 146 VPKGNVgpFKVPPLLSDDKALFL--SDIlpTAWQAAKNAQIQQGS-SVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPY 222
Cdd:cd08240   136 VPHSRY--LVDPGGLDPALAATLacSGL--TAYSAVKKLMPLVADePVVIIGAGGLGLMALALLKALGPANIIVVDIDEA 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 223 RLHfAADRYGAIPINFDEDSDPAQSIIEQTAGhrGVDAVIDAVGFEAkgsttetvltnlklegSSGKALRqciaAVRRGG 302
Cdd:cd08240   212 KLE-AAKAAGADVVVNGSDPDAAKRIIKAAGG--GVDAVIDFVNNSA----------------TASLAFD----ILAKGG 268
                         330
                  ....*....|
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPGVEQADDIILRITATAICGSDlhlyrgkIPQV-KHGDIF-----GHEFMGEVVETGKDVK 74
Cdd:PRK10309    1 MKSVVNDTDGIVRVAESPIPEIKHQDDVLVKVASSGLCGSD-------IPRIfKNGAHYypitlGHEFSGYVEAVGSGVD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  75 NLQKGDRVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkkqipapaalfgYSHLYGGVPGGQAEYVRVPKGNVgpF 154
Cdd:PRK10309   74 DLHPGDAVACVPLLPCFTCPECLRGFYSLCAK----------------------YDFIGSRRDGGNAEYIVVKRKNL--F 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 155 KVPPLLSDDKALFLSDIlPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADrYGAI 234
Cdd:PRK10309  130 ALPTDMPIEDGAFIEPI-TVGLHAFHLAQGCEGKNVIIIGAGTIGLLAIQCAVALGAKSVTAIDINSEKLALAKS-LGAM 207
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184135 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 1352184135  24 QADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAA 103
Cdd:cd05279    24 KAGEVRIKVVATGVCHTDLHVIDGKLP-TPLPVILGHEGAGIVESIGPGVTTLKPGDKVIPLFGPQCGKCKQCLNPRPNL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 104 CENTNA--GKGA------ALNKKQIPApaalfgysHLYGGVpGGQAEYVRVPKGNVGpfKVPPLLSDDKALFLSDILPTA 175
Cdd:cd05279   103 CSKSRGtnGRGLmsdgtsRFTCKGKPI--------HHFLGT-STFAEYTVVSEISLA--KIDPDAPLEKVCLIGCGFSTG 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 176 WQAAKN-AQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAAdRYGAIP-IN-FDEDSDPAQSIIEQT 252
Cdd:cd05279   172 YGAAVNtAKVTPGSTCAVFGLGGVGLSVIMGCKAAGASRIIAVDINKDKFEKAK-QLGATEcINpRDQDKPIVEVLTEMT 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 253 AGhrGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGG----IVSVP--GVYAGFIHGFLFGDAFDKG 326
Cdd:cd05279   251 DG--GVDYAFEVIG--------------------SADTLKQALDATRLGGgtsvVVGVPpsGTEATLDPNDLLTGRTIKG 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1352184135 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 1352184135   9 PHHVQVENVPDPGveqADDIILRITATAICGSDLHLYRG----KIPQVkhgdiFGHEFMGEVVETGKDVKNLQKGDRVVI 84
Cdd:cd08281    20 PLVIEEVELDPPG---PGEVLVKIAAAGLCHSDLSVINGdrprPLPMA-----LGHEAAGVVVEVGEGVTDLEVGDHVVL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  85 PFVIACGDCFFCRLQQYAACEntnagKGAALNKKqipapAALFG------------YSHLygGVpGGQAEYVRVPKGNVg 152
Cdd:cd08281    92 VFVPSCGHCRPCAEGRPALCE-----PGAAANGA-----GTLLSggrrlrlrggeiNHHL--GV-SAFAEYAVVSRRSV- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 153 pFKVPPLLSDDK-ALFLSDILPTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADrY 231
Cdd:cd08281   158 -VKIDKDVPLEIaALFGCAVLTGVGAVVNTAGVRPGQSVAVVGLGGVGLSALLGAVAAGASQVVAVDLNEDKLALARE-L 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184135 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 1352184135   1 MKALTYHGPHH-VQVENV--PDPGVeqaDDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQ 77
Cdd:PRK13771    1 MKAVILPGFKQgYRIEEVpdPKPGK---DEVVIKVNYAGLCYRDLLQLQGFYPRMKYPVILGHEVVGTVEEVGENVKGFK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  78 KGDRVVIPFVIACGDCFFCRLQQYAACENtnagkgaalnkKQIpapaalfgyshlYG-GVPGGQAEYVRVPKGNVgpFKV 156
Cdd:PRK13771   78 PGDRVASLLYAPDGTCEYCRSGEEAYCKN-----------RLG------------YGeELDGFFAEYAKVKVTSL--VKV 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 157 PPLLSDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVVDHHPYR--LHFAADrYGA 233
Cdd:PRK13771  133 PPNVSDEGAVIVPCVTGMVYRGLRRAGVKKGETVLVTGAgGGVGIHAIQVAKALGAKVIAVTSSESKAkiVSKYAD-YVI 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1352184135 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 1352184135  26 DDIILRITATAICGSDLHLYRG-KIPQ--VKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYA 102
Cdd:PLN02702   42 HDVRVRMKAVGICGSDVHYLKTmRCADfvVKEPMVIGHECAGIIEEVGSEVKHLVVGDRVALEPGISCWRCNLCKEGRYN 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 103 ACENTnagkgaalnkKQIPAPAalfgyshlyggVPGGQAEYVRVPkGNVGpFKVPPLLSDDKALfLSDILPTAWQAAKNA 182
Cdd:PLN02702  122 LCPEM----------KFFATPP-----------VHGSLANQVVHP-ADLC-FKLPENVSLEEGA-MCEPLSVGVHACRRA 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 183 QIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADrYGAIPI----NFDEDSDPAQSIIEQTAGhRGV 258
Cdd:PLN02702  178 NIGPETNVLVMGAGPIGLVTMLAARAFGAPRIVIVDVDDERLSVAKQ-LGADEIvlvsTNIEDVESEVEEIQKAMG-GGI 255
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1352184135 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 1352184135   6 YHGPHHVQVENVPDPGveqADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIP 85
Cdd:cd08245     8 AGGPLEPEEVPVPEPG---PGEVLIKIEACGVCHTDLHAAEGDWGGSKYPLVPGHEIVGEVVEVGAGVEGRKVGDRVGVG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  86 FVI-ACGDCFFCRLQQYAACENtnagkgaalnkkqipapAALFGYSHLyggvpGGQAEYVRVPKGNVGPFkvPPLLSDDK 164
Cdd:cd08245    85 WLVgSCGRCEYCRRGLENLCQK-----------------AVNTGYTTQ-----GGYAEYMVADAEYTVLL--PDGLPLAQ 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 165 A--LFLSDIlpTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGAIPINFDEDS 242
Cdd:cd08245   141 AapLLCAGI--TVYSALRDAGPRPGERVAVLGIGGLGHLAVQYARAMGFE-TVAITRSPDKRELARKLGADEVVDSGAEL 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 243 DpaqsiIEQTAGhrGVDAVIDAVgfeakgsttetvltnlklegSSGKALRQCIAAVRRGGIVSVPGVYAGFIHGFLFGDA 322
Cdd:cd08245   218 D-----EQAAAG--GADVILVTV--------------------VSGAAAEAALGGLRRGGRIVLVGLPESPPFSPDIFPL 270
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184135 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 1352184135  24 QADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAA 103
Cdd:cd08301    26 QAMEVRIKILHTSLCHTDVYFWEAKGQTPLFPRILGHEAAGIVESVGEGVTDLKPGDHVLPVFTGECKECRHCKSEKSNM 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 104 CE--NTNAGKGAALNKKQIPAPAALFGYSHLYGGvpGGQAEYVRVPKGNVGpfKVPPLLSDDKALFLSDILPTAWQAA-K 180
