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Conserved domains on  [gi|492052054|ref|WP_005733787|]
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MULTISPECIES: zinc-dependent alcohol dehydrogenase [Pseudomonas syringae group genomosp. 2]

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

EC:  1.1.1.-
Gene Ontology:  GO:0030554|GO:0004024|GO:0008270
PubMed:  19011745|19011751
SCOP:  3000040

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: 587.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQEADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGD 80
Cdd:cd08283    1 MKALVWHGKGDVRVEEVPDPKIEDPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGPEVRNLKVGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCFFCNIDLFAACETTNTGrgAIINKKSIPPGAALFGFSHLYGGIPGGQAEYVRVPKANVGPFKVPGTL 160
Cdd:cd08283   81 RVVVPFTIACGECFYCKRGLYSQCDNTNPS--AEMAKLYGHAGAGIFGYSHLTGGYAGGQAEYVRVPFADVGPFKIPDDL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 161 ADEKVLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKTYGVIPINFDD 240
Cdd:cd08283  159 SDEKALFLSDILPTGYHAAELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLGAETINFEE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 241 DDDPADTIIRQTAGmRGVDGVVDAVGFEAKGSTTETIL-ATLKLEGSSGKALRQCIAAVRRGGVVSVPGVYAGFIHGFMF 319
Cdd:cd08283  239 VDDVVEALRELTGG-RGPDVCIDAVGMEAHGSPLHKAEqALLKLETDRPDALREAIQAVRKGGTVSIIGVYGGTVNKFPI 317
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492052054 320 GDAFDKGLTFKMGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEEDCRKVILTP 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: 587.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQEADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGD 80
Cdd:cd08283    1 MKALVWHGKGDVRVEEVPDPKIEDPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGPEVRNLKVGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCFFCNIDLFAACETTNTGrgAIINKKSIPPGAALFGFSHLYGGIPGGQAEYVRVPKANVGPFKVPGTL 160
Cdd:cd08283   81 RVVVPFTIACGECFYCKRGLYSQCDNTNPS--AEMAKLYGHAGAGIFGYSHLTGGYAGGQAEYVRVPFADVGPFKIPDDL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 161 ADEKVLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKTYGVIPINFDD 240
Cdd:cd08283  159 SDEKALFLSDILPTGYHAAELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLGAETINFEE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 241 DDDPADTIIRQTAGmRGVDGVVDAVGFEAKGSTTETIL-ATLKLEGSSGKALRQCIAAVRRGGVVSVPGVYAGFIHGFMF 319
Cdd:cd08283  239 VDDVVEALRELTGG-RGPDVCIDAVGMEAHGSPLHKAEqALLKLETDRPDALREAIQAVRKGGTVSIIGVYGGTVNKFPI 317
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492052054 320 GDAFDKGLTFKMGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEEDCRKVILTP 388
Cdd:cd08283  318 GAAMNKGLTLRMGQTHVQRYLPRLLELIESGELDPSFIITHRLPLEDAPEAYKIFDKKEDGCIKVVLKP 386
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
1-389 1.54e-125

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: 366.39  E-value: 1.54e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIqEADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGD 80
Cdd:COG1063    1 MKALVLHGPGDLRLEEVPDPEP-GPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCFFCNIDLFAACETTNtgrgaiinkksippgaaLFGFSHlyggIPGGQAEYVRVPKANVgpFKVPGTL 160
Cdd:COG1063   80 RVVVEPNIPCGECRYCRRGRYNLCENLQ-----------------FLGIAG----RDGGFAEYVRVPAANL--VKVPDGL 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 161 ADEkVLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKtYGV-IPINFd 239
Cdd:COG1063  137 SDE-AAALVEPLAVALHAVERAGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARE-LGAdAVVNP- 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 240 DDDDPADTIIRQTAGmRGVDGVVDAVGFEAkgsttetilatlklegssgkALRQCIAAVRRGGVVSVPGVYAGFIhGFMF 319
Cdd:COG1063  214 REEDLVEAVRELTGG-RGADVVIEAVGAPA--------------------ALEQALDLVRPGGTVVLVGVPGGPV-PIDL 271
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 320 GDAFDKGLTFKMGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEEDCRKVILTPG 389
Cdd:COG1063  272 NALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPLITHRFPLDDAPEAFEAAADRADGAIKVVLDPD 341
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
1-388 1.47e-37

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 138.80  E-value: 1.47e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRAL--TYHGANSVKVDtVPDPEIQEaDDIILKVTATAICGSDLHLY------RGKIPTvehGDIFGHEFMGIVEETGPA 72
Cdd:PRK05396   1 MKALvkLKAEPGLWLTD-VPVPEPGP-NDVLIKVKKTAICGTDVHIYnwdewaQKTIPV---PMVVGHEFVGEVVEVGSE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  73 VTAVQKGDRVVIPFVIACGSCFFCNidlfaacettnTGRGAI-INKKSIppgaalfgfshlyG-GIPGGQAEYVRVPKAN 150
Cdd:PRK05396  76 VTGFKVGDRVSGEGHIVCGHCRNCR-----------AGRRHLcRNTKGV-------------GvNRPGAFAEYLVIPAFN 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 151 VgpFKVPGTLADEkvlfLSDILPTAWQAVTNAGIGQ--GSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQ 228
Cdd:PRK05396 132 V--WKIPDDIPDD----LAAIFDPFGNAVHTALSFDlvGEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELAR 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 229 KTYGVIPINfDDDDDPADTIirQTAGMR-GVDgvvdaVGFEAKGsttetilatlklegsSGKALRQCIAAVRRGGVVSVP 307
Cdd:PRK05396 206 KMGATRAVN-VAKEDLRDVM--AELGMTeGFD-----VGLEMSG---------------APSAFRQMLDNMNHGGRIAML 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 308 GVYAGFIhGFMFGDAFDKGLTFK------MGQThvHRFMPELLEhieaGRLEPEAIITHRMSLEDAAKGYKLFdkKEEDC 381
Cdd:PRK05396 263 GIPPGDM-AIDWNKVIFKGLTIKgiygreMFET--WYKMSALLQ----SGLDLSPIITHRFPIDDFQKGFEAM--RSGQS 333