Cdd:cd08301   106 CDllRINTDRGVMINDGKSRFSINGKPIYHFVGT--STFSEYTVVHVGCVA--KINPEAPLDKVCLLSCGVSTGLGAAwN 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 181 NAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHfAADRYGAIP-INFDEDSDPAQSII-EQTAGhrGV 258
Cdd:cd08301   182 VAKVKKGSTVAIFGLGAVGLAVAEGARIRGASRIIGVDLNPSKFE-QAKKFGVTEfVNPKDHDKPVQEVIaEMTGG--GV 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 259 DAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVRRGG----IVSVPGVYAGF-IHGFLFgdafdkgLSfkmGQ 333
Cdd:cd08301   259 DYSFECTG--------------------NIDAMISAFECVHDGWgvtvLLGVPHKDAVFsTHPMNL-------LN---GR 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184135 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 1352184135   7 HGPHHVQVEnvpDPGVE-QADDIILRITATAICGSDLHLYR-GKIP--QVKHGDIFGHEFMGEVVETgkDVKNLQKGDRV 82
Cdd:PRK09880   11 AGKKDVAVT---EQEIEwNNNGTLVQITRGGICGSDLHYYQeGKVGnfVIKAPMVLGHEVIGKIVHS--DSSGLKEGQTV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  83 VIPFVIACGDCFFCRLQQYAACENTNagkgaalnkkqipapaaLFGYSHLYGGVPGGQAEYVRVPKGNVGPFkvpPLLSD 162
Cdd:PRK09880   86 AINPSKPCGHCKYCLSHNENQCTTMR-----------------FFGSAMYFPHVDGGFTRYKVVDTAQCIPY---PEKAD 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPqvKHGdIFGHEFMGEVVETGKdvKNLQkGD 80
Cdd:cd08242     1 MKALVLDGGLDLRVEDLPKPEPP-PGEALVRVLLAGICNTDLEIYKGYYP--FPG-VPGHEFVGIVEEGPE--AELV-GK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  81 RVVIPFVIACGDCFFCRLQQYAACENTNAgkgaalnkkqipapaalFGYShlygGVPGGQAEYVRVPKGNvgPFKVPPLL 160
Cdd:cd08242    74 RVVGEINIACGRCEYCRRGLYTHCPNRTV-----------------LGIV----DRDGAFAEYLTLPLEN--LHVVPDLV 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 161 SDDKALFlsdILPTAwqAAKNAQIQQ----GSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGAIPI 236
Cdd:cd08242   131 PDEQAVF---AEPLA--AALEILEQVpitpGDKVAVLGDGKLGLLIAQVLALTGPD-VVLVGRHSEKLALARRLGVETVL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 237 NFDEDSDPaqsiieqtaghRGVDAVIDAVGfeakgsttetvltnlklegsSGKALRQCIAAVR-RGGIV--SVPGVYAGF 313
Cdd:cd08242   205 PDEAESEG-----------GGFDVVVEATG--------------------SPSGLELALRLVRpRGTVVlkSTYAGPASF 253
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 314 -----------IHGFLFGDaFDKGlsfkmgqthvhawlgelLPLIEKGLLKPEEIVTHYMPFEEAargYEIFEK-REEEC 381
Cdd:cd08242   254 dltkavvneitLVGSRCGP-FAPA-----------------LRLLRKGLVDVDPLITAVYPLEEA---LEAFERaAEPGA 312

                  ....*..
gi 1352184135 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 1352184135  19 DPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRV-VIPFVIACGDCFFCR 97
Cdd:cd05283    18 ERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDRVgVGCQVDSCGTCEQCK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  98 --LQQYaaCENTnagkgaalnkkqipapaALFGYSHLYGGVP--GGQAEYVRVPKGNVgpFKVPPLLSDDKA--LFLSDI 171
Cdd:cd05283    98 sgEEQY--CPKG-----------------VVTYNGKYPDGTItqGGYADHIVVDERFV--FKIPEGLDSAAAapLLCAGI 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1352184135 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 1352184135   1 MKALTY---HGPHHVQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPQVKHG-DIFGHEFMGEVVETGKDVKNL 76
Cdd:cd05276     1 MKAIVIkepGGPEVLELGEVPKPAPG-PGEVLIRVAAAGVNRADLLQRQGLYPPPPGAsDILGLEVAGVVVAVGPGVTGW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  77 QKGDRVvipfviacgdcffcrlqqyaacentnagkgaalnkkqipapAALfgyshLYGGvpgGQAEYVRVPKGNVgpFKV 156
Cdd:cd05276    80 KVGDRV-----------------------------------------CAL-----LAGG---GYAEYVVVPAGQL--LPV 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 157 PPLLSDDKALFLSDILPTAWQAAKN-AQIQQGSSVAVY-GAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADrYGA- 233
Cdd:cd05276   109 PEGLSLVEAAALPEVFFTAWQNLFQlGGLKAGETVLIHgGASGVGTAAIQLAKALGAR-VIATAGSEEKLEACRA-LGAd 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 234 IPINFDEDsDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRRGG-IVSVpGVYAG 312
Cdd:cd05276   187 VAINYRTE-DFAEEVKEATGG-RGVDVILDMVG---------------------GDYLARNLRALAPDGrLVLI-GLLGG 242
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184135 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 1352184135  24 QADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAA 103
Cdd:cd08300    26 KAGEVRIKILATGVCHTDAYTLSGADPEGLFPVILGHEGAGIVESVGEGVTSVKPGDHVIPLYTPECGECKFCKSGKTNL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 104 CENTNA--GKGAA--------LNKKQIpapaalfgySHLYGgvPGGQAEYVRVPKGNVGpfKVPPLLSDDKALFLSDILP 173
Cdd:cd08300   106 CQKIRAtqGKGLMpdgtsrfsCKGKPI---------YHFMG--TSTFSEYTVVAEISVA--KINPEAPLDKVCLLGCGVT 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 174 TAWQAAKN-AQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRlhFA-ADRYGAIP-INFDEDSDPAQS-II 249
Cdd:cd08300   173 TGYGAVLNtAKVEPGSTVAVFGLGAVGLAVIQGAKAAGASRIIGIDINPDK--FElAKKFGATDcVNPKDHDKPIQQvLV 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 250 EQTAGhrGVDAVIDAVGfeakgsttetvltNLKLegssgkaLRQCIAAVRRGGIVSV-PGVYAGF--IHGFLF------- 319
Cdd:cd08300   251 EMTDG--GVDYTFECIG-------------NVKV-------MRAALEACHKGWGTSViIGVAAAGqeISTRPFqlvtgrv 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1352184135 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 1352184135   1 MKAL---TYHGPHHVQVENV-PDPGVEqaDDIILRITATAICGSDLHLYRGKIpQVKHGDIF--GHEFMGEVVETGKDVK 74
Cdd:cd08241     1 MKAVvckELGGPEDLVLEEVpPEPGAP--GEVRIRVEAAGVNFPDLLMIQGKY-QVKPPLPFvpGSEVAGVVEAVGEGVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  75 NLQKGDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqipapAALFGyshlyggvpGGQAEYVRVPKGNVgpF 154
Cdd:cd08241    78 GFKVGDRVV----------------------------------------ALTGQ---------GGFAEEVVVPAAAV--F 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 155 KVPPLLSDDKALFLSDILPTAWQAAKN-AQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVVdHHPYRLHFAAdRYG 232
Cdd:cd08241   107 PLPDGLSFEEAAALPVTYGTAYHALVRrARLQPGETVLVLGAaGGVGLAAVQLAKALGARVIAAA-SSEEKLALAR-ALG 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135 312 GFI---------------HGFLFGDafdkglsFKMGQTHVHAW-LGELLPLIEKGLLKPEeiVTHYMPFEEAARGYEIFE 375
Cdd:cd08241   242 GEIpqipanllllknisvVGVYWGA-------YARREPELLRAnLAELFDLLAEGKIRPH--VSAVFPLEQAAEALRALA 312

                  ...