                 ....*..
gi 492052054 382 RKVILTP 388
Cdd:PRK05396 334 GKVILDW 340
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
26-151 1.18e-35

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: 126.57  E-value: 1.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   26 DDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVIACGSCFFCNIDLFAACe 105
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYNLC- 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 492052054  106 ttntgrgaiinkksipPGAALFGFshlygGIPGGQAEYVRVPKANV 151
Cdd:pfam08240  80 ----------------PNGRFLGY-----DRDGGFAEYVVVPERNL 104
adh_fam_2 TIGR02822
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
17-212 1.61e-10

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: 61.86  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   17 VPDPEIQEaddIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIPFV-IACGSCFF 95
Cdd:TIGR02822  22 VPRPGPGE---LLVRVRACGVCRTDLHVSEGDLPVHRPRVTPGHEVVGEVAGRGADAGGFAVGDRVGIAWLrRTCGVCRY 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   96 CNidlfaacettntgRGAiinkKSIPPGAALFGFSHlyggiPGGQAEYVRVPKANVgpFKVPGTLADEKV--LFLSDILp 173
Cdd:TIGR02822  99 CR-------------RGA----ENLCPASRYTGWDT-----DGGYAEYTTVPAAFA--YRLPTGYDDVELapLLCAGII- 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 492052054  174 tAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAE 212
Cdd:TIGR02822 154 -GYRALLRASLPPGGRLGLYGFGGSAHLTAQVALAQGAT 191
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
31-373 2.01e-07

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 52.01  E-value: 2.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054    31 KVTATAICGSDLHLYRGKIPtveHGDIFGHEFMGIVEETGPAVTAVQKGDRVvipfviacgscffcnidlfaacettntg 110
Cdd:smart00829   2 EVRAAGLNFRDVLIALGLYP---GEAVLGGECAGVVTRVGPGVTGLAVGDRV---------------------------- 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   111 rgaiinkksippgaalFGFShlyggiPGGQAEYVRVPKANVgpFKVPGTLADEK-----VLFLsdilpTAWQA-VTNAGI 184
Cdd:smart00829  51 ----------------MGLA------PGAFATRVVTDARLV--VPIPDGWSFEEaatvpVVFL-----TAYYAlVDLARL 101
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   185 GQGSSVAIY-GAGPVGLMSAACARMLGAEkIFMVDHHPYRLTYAqKTYGVIP--------INFdddddpADTIIRQTAGm 255
Cdd:smart00829 102 RPGESVLIHaAAGGVGQAAIQLARHLGAE-VFATAGSPEKRDFL-RALGIPDdhifssrdLSF------ADEILRATGG- 172
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   256 RGVDgVVdavgfeakgsttetiLATLklegsSGKALRQCIAAVRRGGVvsvpgvyagFI---------HGFMFGDAFDKG 326
Cdd:smart00829 173 RGVD-VV---------------LNSL-----SGEFLDASLRCLAPGGR---------FVeigkrdirdNSQLAMAPFRPN 222
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 492052054   327 LTF------KM--GQTHVHRFMPELLEHIEAGRLEPeaIITHRMSLEDAAKGYKL 373
Cdd:smart00829 223 VSYhavdldALeeGPDRIRELLAEVLELFAEGVLRP--LPVTVFPISDAEDAFRY 275
 
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: 587.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQEADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGD 80
Cdd:cd08283    1 MKALVWHGKGDVRVEEVPDPKIEDPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGPEVRNLKVGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCFFCNIDLFAACETTNTGrgAIINKKSIPPGAALFGFSHLYGGIPGGQAEYVRVPKANVGPFKVPGTL 160
Cdd:cd08283   81 RVVVPFTIACGECFYCKRGLYSQCDNTNPS--AEMAKLYGHAGAGIFGYSHLTGGYAGGQAEYVRVPFADVGPFKIPDDL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 161 ADEKVLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKTYGVIPINFDD 240
Cdd:cd08283  159 SDEKALFLSDILPTGYHAAELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLGAETINFEE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 241 DDDPADTIIRQTAGmRGVDGVVDAVGFEAKGSTTETIL-ATLKLEGSSGKALRQCIAAVRRGGVVSVPGVYAGFIHGFMF 319
Cdd:cd08283  239 VDDVVEALRELTGG-RGPDVCIDAVGMEAHGSPLHKAEqALLKLETDRPDALREAIQAVRKGGTVSIIGVYGGTVNKFPI 317
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492052054 320 GDAFDKGLTFKMGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEEDCRKVILTP 388
Cdd:cd08283  318 GAAMNKGLTLRMGQTHVQRYLPRLLELIESGELDPSFIITHRLPLEDAPEAYKIFDKKEDGCIKVVLKP 386
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
1-388 4.43e-151

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: 431.31  E-value: 4.43e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQEADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGD 80
Cdd:cd05278    1 MKALVYLGPGKIGLEEVPDPKIQGPHDAIVRVTATSICGSDLHIYRGGVPGAKHGMILGHEFVGEVVEVGSDVKRLKPGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCFFCNIDLFAACETTNTGRGaiinkksippgaalfgfshLYGGIPGGQAEYVRVPKANVGPFKVPGTL 160
Cdd:cd05278   81 RVSVPCITFCGRCRFCRRGYHAHCENGLWGWK-------------------LGNRIDGGQAEYVRVPYADMNLAKIPDGL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 161 ADEKVLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKTYGVIPINFdD 240
Cdd:cd05278  142 PDEDALMLSDILPTGFHGAELAGIKPGSTVAVIGAGPVGLCAVAGARLLGAARIIAVDSNPERLDLAKEAGATDIINP-K 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 241 DDDPADTIIRQTAGmRGVDGVVDAVGFEAkgsttetilatlklegssgkALRQCIAAVRRGGVVSVPGVYAGFIHGFMFG 320
Cdd:cd05278  221 NGDIVEQILELTGG-RGVDCVIEAVGFEE--------------------TFEQAVKVVRPGGTIANVGVYGKPDPLPLLG 279
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492052054 321 DAFDKGLTFKMGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEEDCRKVILTP 388
Cdd:cd05278  280 EWFGKNLTFKTGLVPVRARMPELLDLIEEGKIDPSKLITHRFPLDDILKAYRLFDNKPDGCIKVVIRP 347
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
1-389 1.54e-125

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: 366.39  E-value: 1.54e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIqEADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGD 80
Cdd:COG1063    1 MKALVLHGPGDLRLEEVPDPEP-GPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCFFCNIDLFAACETTNtgrgaiinkksippgaaLFGFSHlyggIPGGQAEYVRVPKANVgpFKVPGTL 160
Cdd:COG1063   80 RVVVEPNIPCGECRYCRRGRYNLCENLQ-----------------FLGIAG----RDGGFAEYVRVPAANL--VKVPDGL 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 161 ADEkVLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKtYGV-IPINFd 239
Cdd:COG1063  137 SDE-AAALVEPLAVALHAVERAGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARE-LGAdAVVNP- 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 240 DDDDPADTIIRQTAGmRGVDGVVDAVGFEAkgsttetilatlklegssgkALRQCIAAVRRGGVVSVPGVYAGFIhGFMF 319
Cdd:COG1063  214 REEDLVEAVRELTGG-RGADVVIEAVGAPA--------------------ALEQALDLVRPGGTVVLVGVPGGPV-PIDL 271
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 320 GDAFDKGLTFKMGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEEDCRKVILTPG 389
Cdd:COG1063  272 NALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPLITHRFPLDDAPEAFEAAADRADGAIKVVLDPD 341
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
1-388 4.62e-123

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: 361.14  E-value: 4.62e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQEADDIILKVTATAICGSDLHLYRGKIpTVEHGDIFGHEFMGIVEETGPAVTAVQKGD 80
Cdd:cd08282    1 MKAVVYGGPGNVAVEDVPDPKIEHPTDAIVRITTTAICGSDLHMYRGRT-GAEPGLVLGHEAMGEVEEVGSAVESLKVGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCFFCNIDLFAACETTNTGrgaiinkksiPPGAALFGFShlYGGIPGGQAEYVRVPKANVGPFKVPGTL 160
Cdd:cd08282   80 RVVVPFNVACGRCRNCKRGLTGVCLTVNPG----------RAGGAYGYVD--MGPYGGGQAEYLRVPYADFNLLKLPDRD 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 161 ADEKV---LFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAqKTYGVIPIN 237
Cdd:cd08282  148 GAKEKddyLMLSDIFPTGWHGLELAGVQPGDTVAVFGAGPVGLMAAYSAILRGASRVYVVDHVPERLDLA-ESIGAIPID 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 238 FdDDDDPADTIIRQTAGmrGVDGVVDAVGFEAKGSttetilatlKLEGSSGKALRQCIAAVRRGGVVSVPGVYAGF---- 313
Cdd:cd08282  227 F-SDGDPVEQILGLEPG--GVDRAVDCVGYEARDR---------GGEAQPNLVLNQLIRVTRPGGGIGIVGVYVAEdpga 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 314 -----IHG---FMFGDAFDKGLTFKMGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEEDcrKVI 385
Cdd:cd08282  295 gdaaaKQGelsFDFGLLWAKGLSFGTGQAPVKKYNRQLRDLILAGRAKPSFVVSHVISLEDAPEAYARFDKRLET--KVV 372

                 ...
gi 492052054 386 LTP 388
Cdd:cd08282  373 IKP 375
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
1-388 1.58e-116