gi 1352184135 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 1352184135  30 LRITATAICGSDLHLYRGKIP-QVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAACEN-- 106
Cdd:PLN02740   40 IKILYTSICHTDLSAWKGENEaQRAYPRILGHEAAGIVESVGEGVEDLKAGDHVIPIFNGECGDCRYCKRDKTNLCETyr 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 107 --------TNAGkGAALNKKQIPAPAALFGYSHLYggvpggqAEYVRVPKGNVgpFKVPPLLSDDKALFLSDILPTAWQA 178
Cdd:PLN02740  120 vdpfksvmVNDG-KTRFSTKGDGQPIYHFLNTSTF-------TEYTVLDSACV--VKIDPNAPLKKMSLLSCGVSTGVGA 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 179 AKN-AQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRlhFAADRYGAIP--INFDEDSDPAQSII-EQTAG 254
Cdd:PLN02740  190 AWNtANVQAGSSVAIFGLGAVGLAVAEGARARGASKIIGVDINPEK--FEKGKEMGITdfINPKDSDKPVHERIrEMTGG 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 255 hrGVDavidaVGFEAKGSTtetvltnlklegssgKALRQCIAAVRRG-GIVSVPGVYAG---------------FIHGFL 318
Cdd:PLN02740  268 --GVD-----YSFECAGNV---------------EVLREAFLSTHDGwGLTVLLGIHPTpkmlplhpmelfdgrSITGSV 325
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184135 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 1352184135   4 LTYHGPH---HVQVENVPDPGveqADDIILRITATAICGSDLHLYRGKIPQVKHGDIF-GHEFMGEVVETGKDVKNLQKG 79
Cdd:cd08273     6 VTRRGGPevlKVVEADLPEPA---AGEVVVKVEASGVSFADVQMRRGLYPDQPPLPFTpGYDLVGRVDALGSGVTGFEVG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  80 DRVvipfviacgdcffcrlqqyaacentnagkgAALNKKqipapaalfgyshlyggvpGGQAEYVRVPKGNVGPfkVPPL 159
Cdd:cd08273    83 DRV------------------------------AALTRV-------------------GGNAEYINLDAKYLVP--VPEG 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 160 LSDDKALFLSDILPTAWQAAKN-AQIQQGSSVAVYGA-GPVGLLTIACARLLGAeQIFVVDhhPYRLHFAADRYGAIPIN 237
Cdd:cd08273   112 VDAAEAVCLVLNYVTAYQMLHRaAKVLTGQRVLIHGAsGGVGQALLELALLAGA-EVYGTA--SERNHAALRELGATPID 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 238 FDEDSDPAQSIIEqtaghRGVDAVIDAVGFEakgsttetvltnlklegssgkALRQCIAAVRRGGIVSVPGVYAGFIHGF 317
Cdd:cd08273   189 YRTKDWLPAMLTP-----GGVDVVFDGVGGE---------------------SYEESYAALAPGGTLVCYGGNSSLLQGR 242
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 318 L-------FGDAFDKGLSFKMG-QTH---VHAW-----------LGELLPLIEKGLLKPeeIVTHYMPFEEAARGYEIFE 375
Cdd:cd08273   243 RslaalgsLLARLAKLKLLPTGrRATfyyVWRDraedpklfrqdLTELLDLLAKGKIRP--KIAKRLPLSEVAEAHRLLE 320

                  .
gi 1352184135 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 1352184135   1 MKALTYH--GPHHVQVENVPDPGVEQaDDIILRITATAICGSDLHLYRG-KIPQVKHgdIFGHEFMGEVVETGKDVKNLQ 77
Cdd:cd08264     1 MKALVFEksGIENLKVEDVKDPKPGP-GEVLIRVKMAGVNPVDYNVINAvKVKPMPH--IPGAEFAGVVEEVGDHVKGVK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  78 KGDRVVIPFVIACGDCFFCRLQQYAACENTNAGkGAALNkkqipapaalfgyshlyggvpGGQAEYVRVPKGNVgpFKVP 157
Cdd:cd08264    78 KGDRVVVYNRVFDGTCDMCLSGNEMLCRNGGII-GVVSN---------------------GGYAEYIVVPEKNL--FKIP 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 158 PLLSDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVVDHHPYRlhfaadRYGAIPI 236
Cdd:cd08264   134 DSISDELAASLPVAALTAYHALKTAGLGPGETVVVFGAsGNTGIFAVQLAKMMGAEVIAVSRKDWLK------EFGADEV 207
                         250       260       270
                  ....*....|....*....|....*....|
gi 1352184135 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 1352184135  24 QADDIILRITATAICGSDLHLYRGK--IPQvkhgdIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQY 101
Cdd:PLN02827   36 QPLEIRIKVVSTSLCRSDLSAWESQalFPR-----IFGHEASGIVESIGEGVTEFEKGDHVLTVFTGECGSCRHCISGKS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 102 AACENTNAGKGAALNKKQIPAPAALFGYSHLYGGVpGGQAEYVRVPKGNVgpFKVPPLLSDDKALFLSDILPTAWQAAKN 181
Cdd:PLN02827  111 NMCQVLGLERKGVMHSDQKTRFSIKGKPVYHYCAV-SSFSEYTVVHSGCA--VKVDPLAPLHKICLLSCGVAAGLGAAWN 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 182 -AQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPINFDEDSDPAQSIIEQTAGHrGVDa 260
Cdd:PLN02827  188 vADVSKGSSVVIFGLGTVGLSVAQGAKLRGASQIIGVDINPEKAEKAKTFGVTDFINPNDLSEPIQQVIKRMTGG-GAD- 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 261 vidaVGFEAKGSTtetvltnlkleGSSGKALRQCI----AAVRRGGIVSVPGVYAGFihGFLFGDAFDKGLSFkmGQTHV 336
Cdd:PLN02827  266 ----YSFECVGDT-----------GIATTALQSCSdgwgLTVTLGVPKAKPEVSAHY--GLFLSGRTLKGSLF--GGWKP 326
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1352184135 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 1352184135   7 HGPHHVQVENVPDPGVEQaddIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIP- 85
Cdd:cd08296    10 GGPLELVERDVPLPGPGE---VLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVGEGVSRWKVGDRVGVGw 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  86 FVIACGDCFFCRLQQYAACENtnagkgaalnkKQIPapaalfGYShlyggVPGGQAEYVRVPKGNVGPfkVPPLLSDDKA 165
Cdd:cd08296    87 HGGHCGTCDACRRGDFVHCEN-----------GKVT------GVT-----RDGGYAEYMLAPAEALAR--IPDDLDAAEA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 166 --LFLSDIlpTAWQAAKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIfVVDHHPYRLHFA----ADRYgaipINFD 239
Cdd:cd08296   143 apLLCAGV--TTFNALRNSGAKPGDLVAVQGIGGLGHLAVQYAAKMGFRTV-AISRGSDKADLArklgAHHY----IDTS 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 240 EDsDPAQSIieQTAGhrGVDAVIDAVGFeakGSTTETVLTNLKLEGssgkalRQCIAAVRRGGIVSVPGVYAGF---IHG 316
Cdd:cd08296   216 KE-DVAEAL--QELG--GAKLILATAPN---AKAISALVGGLAPRG------KLLILGAAGEPVAVSPLQLIMGrksIHG 281