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: 343.47  E-value: 1.58e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQEADDIILKVTATAICGSDLHLYRGKIPtVEHGDIFGHEFMGIVEETGPAVTAVQKGD 80
Cdd:cd08284    1 MKAVVFKGPGDVRVEEVPIPQIQDPTDAIVKVTAAAICGSDLHIYRGHIP-STPGFVLGHEFVGEVVEVGPEVRTLKVGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCFFCNIDLFAACETTNtgrgaiinkksippgaaLFGFShLYGGIPGGQAEYVRVPKANVGPFKVPGTL 160
Cdd:cd08284   80 RVVSPFTIACGECFYCRRGQSGRCAKGG-----------------LFGYA-GSPNLDGAQAEYVRVPFADGTLLKLPDGL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 161 ADEKVLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAqKTYGVIPINFdD 240
Cdd:cd08284  142 SDEAALLLGDILPTGYFGAKRAQVRPGDTVAVIGCGPVGLCAVLSAQVLGAARVFAVDPVPERLERA-AALGAEPINF-E 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 241 DDDPADTIIRQTAGmRGVDGVVDAVGfeakgsttetilatlklegsSGKALRQCIAAVRRGGVVSVPGVYAGfiHGFMF- 319
Cdd:cd08284  220 DAEPVERVREATEG-RGADVVLEAVG--------------------GAAALDLAFDLVRPGGVISSVGVHTA--EEFPFp 276
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 320 -GDAFDKGLTFKMGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEEdcRKVILTP 388
Cdd:cd08284  277 gLDAYNKNLTLRFGRCPVRSLFPELLPLLESGRLDLEFLIDHRMPLEEAPEAYRLFDKRKV--LKVVLDP 344
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
1-388 3.47e-79

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: 247.99  E-value: 3.47e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQEADDIILKVTATAICGSDLHLYRGKIPTVEHGDIfGHEFMGIVEETGPAVTAVQKGD 80
Cdd:cd08287    1 MRATVIHGPGDIRVEEVPDPVIEEPTDAVIRVVATCVCGSDLWPYRGVSPTRAPAPI-GHEFVGVVEEVGSEVTSVKPGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCFFCNIDLFAACettntgrgaiinkksipPGAALFGfshlyGGIPGGQAEYVRVPKANVGPFKVPGTL 160
Cdd:cd08287   80 FVIAPFAISDGTCPFCRAGFTTSC-----------------VHGGFWG-----AFVDGGQGEYVRVPLADGTLVKVPGSP 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 161 ADEK-----VLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKtYGVIP 235
Cdd:cd08287  138 SDDEdllpsLLALSDVMGTGHHAAVSAGVRPGSTVVVVGDGAVGLCAVLAAKRLGAERIIAMSRHEDRQALARE-FGATD 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 236 INFDDDDDPADTIIRQTAGMrGVDGVVDAVGfeakgsttetilatlklegsSGKALRQCIAAVRRGGVVSVPGVYAGFIh 315
Cdd:cd08287  217 IVAERGEEAVARVRELTGGV-GADAVLECVG--------------------TQESMEQAIAIARPGGRVGYVGVPHGGV- 274
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492052054 316 GFMFGDAFDKGLTFKMGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDkkEEDCRKVILTP 388
Cdd:cd08287  275 ELDVRELFFRNVGLAGGPAPVRRYLPELLDDVLAGRINPGRVFDLTLPLDEVAEGYRAMD--ERRAIKVLLRP 345
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
1-387 4.57e-79

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: 247.55  E-value: 4.57e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQEADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGD 80
Cdd:cd08286    1 MKALVYHGPGKISWEDRPKPTIQEPTDAIVKMLKTTICGTDLHILKGDVPTVTPGRILGHEGVGVVEEVGSAVTNFKVGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCFFCNIDLFAACETtntgrgaiinkksippGAALFGfsHLyggIPGGQAEYVRVPKANVGPFKVPGTL 160
Cdd:cd08286   81 RVLISCISSCGTCGYCRKGLYSHCES----------------GGWILG--NL---IDGTQAEYVRIPHADNSLYKLPEGV 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 161 ADEKVLFLSDILPTAWQ-AVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKTYGVIPINfD 239
Cdd:cd08286  140 DEEAAVMLSDILPTGYEcGVLNGKVKPGDTVAIVGAGPVGLAALLTAQLYSPSKIIMVDLDDNRLEVAKKLGATHTVN-S 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 240 DDDDPADTIIRQTAGmRGVDGVVDAVGfeakgsttetILATLKLegssgkalrqCIAAVRRGGVVSVPGVyagfiHG--- 316
Cdd:cd08286  219 AKGDAIEQVLELTDG-RGVDVVIEAVG----------IPATFEL----------CQELVAPGGHIANVGV-----HGkpv 272
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492052054 317 -FMFGDAFDKGLTFKMGQTHVHRfMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLF-DKKEEDCRKVILT 387
Cdd:cd08286  273 dLHLEKLWIKNITITTGLVDTNT-TPMLLKLVSSGKLDPSKLVTHRFKLSEIEKAYDTFsAAAKHKALKVIID 344
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
1-387 5.21e-59