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184135 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 1352184135   1 MKAL---TYHGPHHVQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIP-QVKHGDIFGHEFMGEVVETGKDVKNL 76
Cdd:cd08272     1 MKALvleSFGGPEVFELREVPRPQPG-PGQVLVRVHASGVNPLDTKIRRGGAAaRPPLPAILGCDVAGVVEAVGEGVTRF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  77 QKGDRVvipfviacgdcFFCrlqqyaacentNAGkgaalnkkqipapaalfgyshlYGGVPGGQAEYVRVPKGNVGPfkV 156
Cdd:cd08272    80 RVGDEV-----------YGC-----------AGG----------------------LGGLQGSLAEYAVVDARLLAL--K 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 157 PPLLSDDKALFLSDILPTAWQAAKN-AQIQQGSSVAVY-GAGPVGLLTIACARLLGAEQIFVVDhhPYRLHFaADRYGAI 234
Cdd:cd08272   114 PANLSMREAAALPLVGITAWEGLVDrAAVQAGQTVLIHgGAGGVGHVAVQLAKAAGARVYATAS--SEKAAF-ARSLGAD 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 235 PINfDEDSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRR-GGIVSVPGVYAGF 313
Cdd:cd08272   191 PII-YYRETVVEYVAEHTGG-RGFDVVFDTVG---------------------GETLDASFEAVALyGRVVSILGGATHD 247
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184135 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 1352184135   1 MKALTYHGPHH--VQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKNLQK 78
Cdd:cd08249     1 QKAAVLTGPGGglLVVVDVPVPKPG-PDEVLVKVKAVALNPVDWKHQDYGFI-PSYPAILGCDFAGTVVEVGSGVTRFKV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  79 GDRVvipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalFGYSHLYGGVP---GGQAEYVRVPKGNVgpFK 155
Cdd:cd08249    79 GDRV--------------------------------------------AGFVHGGNPNDprnGAFQEYVVADADLT--AK 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 156 VPPLLSDDKA-------------LFLSDILPTAWQAAKNAqiQQGSSVAVYGAG-PVGLLTIACARLLGAEqIFVV---D 218
Cdd:cd08249   113 IPDNISFEEAatlpvglvtaalaLFQKLGLPLPPPKPSPA--SKGKPVLIWGGSsSVGTLAIQLAKLAGYK-VITTaspK 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 219 HHPYrlhfaADRYGAIPInFD-EDSDPAQSIIEQTAGHrgVDAVIDAVGfeakgsttetvltnlklEGSSGKALRQCIAA 297
Cdd:cd08249   190 NFDL-----VKSLGADAV-FDyHDPDVVEDIRAATGGK--LRYALDCIS-----------------TPESAQLCAEALGR 244
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184135 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 1352184135  37 ICGSDLHlyrgkipqVKHGD-------IFGHEFMGEVVETGKDVKNLQKGDRVVIP-FVIACGDCFFCRLQQYAACENT- 107
Cdd:PRK09422   37 VCHTDLH--------VANGDfgdktgrILGHEGIGIVKEVGPGVTSLKVGDRVSIAwFFEGCGHCEYCTTGRETLCRSVk 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 108 NAgkgaalnkkqipapaalfGYShlyggVPGGQAEYVRVPKGNVgpFKVPPLLSDDKALFLSDILPTAWQAAKNAQIQQG 187
Cdd:PRK09422  109 NA------------------GYT-----VDGGMAEQCIVTADYA--VKVPEGLDPAQASSITCAGVTTYKAIKVSGIKPG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 188 SSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRLHFAADRYGAIPINFDEDSDPAQSIIEQTAGHRGvdAVIDAVgf 267
Cdd:PRK09422  164 QWIAIYGAGGLGNLALQYAKNVFNAKVIAVDINDDKLALAKEVGADLTINSKRVEDVAKIIQEKTGGAHA--AVVTAV-- 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135   1 MKALTYH---GPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYRGKIP-QVKHGDIFGHEFMGEVVETGKDVKNL 76
Cdd:cd08276     1 MKAWRLSgggGLDNLKLVEEPVPEP-GPGEVLVRVHAVSLNYRDLLILNGRYPpPVKDPLIPLSDGAGEVVAVGEGVTRF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  77 QKGDRVVIpfviacgdCFFcrlQQYAACENTNAGKGAAlnkkqipapaalfgyshLYGGVPGGQAEYVRVPKGnvGPFKV 156
Cdd:cd08276    80 KVGDRVVP--------TFF---PNWLDGPPTAEDEASA-----------------LGGPIDGVLAEYVVLPEE--GLVRA 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 157 PPLLSDDKAlflsDILP----TAWQA-AKNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIfvvdhhpyrlhfA---- 227
Cdd:cd08276   130 PDHLSFEEA----ATLPcaglTAWNAlFGLGPLKPGDTVLVQGTGGVSLFALQFAKAAGARVI------------Atsss 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 228 ---ADRYGAIP----INFDEDSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRR 300
Cdd:cd08276   194 dekLERAKALGadhvINYRTTPDWGEEVLKLTGG-RGVDHVVEVGG---------------------PGTLAQSIKAVAP 251
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184135 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 1352184135   1 MKALTYHGPHHVQVEN--VPDPGVEqADDIILRITATAICGSDLHLYRGKIP---QVKHGDIFGHEFMGEVVETGKDVKN 75
Cdd:cd08267     1 VVYTRYGSPEVLLLLEveVPIPTPK-PGEVLVKVHAASVNPVDWKLRRGPPKlllGRPFPPIPGMDFAGEVVAVGSGVTR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  76 LQKGDRVvipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalFGYSHLYGGvpGGQAEYVRVPKGNVgpFK 155
Cdd:cd08267    80 FKVGDEV--------------------------------------------FGRLPPKGG--GALAEYVVAPESGL--AK 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 156 VPPLLSDD--KALFLSDIlpTAWQA-AKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFV-----VDhhpyrlhF 226
Cdd:cd08267   112 KPEGVSFEeaAALPVAGL--TALQAlRDAGKVKPGQRVLINGAsGGVGTFAVQIAKALGAHVTGVcstrnAE-------L 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 227 AADrYGAipinfDEDSD-PAQSIIEQTAGHRGVDAVIDAVgfeakGSTTETVLTNLKLEGSSGKalrqciaAVRRGGIVS 305
Cdd:cd08267   183 VRS-LGA-----DEVIDyTTEDFVALTAGGEKYDVIFDAV-----GNSPFSLYRASLALKPGGR-------YVSVGGGPS 244
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184135 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 1352184135   1 MKALTYHGPH-HVQVENVPDPGVEqADDIILRITATAICGSDLHLYRGKIPQVKHGD---IFGHEFMGEVVETGKDvKNL 76
Cdd:cd08230     1 MKAIAVKPGKpGVRVVDIPEPEPT-PGEVLVRTLEVGVCGTDREIVAGEYGTAPPGEdflVLGHEALGVVEEVGDG-SGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  77 QKGDRVViPFVI-ACGDCFFCRLQQYAACEN---TNAG-KGAalnkkqipapaalfgyshlyggvPGGQAEYVRVPKGNV 151