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: 195.51  E-value: 5.21e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQEaDDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGD 80
Cdd:cd08235    1 MKAAVLHGPNDVRLEEVPVPEPGP-GEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGDGVTGFKVGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCFFCNIDLFAACETtntgrgaiinkksippgaaLFGFSHLYggiPGGQAEYVRVPKANV---GPFKVP 157
Cdd:cd08235   80 RVFVAPHVPCGECHYCLRGNENMCPN-------------------YKKFGNLY---DGGFAEYVRVPAWAVkrgGVLKLP 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 158 GTLADEkVLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKTYGVIPIN 237
Cdd:cd08235  138 DNVSFE-EAALVEPLACCINAQRKAGIKPGDTVLVIGAGPIGLLHAMLAKASGARKVIVSDLNEFRLEFAKKLGADYTID 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 238 fDDDDDPADTIIRQTAGmRGVDGVvdavgfeakgsttetILATlklegSSGKALRQCIAAVRRGGVVSvpgVYAGFIHGF 317
Cdd:cd08235  217 -AAEEDLVEKVRELTDG-RGADVV---------------IVAT-----GSPEAQAQALELVRKGGRIL---FFGGLPKGS 271
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492052054 318 M----FGDAFDKGLTFKMGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEEdcRKVILT 387
Cdd:cd08235  272 TvnidPNLIHYREITITGSYAASPEDYKEALELIASGKIDVKDLITHRFPLEDIEEAFELAADGKS--LKIVIT 343
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
1-386 1.69e-58

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: 194.37  E-value: 1.69e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQeADDIILKVTATAICGSDLHLYRGKIPTVeHGDIFGHEFMGIVEETGPAVTAVQKGD 80
Cdd:cd08236    1 MKALVLTGPGDLRYEDIPKPEPG-PGEVLVKVKACGICGSDIPRYLGTGAYH-PPLVLGHEFSGTVEEVGSGVDDLAVGD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCFFCNIDLFAACettnTGRGaiinkksippgaaLFGfSHLyggiPGGQAEYVRVPKANVgpFKVPGTL 160
Cdd:cd08236   79 RVAVNPLLPCGKCEYCKKGEYSLC----SNYD-------------YIG-SRR----DGAFAEYVSVPARNL--IKIPDHV 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 161 ADEKVLFLsDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAqKTYGV-IPINfd 239
Cdd:cd08236  135 DYEEAAMI-EPAAVALHAVRLAGITLGDTVVVIGAGTIGLLAIQWLKILGAKRVIAVDIDDEKLAVA-RELGAdDTIN-- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 240 DDDDPADTIIRQTAGmRGVDGVVDAVGfeakgsttetilatlklegsSGKALRQCIAAVRRGGVVsvpgVYAG------F 313
Cdd:cd08236  211 PKEEDVEKVRELTEG-RGADLVIEAAG--------------------SPATIEQALALARPGGKV----VLVGipygdvT 265
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492052054 314 IHGFMFGDAFDKGLTFK-----MGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEEDCRKVIL 386
Cdd:cd08236  266 LSEEAFEKILRKELTIQgswnsYSAPFPGDEWRTALDLLASGKIKVEPLITHRLPLEDGPAAFERLADREEFSGKVLL 343
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
1-385 3.95e-58

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 193.02  E-value: 3.95e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANS-VKVDTVPDPEIqEADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKG 79
Cdd:COG1064    1 MKAAVLTEPGGpLELEEVPRPEP-GPGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGVTGFKVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  80 DRVVIPFVIACGSCFFCNIDLFAACETtntgrgaiinkksippgAALFGFSHlyggiPGGQAEYVRVPKANVgpFKVPGT 159
Cdd:COG1064   80 DRVGVGWVDSCGTCEYCRSGRENLCEN-----------------GRFTGYTT-----DGGYAEYVVVPARFL--VKLPDG 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 160 LADEKVLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEkIFMVDHHPYRLTYAqKTYG---VIPI 236
Cdd:COG1064  136 LDPAEAAPLLCAGITAYRALRRAGVGPGDRVAVIGAGGLGHLAVQIAKALGAE-VIAVDRSPEKLELA-RELGadhVVNS 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 237 NfdddddpADTIIRQTAGMRGVDGVVDAVGfeakgsttetilatlklegsSGKALRQCIAAVRRGGVVSVPGVYAGFIHG 316
Cdd:COG1064  214 S-------DEDPVEAVRELTGADVVIDTVG--------------------APATVNAALALLRRGGRLVLVGLPGGPIPL 266
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492052054 317 FMFgDAFDKGLTFK----MGQTHvhrfMPELLEHIEAGRLEPEaiiTHRMSLEDAAKGYKLFDKKEEDCRKVI 385
Cdd:COG1064  267 PPF-DLILKERSIRgsliGTRAD----LQEMLDLAAEGKIKPE---VETIPLEEANEALERLRAGKVRGRAVL 331
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
1-387 3.97e-57

(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: 190.83  E-value: 3.97e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQeADDIILKVTATAICGSDLHLYRGK---IPTVEHGDI--------FGHEFMGIVEET 69
Cdd:cd08233    1 MKAARYHGRKDIRVEEVPEPPVK-PGEVKIKVAWCGICGSDLHEYLDGpifIPTEGHPHLtgetapvtLGHEFSGVVVEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  70 GPAVTAVQKGDRVVIPFVIACGSCFFCNIDLFAACETtntgrgaiinkksippgaalFGFSHLyGGIPGGQAEYVRVPKA 149
Cdd:cd08233   80 GSGVTGFKVGDRVVVEPTIKCGTCGACKRGLYNLCDS--------------------LGFIGL-GGGGGGFAEYVVVPAY 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 150 NVgpFKVPGTLADEkVLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQK 229
Cdd:cd08233  139 HV--HKLPDNVPLE-EAALVEPLAVAWHAVRRSGFKPGDTALVLGAGPIGLLTILALKAAGASKIIVSEPSEARRELAEE 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 230 TYGVIPINFDDDDDPAdtIIRQTAGMRGVDgvvdaVGFEAKGSTtetilatlklegssgKALRQCIAAVRRGGVVSVPGV 309
Cdd:cd08233  216 LGATIVLDPTEVDVVA--EVRKLTGGGGVD-----VSFDCAGVQ---------------ATLDTAIDALRPRGTAVNVAI 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 310 YAGFIhGFMFGDAFDKGLTFKMGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDA-AKGYK-LFDKKEEDCrKVILT 387
Cdd:cd08233  274 WEKPI-SFNPNDLVLKEKTLTGSICYTREDFEEVIDLLASGKIDAEPLITSRIPLEDIvEKGFEeLINDKEQHV-KILVS 351
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
1-385 1.46e-55