Cdd:cd08230    79 SPGDLVV-PTVRrPPGKCLNCRIGRPDFCETgeyTERGiKGL-----------------------HGFMREYFVDDPEYL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 152 gpFKVPPLLSDDKALF--LSDILpTAWQAAKNAQ----IQQGSSVAVYGAGPVGLLTIACARLLGAEqIFVVDHHPYRLH 225
Cdd:cd08230   135 --VKVPPSLADVGVLLepLSVVE-KAIEQAEAVQkrlpTWNPRRALVLGAGPIGLLAALLLRLRGFE-VYVLNRRDPPDP 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1352184135 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 1352184135  26 DDIILRITATAICGSDLHLYRGKIPQVKHGdiFGHEFMGEVVETGKDVKNLQKGDRVVipfviacgdcffcrlqqyaace 105
Cdd:cd05195     1 DEVEVEVKAAGLNFRDVLVALGLLPGDETP--LGLECSGIVTRVGSGVTGLKVGDRVM---------------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 106 ntnagkgaalnkkqipapaalfgyshlyGGVPGGQAEYVRVPKGNVgpFKVPPLLSDDKAlflsDILP----TAWQAAKN 181
Cdd:cd05195    57 ----------------------------GLAPGAFATHVRVDARLV--VKIPDSLSFEEA----ATLPvaylTAYYALVD 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 182 -AQIQQGSSVAVY-GAGPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGAIP-INFDEDSDPAQSIIEQTAGhRGV 258
Cdd:cd05195   103 lARLQKGESVLIHaAAGGVGQAAIQLAQHLGAE-VFATVGSEEKREFLRELGGPVDhIFSSRDLSFADGILRATGG-RGV 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 259 DAVIDAVgfeakgsttetvltnlklegsSGKALRQCIAAVRRGG-IVSVpGVYAGFIHGFLFGDAFDKGLSF-------- 329
Cdd:cd05195   181 DVVLNSL---------------------SGELLRASWRCLAPFGrFVEI-GKRDILSNSKLGMRPFLRNVSFssvdldql 238
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135   1 MKALT---YHGPHHVQVENVPDPGVEQaDDIILRITATAICGSDLHLYRGKIPQVK-HGDIFGHEFMGEVVETGKDVKNL 76
Cdd:PTZ00354    2 MRAVTlkgFGGVDVLKIGESPKPAPKR-NDVLIKVSAAGVNRADTLQRQGKYPPPPgSSEILGLEVAGYVEDVGSDVKRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  77 QKGDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaALFGyshlyggvPGGQAEYVRVPKGNVgpFKV 156
Cdd:PTZ00354   81 KEGDRVM-----------------------------------------ALLP--------GGGYAEYAVAHKGHV--MHI 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 157 PPLLSDDKALFLSDILPTAWQAAK-NAQIQQGSSVAVY-GAGPVGLLTIACARLLGAEQIfVVDHHPYRLHFAaDRYGAI 234
Cdd:PTZ00354  110 PQGYTFEEAAAIPEAFLTAWQLLKkHGDVKKGQSVLIHaGASGVGTAAAQLAEKYGAATI-ITTSSEEKVDFC-KKLAAI 187
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1352184135 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 1352184135  24 QADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVIACGDCFFCRLQQYAA 103
Cdd:cd08299    31 KAHEVRIKIVATGICRSDDHVVSGKLV-TPFPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFVPQCGKCRACLNPESNL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 104 CENTNAGKGAAL----------NKKQIpapaalfgysHLYGGVpGGQAEYVRVPKGNVGpfKVPPLLSDDKALFLSDILP 173
Cdd:cd08299   110 CLKNDLGKPQGLmqdgtsrftcKGKPI----------HHFLGT-STFSEYTVVDEIAVA--KIDAAAPLEKVCLIGCGFS 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 174 TAWQAA-KNAQIQQGSSVAVYGAGPVGLLTIACARLLGAEQIFVVDHHPYRlhFA-ADRYGAIP-INFDEDSDPAQSII- 249
Cdd:cd08299   177 TGYGAAvNTAKVTPGSTCAVFGLGGVGLSAIMGCKAAGASRIIAVDINKDK--FAkAKELGATEcINPQDYKKPIQEVLt 254
                         250
                  ....*....|....*..
gi 1352184135 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 1352184135   1 MKA--LTYHGP----HHVQVENVPDPGveqADDIILRITATAICGSDLHLYRG-------------------------KI 49
Cdd:cd08274     1 MRAvlLTGHGGldklVYRDDVPVPTPA---PGEVLIRVGACGVNNTDINTREGwystevdgatdstgageagwwggtlSF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  50 PQVKHGDIFGHefmgeVVETGKDVKNLQKGDRVVIPFVIacgdcffcrlqqYAACENTnagkgaalnkkqiPAPAALFGy 129
Cdd:cd08274    78 PRIQGADIVGR-----VVAVGEGVDTARIGERVLVDPSI------------RDPPEDD-------------PADIDYIG- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 130 shlyGGVPGGQAEYVRVPKGNVgpFKVPPLLSDDK-ALFlsdilPTAWQAAKN----AQIQQGSSVAVYGA-GPVGLLTI 203
Cdd:cd08274   127 ----SERDGGFAEYTVVPAENA--YPVNSPLSDVElATF-----PCSYSTAENmlerAGVGAGETVLVTGAsGGVGSALV 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 204 ACARLLGAEQIFVV--DHHPYRLHFAADRYgaipINFDEDSDPAqsiiEQTAGHRGVDAVIDAVGfeakGSTTETVLTNL 281
Cdd:cd08274   196 QLAKRRGAIVIAVAgaAKEEAVRALGADTV----ILRDAPLLAD----AKALGGEPVDVVADVVG----GPLFPDLLRLL 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 282 KLEGssgkalRQCIAAVRRGGIVSVPgvyagfihgflFGDAFDKGLSFkMGQTHV-HAWLGELLPLIEKGLLKPeeIVTH 360
Cdd:cd08274   264 RPGG------RYVTAGAIAGPVVELD-----------LRTLYLKDLTL-FGSTLGtREVFRRLVRYIEEGEIRP--VVAK 323
                         410       420
                  ....*....|....*....|....*...
gi 1352184135 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 1352184135   1 MKALTYH---GPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDvkNLQ 77
Cdd:cd08243     1 MKAIVIEqpgGPEVLKLREIPIP-EPKPGWVLIRVKAFGLNRSEIFTRQGHSPSVKFPRVLGIEAVGEVEEAPGG--TFT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  78 KGDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqipapAALFGYSHLYggvPGGQAEYVRVPKGNVGPFKVP 157
Cdd:cd08243    78 PGQRVA----------------------------------------TAMGGMGRTF---DGSYAEYTLVPNEQVYAIDSD 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 158 plLSDDKALFLSDILPTAWQAAKNA-QIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVVdHHPYR----LHFAADRY 231
Cdd:cd08243   115 --LSWAELAALPETYYTAWGSLFRSlGLQPGDTLLIRGGtSSVGLAALKLAKALGATVTATT-RSPERaallKELGADEV 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 232 gaipinFDEDSDPAQSIIEQTAghrGVDAVIDAVGfeakgstTETVLTNLKlegssgkalrqciaAVRRGGIVSVPGVYA 311
Cdd:cd08243   192 ------VIDDGAIAEQLRAAPG---GFDKVLELVG-------TATLKDSLR--------------HLRPGGIVCMTGLLG 241

                  .