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: 186.19  E-value: 1.46e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQEaDDIILKVTATAICGSDLHLYRG----KIPTVehgdiFGHEFMGIVEETGPAVTAV 76
Cdd:cd08234    1 MKALVYEGPGELEVEEVPVPEPGP-DEVLIKVAACGICGTDLHIYEGefgaAPPLV-----PGHEFAGVVVAVGSKVTGF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  77 QKGDRVVIPFVIACGSCFFCNIDLFAACEttntgrgaiinkksippgaalfgfsHLYG---GIPGGQAEYVRVPKANVgp 153
Cdd:cd08234   75 KVGDRVAVDPNIYCGECFYCRRGRPNLCE-------------------------NLTAvgvTRNGGFAEYVVVPAKQV-- 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 154 FKVPGTLADEKVLFLsDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKTYGV 233
Cdd:cd08234  128 YKIPDNLSFEEAALA-EPLSCAVHGLDLLGIKPGDSVLVFGAGPIGLLLAQLLKLNGASRVTVAEPNEEKLELAKKLGAT 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 234 IPINfdddDDPADTIIRQTAGMRGVDGVVDAVGfeakgsttetilatlklegsSGKALRQCIAAVRRGGVVSVPGVYAgf 313
Cdd:cd08234  207 ETVD----PSREDPEAQKEDNPYGFDVVIEATG--------------------VPKTLEQAIEYARRGGTVLVFGVYA-- 260
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492052054 314 iHGFMFG----DAFDKGLTFK--MGQTHVHrfmPELLEHIEAGRLEPEAIITHRMSLEDAAKGykLFDKKEEDCRKVI 385
Cdd:cd08234  261 -PDARVSispfEIFQKELTIIgsFINPYTF---PRAIALLESGKIDVKGLVSHRLPLEEVPEA--LEGMRSGGALKVV 332
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
1-388 4.66e-55

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: 185.52  E-value: 4.66e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQeADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGD 80
Cdd:cd08285    1 MKAFAMLGIGKVGWIEKPIPVCG-PNDAIVRPTAVAPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGSEVKDFKPGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCffcnidlfaacettntgrgaiinkksippGAALFGFSHLYGGIPGG----------QAEYVRVPKAN 150
Cdd:cd08285   80 RVIVPAITPDWRS-----------------------------VAAQRGYPSQSGGMLGGwkfsnfkdgvFAEYFHVNDAD 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 151 VGPFKVPGTLADEKVLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKt 230
Cdd:cd08285  131 ANLAPLPDGLTDEQAVMLPDMMSTGFHGAELANIKLGDTVAVFGIGPVGLMAVAGARLRGAGRIIAVGSRPNRVELAKE- 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 231 YGVIPINFDDDDDPADTIIRQTAGmRGVDGVVDAVGfeakgsTTETilatlklegssgkaLRQCIAAVRRGGVVSVPGVY 310
Cdd:cd08285  210 YGATDIVDYKNGDVVEQILKLTGG-KGVDAVIIAGG------GQDT--------------FEQALKVLKPGGTISNVNYY 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 311 AGFIHGFMFGDAFDKGltfkMGQTHVH--------RFMPELLEHIEAGRLEPEAIITHRM-SLEDAAKGYKLFDKKEEDC 381
Cdd:cd08285  269 GEDDYLPIPREEWGVG----MGHKTINgglcpggrLRMERLASLIEYGRVDPSKLLTHHFfGFDDIEEALMLMKDKPDDL 344

                 ....*..
gi 492052054 382 RKVILTP 388
Cdd:cd08285  345 IKPVIIF 351
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
1-387 3.64e-54

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: 182.77  E-value: 3.64e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIqEADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGD 80
Cdd:cd08261    1 MKALVCEKPGRLEVVDIPEPVP-GAGEVLVRVKRVGICGSDLHIYHGRNPFASYPRILGHELSGEVVEVGEGVAGLKVGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCFFCNIDLFAACETTNTgrgaiinkksippgaalFGfSHlyggIPGGQAEYVRVPKANVgpfKVPGTL 160
Cdd:cd08261   80 RVVVDPYISCGECYACRKGRPNCCENLQV-----------------LG-VH----RDGGFAEYIVVPADAL---LVPEGL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 161 ADEKvLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAeKIFMVDHHPYRLTYAQKTYGVIPINfDD 240
Cdd:cd08261  135 SLDQ-AALVEPLAIGAHAVRRAGVTAGDTVLVVGAGPIGLGVIQVAKARGA-RVIVVDIDDERLEFARELGADDTIN-VG 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 241 DDDPADTIIRQTAGmRGVDGVVDAVGfeakgsttetilatlklegsSGKALRQCIAAVRRGGVVSVPGVYAGFIhgfmfg 320
Cdd:cd08261  212 DEDVAARLRELTDG-EGADVVIDATG--------------------NPASMEEAVELVAHGGRVVLVGLSKGPV------ 264
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492052054 321 dAF-DKGLTFK----MGQTHVHRFM-PELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEEDCRKVILT 387
Cdd:cd08261  265 -TFpDPEFHKKeltiLGSRNATREDfPDVIDLLESGKVDPEALITHRFPFEDVPEAFDLWEAPPGGVIKVLIE 336
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
1-388 3.08e-51