gi 1352184135 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 1352184135   8 GPHHVQVENVPDPGveqADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFV 87
Cdd:TIGR02822  13 GPLRFVERPVPRPG---PGELLVRVRACGVCRTDLHVSEGDLPVHRPRVTPGHEVVGEVAGRGADAGGFAVGDRVGIAWL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  88 -IACGDCFFCRLQQYAACENTNagkgaalnkkqipapaalfgyshlYGG--VPGGQAEYVRVPKGNVgpFKVPPLLSDDK 164
Cdd:TIGR02822  90 rRTCGVCRYCRRGAENLCPASR------------------------YTGwdTDGGYAEYTTVPAAFA--YRLPTGYDDVE 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135   1 MKALTYH---GPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGK-IPQVKHGDIFGHEFMGEVVETGKDVKNL 76
Cdd:cd08268     1 MRAVRFHqfgGPEVLRIEELPVP-APGAGEVLIRVEAIGLNRADAMFRRGAyIEPPPLPARLGYEAAGVVEAVGAGVTGF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  77 QKGDRVVIpfviacgdcffcrlqqyaacentnagkgaalnkkqipAPAALFGYSHLYGgvpggqaEYVRVPKGNVgpFKV 156
Cdd:cd08268    80 AVGDRVSV-------------------------------------IPAADLGQYGTYA-------EYALVPAAAV--VKL 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 157 PPLLSDDKALFLSDILPTAWQA-AKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVVDHhPYRLHFAADrYGAI 234
Cdd:cd08268   114 PDGLSFVEAAALWMQYLTAYGAlVELAGLRPGDSVLITAAsSSVGLAAIQIANAAGATVIATTRT-SEKRDALLA-LGAA 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 235 PINFDEDSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRRGGIVSVPGVYAGFI 314
Cdd:cd08268   192 HVIVTDEEDLVAEVLRITGG-KGVDVVFDPVG---------------------GPQFAKLADALAPGGTLVVYGALSGEP 249
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135   2 KALTYH---GPHHVQVENVPDPgVEQADDIILRITATAICGSDLHLYRGKIPqVKHGDIFGHEFMGEVVETGKDVKNLQK 78
Cdd:cd05286     1 KAVRIHktgGPEVLEYEDVPVP-EPGPGEVLVRNTAIGVNFIDTYFRSGLYP-LPLPFVLGVEGAGVVEAVGPGVTGFKV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  79 GDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalfgyshlYGGVPGGQAEYVRVPKGNVgpFKVPP 158
Cdd:cd05286    79 GDRVA-------------------------------------------------YAGPPGAYAEYRVVPASRL--VKLPD 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 159 LLSDDKA--LFLSDIlpTAWQAAKNA-QIQQGSSVAVYG-AGPVGLLTIACARLLGAEQIFVVDHhPYRLHFAADrYGAI 234
Cdd:cd05286   108 GISDETAaaLLLQGL--TAHYLLRETyPVKPGDTVLVHAaAGGVGLLLTQWAKALGATVIGTVSS-EEKAELARA-AGAD 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 235 -PINFDEDsDPAQSIIEQTAGhRGVDAVIDAVGfeakGSTtetvltnlkLEGSsgkalrqcIAAVRRGGIVSVPGVYAGF 313
Cdd:cd05286   184 hVINYRDE-DFVERVREITGG-RGVDVVYDGVG----KDT---------FEGS--------LDSLRPRGTLVSFGNASGP 240
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 314 IHGFLFGDAFDKGLSFK----MGQTHVHAWL----GELLPLIEKGLLKPeEIVTHYmPFEEAARGYEIFEKReeecR--- 382
Cdd:cd05286   241 VPPFDLLRLSKGSLFLTrpslFHYIATREELlaraAELFDAVASGKLKV-EIGKRY-PLADAAQAHRDLESR----Kttg 314

                  ....*.
gi 1352184135 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 1352184135   9 PHHVQVENVP-DPGVEQADDIILRITATAICGSDLHL----YRGKIPQvkhGDIFGHEFMGEVVETGKDVKNLQKGDRVv 83
Cdd:cd05282     9 PLPLVLELVSlPIPPPGPGEVLVRMLAAPINPSDLITisgaYGSRPPL---PAVPGNEGVGVVVEVGSGVSGLLVGQRV- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  84 ipfviacgdcffcrlqqyaacentnagkgaalnkkqIPAPAAlfgyshlyggvpGGQAEYVRVPKGNVgpFKVPPLLSDD 163
Cdd:cd05282    85 ------------------------------------LPLGGE------------GTWQEYVVAPADDL--IPVPDSISDE 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 164 KALFLSdILP-TAW-QAAKNAQIQQGSSVAVYGAGP-VGLLTIACARLLGAEQIFVV--DHHPYRLhfaaDRYGAIPINF 238
Cdd:cd05282   115 QAAMLY-INPlTAWlMLTEYLKLPPGDWVIQNAANSaVGRMLIQLAKLLGFKTINVVrrDEQVEEL----KALGADEVID 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 239 DEDSDPAQSIIEQTaGHRGVDAVIDAVGfeakgsttetvltnlkleGSSGKALrqcIAAVRRGGIVSVPGVYAG----FI 314
Cdd:cd05282   190 SSPEDLAQRVKEAT-GGAGARLALDAVG------------------GESATRL---ARSLRPGGTLVNYGLLSGepvpFP 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 315 HGFLFGDAFD-KG--LSFKMGQTHVHAW---LGELLPLIEKGLLKPEeiVTHYMPFEEAArgyEIFEKREEECR--KVIL 386
Cdd:cd05282   248 RSVFIFKDITvRGfwLRQWLHSATKEAKqetFAEVIKLVEAGVLTTP--VGAKFPLEDFE---EAVAAAEQPGRggKVLL 322

                  .
gi 1352184135 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 1352184135 197 PVGLLTIACARLLGAEqIFVVDHHPYRLHFAAdRYGAIPINFDEDSDPAQSIIEQTAGhRGVDAVIDAVGfeakgsttet 276
Cdd:pfam00107   1 GVGLAAIQLAKAAGAK-VIAVDGSEEKLELAK-ELGADHVINPKETDLVEEIKELTGG-KGVDVVFDCVG---------- 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184135 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 1352184135  25 ADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQKGDRVVIPFVI-ACGDCFFCR--LQQY 101
Cdd:PLN02514   34 PEDVVIKVIYCGICHTDLHQIKNDLGMSNYPMVPGHEVVGEVVEVGSDVSKFTVGDIVGVGVIVgCCGECSPCKsdLEQY 113
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 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 1352184135   41 DLHLYRGKIPqvkHGDIFGHEFMGEVVETGKDVKNLQKGDRVVipfviacgdcffcrlqqyaacentnagkgaalnkkqi 120
Cdd:smart00829  12 DVLIALGLYP---GEAVLGGECAGVVTRVGPGVTGLAVGDRVM------------------------------------- 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  121 papaalfgyshlyGGVPGGQAEYVRVPKGNVgpFKVPPLLSDDKALFLSDILPTAWQAAKN-AQIQQGSSVAVY-GAGPV 198
Cdd:smart00829  52 -------------GLAPGAFATRVVTDARLV--VPIPDGWSFEEAATVPVVFLTAYYALVDlARLRPGESVLIHaAAGGV 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  199 GLLTIACARLLGAEqIFVVDHHPYRLHFaADRYGaIPIN--FD-EDSDPAQSIIEQTAGhRGVDAVIDAVgfeakgstte 275
Cdd:smart00829 117 GQAAIQLARHLGAE-VFATAGSPEKRDF-LRALG-IPDDhiFSsRDLSFADEILRATGG-RGVDVVLNSL---------- 182
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  276 tvltnlklegsSGKALRQCIAAVRRGGIvsvpgvyagFI---------HGFLFGDAFDKGLSF------KM--GQTHVHA 338
Cdd:smart00829 183 -----------SGEFLDASLRCLAPGGR---------FVeigkrdirdNSQLAMAPFRPNVSYhavdldALeeGPDRIRE 242
                          330
                   ....*....|....*.
gi 1352184135  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 1352184135   1 MKALTYHGP---HHVQVENVPDPGVeQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVKNLQ 77
Cdd:cd08271     1 MKAWVLPKPgaaLQLTLEEIEIPGP-GAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTGWK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  78 KGDRVVIpfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalfgysHLYGGVPGGQAEYVRVPkgNVGPFKVP 157
Cdd:cd08271    80 VGDRVAY----------------------------------------------HASLARGGSFAEYTVVD--ARAVLPLP 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 158 PLLSDDKALFLSDILPTAWQA-AKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEqIFVV---DHHPYRLHFAADryg 232
Cdd:cd08271   112 DSLSFEEAAALPCAGLTAYQAlFKKLRIEAGRTILITGGaGGVGSFAVQLAKRAGLR-VITTcskRNFEYVKSLGAD--- 187
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1352184135 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 1352184135   1 MKALTYH--GPHHV-QVENVPDPGVEqADDIILRITATAICGSDLHLYRGKI------PQVKHGDIfghefMGEVVETGK 71
Cdd:cd08253     1 MRAIRYHefGAPDVlRLGDLPVPTPG-PGEVLVRVHASGVNPVDTYIRAGAYpglpplPYVPGSDG-----AGVVEAVGE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  72 DVKNLQKGDRVvipfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalFGYSHLYGGVPGGQAEYVRVPKGNV 151
Cdd:cd08253    75 GVDGLKVGDRV--------------------------------------------WLTNLGWGRRQGTAAEYVVVPADQL 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 152 gpFKVPPLLSDDKALFLSdiLP--TAWQAA-KNAQIQQGSSVAVYG-AGPVGLLTIACARLLGAEQIFVVDhHPYRLHFA 227
Cdd:cd08253   111 --VPLPDGVSFEQGAALG--IPalTAYRALfHRAGAKAGETVLVHGgSGAVGHAAVQLARWAGARVIATAS-SAEGAELV 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 228 ADRYGAIPINFDEDsDPAQSIIEQTAGhRGVDAVIDAvgfeakgsttetvltnlklegSSGKALRQCIAAVRRGGIVSVP 307
Cdd:cd08253   186 RQAGADAVFNYRAE-DLADRILAATAG-QGVDVIIEV---------------------LANVNLAKDLDVLAPGGRIVVY 242
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 308 G--VYAGFIHgflFGDAFDKGLS------FKMGQTHVHAWLGELLPLIEKGLLKPEeiVTHYMPFEEAARGYEIFEkREE 379
Cdd:cd08253   243 GsgGLRGTIP---INPLMAKEASirgvllYTATPEERAAAAEAIAAGLADGALRPV--IAREYPLEEAAAAHEAVE-SGG 316

                  ....*....
gi 1352184135 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 1352184135   1 MKAL---TYHGPHH-VQVENVPDPGVEQADDIILRITATAI--------CG---SDLHLYRGKIPQVKHGDIF----GHE 61
Cdd:cd08248     1 MKAWqihSYGGIDSlLLLENARIPVIRKPNQVLIKVHAASVnpidvlmrSGygrTLLNKKRKPQSCKYSGIEFpltlGRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  62 FMGEVVETGKDVKNLQKGDRV--VIPFVIacgdcffcrlqqyaacentnagkgaalnkkqipapaalfgyshlyggvPGG 139
Cdd:cd08248    81 CSGVVVDIGSGVKSFEIGDEVwgAVPPWS------------------------------------------------QGT 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 140 QAEYVRVPKGNVGpfKVPPLLSDDKALFLSDILPTAWQAAKNA-----QIQQGSSVAVYGA-GPVGllTIACaRLLGAEQ 213
Cdd:cd08248   113 HAEYVVVPENEVS--KKPKNLSHEEAASLPYAGLTAWSALVNVgglnpKNAAGKRVLILGGsGGVG--TFAI-QLLKAWG 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 214 IFVV-----DHHPYRLHFAADRygAIPINfdedsdpAQSIIEQTAGHRGVDAVIDAVGfeakgsttetvltnLKLEGSSG 288
Cdd:cd08248   188 AHVTttcstDAIPLVKSLGADD--VIDYN-------NEDFEEELTERGKFDVILDTVG--------------GDTEKWAL 244
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 289 KALRQCiaavrrGGIVS-VPGV-----YAGFIHGFLFG--DAFDKGLSFKMGQTHVHaW---------LGELLPLIEKGL 351
Cdd:cd08248   245 KLLKKG------GTYVTlVSPLlkntdKLGLVGGMLKSavDLLKKNVKSLLKGSHYR-WgffspsgsaLDELAKLVEDGK 317
                         410       420
                  ....*....|....*....|....*.
gi 1352184135 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 1352184135   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 1352184135   2 KALTYHGPHHVQVENVPDPGVeQADDIILRITATAICGSDLHLYR--GKIPQV-----KHGDIFGHEFMGEVVETGKDVK 74
Cdd:cd08238     4 KAWRMYGKGDLRLEKFELPEI-ADDEILVRVISDSLCFSTWKLALqgSDHKKVpndlaKEPVILGHEFAGTILKVGKKWQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  75 N-LQKGDRVVIPfviacgdcffcrlqqyaacentnagkgAALnkkQIPAPAALFGYSHLYggvPGGQAEYVRVPKgNVGP 153
Cdd:cd08238    83 GkYKPGQRFVIQ---------------------------PAL---ILPDGPSCPGYSYTY---PGGLATYHIIPN-EVME 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 154 FKVPPLLSDDKALFLSDILPTAW-QAAKNAQIQ--------------QGSSVAVYGAGPVGLLTIACARLL--GAEQIFV 216
Cdd:cd08238   129 QDCLLIYEGDGYAEASLVEPLSCvIGAYTANYHlqpgeyrhrmgikpGGNTAILGGAGPMGLMAIDYAIHGpiGPSLLVV 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184135 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 1352184135   1 MKALTY--HG-PHHV-QVENVPDPGVEQADDIILRITATAICGSDLHL----YRGKIPQVKHGD-IFGHEFMGEVVETGK 71
Cdd:cd08290     1 AKALVYteHGePKEVlQLESYEIPPPGPPNEVLVKMLAAPINPADINQiqgvYPIKPPTTPEPPaVGGNEGVGEVVKVGS 80
                          90
                  ....*....|..