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: 175.20  E-value: 3.08e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQeADDIILKVTATAICGSDLHLYRGKIPTVEHGDIF-GHEFMGIVEETGPAVTAVQKG 79
Cdd:cd08239    1 MRGAVFPGDRTVELREFPVPVPG-PGEVLLRVKASGLCGSDLHYYYHGHRAPAYQGVIpGHEPAGVVVAVGPGVTHFRVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  80 DRVVIPFVIACGSCFFCNidlfaacettntgRGAIINKKSippGAALFGFSHlyggiPGGQAEYVRVPKANVgpFKVPGT 159
Cdd:cd08239   80 DRVMVYHYVGCGACRNCR-------------RGWMQLCTS---KRAAYGWNR-----DGGHAEYMLVPEKTL--IPLPDD 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 160 LADEKVLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKtYGVIPInFD 239
Cdd:cd08239  137 LSFADGALLLCGIGTAYHALRRVGVSGRDTVLVVGAGPVGLGALMLARALGAEDVIGVDPSPERLELAKA-LGADFV-IN 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 240 DDDDPADTIIRQTAGmRGVDGVVDAVGFEAkgsttetilatlklegssgkALRQCIAAVRRGGVVSVPGVYAGFihgfmf 319
Cdd:cd08239  215 SGQDDVQEIRELTSG-AGADVAIECSGNTA--------------------ARRLALEAVRPWGRLVLVGEGGEL------ 267
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492052054 320 gdAFDKGLTFKMGQTHVHR-------FMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEedCRKVILTP 388
Cdd:cd08239  268 --TIEVSNDLIRKQRTLIGswyfsvpDMEECAEFLARHKLEVDRLVTHRFGLDQAPEAYALFAQGE--SGKVVFVF 339
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
27-347 3.28e-50

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: 170.58  E-value: 3.28e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  27 DIILKVTATAICGSDLHLYRGK-IPTVEHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVIACGSCFFCnidlfaace 105
Cdd:cd05188    1 EVLVRVEAAGLCGTDLHIRRGGyPPPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNLGCGTCELC--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 106 ttntgrgaiinkKSIPPGAALFGFshlygGIPGGQAEYVRVPKANVgpFKVPGTLADEKVLFLSDILPTAWQAV-TNAGI 184
Cdd:cd05188   72 ------------RELCPGGGILGE-----GLDGGFAEYVVVPADNL--VPLPDGLSLEEAALLPEPLATAYHALrRAGVL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 185 GQGSSVAIYGAGPVGLMSAACARMLGAeKIFMVDHHPYRLTYAQKTYGVIPINFDDDDDPADtiIRQTAGmRGVDGVVDA 264
Cdd:cd05188  133 KPGDTVLVLGAGGVGLLAAQLAKAAGA-RVIVTDRSDEKLELAKELGADHVIDYKEEDLEEE--LRLTGG-GGADVVIDA 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 265 VGFEAkgsttetilatlklegssgkALRQCIAAVRRGGVVSVPGVYAGFIHGFMFGDAFDKGLTFK--MGQThvHRFMPE 342
Cdd:cd05188  209 VGGPE--------------------TLAQALRLLRPGGRIVVVGGTSGGPPLDDLRRLLFKELTIIgsTGGT--REDFEE 266

                 ....*
gi 492052054 343 LLEHI 347
Cdd:cd05188  267 ALDLL 271
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
1-368 9.93e-48

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: 166.24  E-value: 9.93e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSV-KVDTVPDPEIqEADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKG 79
Cdd:cd08260    1 MRAAVYEEFGEPlEIREVPDPEP-PPDGVVVEVEACGVCRSDWHGWQGHDPDVTLPHVPGHEFAGVVVEVGEDVSRWRVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  80 DRVVIPFVIACGSCFFCNidlfaacettnTGRGAIINKKSIPpgaalfGFSHlyggiPGGQAEYVRVPKANVGPFKVPGT 159
Cdd:cd08260   80 DRVTVPFVLGCGTCPYCR-----------AGDSNVCEHQVQP------GFTH-----PGSFAEYVAVPRADVNLVRLPDD 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 160 LADEKVLFLSDILPTAWQAVTN-AGIGQGSSVAIYGAGPVGLMSAACARMLGAeKIFMVDHHPYRLTYAQKTYGVIPINF 238
Cdd:cd08260  138 VDFVTAAGLGCRFATAFRALVHqARVKPGEWVAVHGCGGVGLSAVMIASALGA-RVIAVDIDDDKLELARELGAVATVNA 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 239 DDDDDPADTIIRQTAGmrGVDGVVDAVGFEAkgsttetilatlklegssgkALRQCIAAVRRGG-VVSVpgvyagfihGF 317
Cdd:cd08260  217 SEVEDVAAAVRDLTGG--GAHVSVDALGIPE--------------------TCRNSVASLRKRGrHVQV---------GL 265
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492052054 318 MFGDafDKGLTFKMGQ----------TH---VHRFmPELLEHIEAGRLEPEAIITHRMSLEDAA 368
Cdd:cd08260  266 TLGE--EAGVALPMDRvvareleivgSHgmpAHRY-DAMLALIASGKLDPEPLVGRTISLDEAP 326
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
1-388 1.89e-47