gi 1352184135  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 1352184135   1 MKALTYHG--PHHVQVENVPDPgVEQADDIILRITATAICGSDLHLyrgkIPQVKHGDIFGHEFMGEVVETGKDVKNLQK 78
Cdd:cd08270     1 MRALVVDPdaPLRLRLGEVPDP-QPAPHEALVRVAAISLNRGELKF----AAERPDGAVPGWDAAGVVERAAADGSGPAV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  79 GDRVVIpfviacgdcffcrlqqyaacentnagkgaalnkkqipapaalfgyshlyGGVPGGQAEYVRVPKGNVGPfkVPP 158
Cdd:cd08270    76 GARVVG-------------------------------------------------LGAMGAWAELVAVPTGWLAV--LPD 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 159 LLSDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAEQIFVVdHHPYRLHFAADRYGA-IPI 236
Cdd:cd08270   105 GVSFAQAATLPVAGVTALRALRRGGPLLGRRVLVTGAsGGVGRFAVQLAALAGAHVVAVV-GSPARAEGLRELGAAeVVV 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 237 NFDEDSDPAqsiieqtaghrgVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRRGGIVSVPGVYAGFIHG 316
Cdd:cd08270   184 GGSELSGAP------------VDLVVDSVG---------------------GPQLARALELLAPGGTVVSVGSSSGEPAV 230
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184135 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 1352184135  26 DDIILRITATAICGSDLHLYRGKIPQV-KHGDIFGHEFMGEVVETGKDVKNLQKGDRVVipfviacgdcffcrlqqyaac 104
Cdd:cd08251     8 GEVRIQVRAFSLNFGDLLCVRGLYPTMpPYPFTPGFEASGVVRAVGPHVTRLAVGDEVI--------------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 105 entnAGKGAALnkkqipapaalfgyshlyggvpGGQAEYVRVPKGNVgpFKVPPLLSDDKALFLSDILPTAWQAAKNAQI 184
Cdd:cd08251    67 ----AGTGESM----------------------GGHATLVTVPEDQV--VRKPASLSFEEACALPVVFLTVIDAFARAGL 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 185 QQGSSVAVYGA-GPVGLLTIACARLLGAEqIFVVDHHPYRLHFAADRYGAIPINFDEDsDPAQSIIEQTaGHRGVDAVID 263
Cdd:cd08251   119 AKGEHILIQTAtGGTGLMAVQLARLKGAE-IYATASSDDKLEYLKQLGVPHVINYVEE-DFEEEIMRLT-GGRGVDVVIN 195

                  ....*.
gi 1352184135 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 1352184135   8 GPHHVQVENVPDPGVEQaDDIILRITAtaiCG---SDLHLYRGKIPQ-VKHGDIFGHEFMGEVVETGKDVKNLQKGDRVV 83
Cdd:cd08275    10 GLDKLKVEKEALPEPSS-GEVRVRVEA---CGlnfADLMARQGLYDSaPKPPFVPGFECAGTVEAVGEGVKDFKVGDRVM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  84 ipfviaCGDCFfcrlqqyaacentnagkgaalnkkqipapaalfgyshlyggvpGGQAEYVRVPKGNVgpFKVPPLLS-D 162
Cdd:cd08275    86 ------GLTRF-------------------------------------------GGYAEVVNVPADQV--FPLPDGMSfE 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 163 DKALFLSDILpTAWQAA-KNAQIQQGSSVAVYGA-GPVGLLTIACARLLgaEQIFVV-DHHPYRLHFAADRYGAIPINFd 239
Cdd:cd08275   115 EAAAFPVNYL-TAYYALfELGNLRPGQSVLVHSAaGGVGLAAGQLCKTV--PNVTVVgTASASKHEALKENGVTHVIDY- 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 240 EDSDPAQSIIEQTAghRGVDAVIDAVGfeakGSTTETVLTNLK------LEGSSgkalrqCIAAVRRGGIVSVPGVY--- 310
Cdd:cd08275   191 RTQDYVEEVKKISP--EGVDIVLDALG----GEDTRKSYDLLKpmgrlvVYGAA------NLVTGEKRSWFKLAKKWwnr 258
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 311 ---------------AGFIHGFLFGDafDKGLSFKMGQthvhawlgeLLPLIEKGLLKPeeIVTHYMPFEEAARGYEIFE 375
Cdd:cd08275   259 pkvdpmklisenksvLGFNLGWLFEE--RELLTEVMDK---------LLKLYEEGKIKP--KIDSVFPFEEVGEAMRRLQ 325
                         410
                  ....*....|...
gi 1352184135 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 1352184135  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 1352184135 250 EQTAGHRGVDAVIDAVGfeakgsttetvltnlklegssGKALRQCIAAVRRGG-IVSVPGVYAGFIHGFLFGDAFDKGLS 328
Cdd:pfam13602  15 VQATGGEGVDVVLDTVG---------------------GEAFEASLRVLPGGGrLVTIGGPPLSAGLLLPARKRGGRGVK 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1352184135 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 1352184135   2 KALTYH---GPHHVQVENVPDPGVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDI-FGHEFMGEVVETGKDVKNLQ 77
Cdd:cd08247     2 KALTFKnntSPLTITTIKLPLPNCYKDNEIVVKVHAAALNPVDLKLYNSYTFHFKVKEKgLGRDYSGVIVKVGSNVASEW 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135  78 K-GDRVvipfviaCGDcffcrlqqyaacentnagkgaalnkkqipapaalfgYSHLYGGVpGGQAEYVRV-PKGNVGPF- 154
Cdd:cd08247    82 KvGDEV-------CGI------------------------------------YPHPYGGQ-GTLSQYLLVdPKKDKKSIt 117
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1352184135 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 1352184135 134 GGVPGGQAEYVRVPKGNVGPfkVPPLLSDDKALFLSDILPTAWQAAKNAQIQQGSSVAVYGA-GPVGLLTIACARLLGAE 212
Cdd:cd08244    92 GRAGGGYAELAVADVDSLHP--VPDGLDLEAAVAVVHDGRTALGLLDLATLTPGDVVLVTAAaGGLGSLLVQLAKAAGAT 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 213 QIFVVdHHPYRLHFAADRYGAIPINFDEDSDPAQsiIEQTAGHRGVDAVIDAVGfeakgsttetvltnlklegssGKALR 292
Cdd:cd08244   170 VVGAA-GGPAKTALVRALGADVAVDYTRPDWPDQ--VREALGGGGVTVVLDGVG---------------------GAIGR 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 293 QCIAAVRRGGIVSVPGVYAGFIHGFLFGDAFDKGLSF------KMGQTHVHAWLGELLPLIEKGLLKPeeIVTHYMPFEE 366
Cdd:cd08244   226 AALALLAPGGRFLTYGWASGEWTALDEDDARRRGVTVvgllgvQAERGGLRALEARALAEAAAGRLVP--VVGQTFPLER 303
                         250       260
                  ....*....|....*....|..
gi 1352184135 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 1352184135 138 GGQAEYVRVPkGNVGPFKVPPLLSDDKALFLSdIL----PTAWQAAKN-AQIQQGSSVAV-YGAGPVGLLTIACARLLGA 211
Cdd:cd05288    94 LGWQEYAVVD-GASGLRKLDPSLGLPLSAYLG-VLgmtgLTAYFGLTEiGKPKPGETVVVsAAAGAVGSVVGQIAKLLGA 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 212 ---------EQI-FVVDHhpyrLHF-AAdrygaipINFDEDsDPAQSIIEQTAGhrGVDAVIDAVGfeakGSTTETVLTN 280
Cdd:cd05288   172 rvvgiagsdEKCrWLVEE----LGFdAA-------INYKTP-DLAEALKEAAPD--GIDVYFDNVG----GEILDAALTL 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184135 281 LKLEGssgkalRqcIAAVrrGGI-------VSVPGVYAGFIH------GFLFGDAFDkglsfkmgqtHVHAWLGELLPLI 347
Cdd:cd05288   234 LNKGG------R--IALC--GAIsqynatePPGPKNLGNIITkrltmqGFIVSDYAD----------RFPEALAELAKWL 293
                         250
                  ....*....|...
gi 1352184135 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 1352184135  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 1352184135   1 MKALTYHGPHHVQVEN------VPDPgVEQADDIILRITATAICGSDLHLYRGKIPQVKHGDIFGHEFMGEVVETGKDVK 74
Cdd:cd08252     1 MKAIGFTQPLPITDPDslidieLPKP-VPGGRDLLVRVEAVSVNPVDTKVRAGGAPVPGQPKILGWDASGVVEAVGSEVT 79

                  ....*...
gi 1352184135  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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