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: 165.48  E-value: 1.89e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALT-YHGANSVKVDTVPDPEIQEaDDIILKVTATAICGSDLHLY--------RGKIPTvehgdIFGHEFMGIVEETGP 71
Cdd:cd05281    1 MKAIVkTKAGPGAELVEVPVPKPGP-GEVLIKVLAASICGTDVHIYewdewaqsRIKPPL-----IFGHEFAGEVVEVGE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  72 AVTAVQKGDRVVIPFVIACGSCFFCNidlfaacettnTGRGAIINKKSIppgaalFGFShlyggIPGGQAEYVRVPKANV 151
Cdd:cd05281   75 GVTRVKVGDYVSAETHIVCGKCYQCR-----------TGNYHVCQNTKI------LGVD-----TDGCFAEYVVVPEENL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 152 gpFKVPGTLADEkVLFLSDILPTAWQAVTNAGIgQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKTY 231
Cdd:cd05281  133 --WKNDKDIPPE-IASIQEPLGNAVHTVLAGDV-SGKSVLITGCGPIGLMAIAVAKAAGASLVIASDPNPYRLELAKKMG 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 232 GVIPINfdddddPADTIIRQTAGMRGVDGvVDAVgfeakgsttetilatLKLEGSSgKALRQCIAAVRRGGVVSVPGVYA 311
Cdd:cd05281  209 ADVVIN------PREEDVVEVKSVTDGTG-VDVV---------------LEMSGNP-KAIEQGLKALTPGGRVSILGLPP 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 312 GFIHGFMFGDAFDKGLTF------KMGQThvHRFMPELLehiEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEedCRKVI 385
Cdd:cd05281  266 GPVDIDLNNLVIFKGLTVqgitgrKMFET--WYQVSALL---KSGKVDLSPVITHKLPLEDFEEAFELMRSGK--CGKVV 338

                 ...
gi 492052054 386 LTP 388
Cdd:cd05281  339 LYP 341
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
25-373 2.87e-47

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 165.26  E-value: 2.87e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  25 ADDIILKVTATAICGSDLHLYRGKIPT---VehgdIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVIACGSCFFCNIDLF 101
Cdd:COG1062   16 PGEVLVRIVAAGLCHSDLHVRDGDLPVplpA----VLGHEGAGVVEEVGPGVTGVAPGDHVVLSFIPSCGHCRYCASGRP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 102 AACEttntgRGAIINKKSIPP----------GAALFGFSHLyggipGGQAEYVRVPKANVgpFKVPGTLADEKVLFLSDI 171
Cdd:COG1062   92 ALCE-----AGAALNGKGTLPdgtsrlssadGEPVGHFFGQ-----SSFAEYAVVPERSV--VKVDKDVPLELAALLGCG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 172 LPTAWQAVTN-AGIGQGSSVAIYGAGPVGLmsAAC--ARMLGAEKIFMVDHHPYRLTYAQK---TYGVIPINfdddDDPA 245
Cdd:COG1062  160 VQTGAGAVLNtAKVRPGDTVAVFGLGGVGL--SAVqgARIAGASRIIAVDPVPEKLELARElgaTHTVNPAD----EDAV 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 246 DTIIRQTAGmrGVDGVVDAVGfeakgsttetilatlklegsSGKALRQCIAAVRRGG---VVSVPGVYAGF-IHGFMFgd 321
Cdd:COG1062  234 EAVRELTGG--GVDYAFETTG--------------------NPAVIRQALEALRKGGtvvVVGLAPPGAEIsLDPFQL-- 289
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492052054 322 aFDKGLTFK---MGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKL 373
Cdd:COG1062  290 -LLTGRTIRgsyFGGAVPRRDIPRLVDLYRAGRLPLDELITRRYPLDEINEAFDD 343
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
3-385 3.54e-46

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: 161.89  E-value: 3.54e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   3 ALTYHGANSVKVDTVPDPEIQEaDDIILKVTATAICGSDLHLYR-GKI--PTVEHGDIFGHEFMGIVEETGPAVTAVQKG 79
Cdd:cd05285    1 AAVLHGPGDLRLEERPIPEPGP-GEVLVRVRAVGICGSDVHYYKhGRIgdFVVKEPMVLGHESAGTVVAVGSGVTHLKVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  80 DRVVIPFVIACGSCFFC-----NID---LFAACettntgrgaiinkksiPPgaalfgfshlyggIPGGQAEYVRVPKANV 151
Cdd:cd05285   80 DRVAIEPGVPCRTCEFCksgryNLCpdmRFAAT----------------PP-------------VDGTLCRYVNHPADFC 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 152 gpFKVPGTLADEK-VLF--LSdilpTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAq 228
Cdd:cd05285  131 --HKLPDNVSLEEgALVepLS----VGVHACRRAGVRPGDTVLVFGAGPIGLLTAAVAKAFGATKVVVTDIDPSRLEFA- 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 229 KTYG---VIPINFDDDDDPADTIIRQTAGMrGVDGVVDAVGFEakgsttetilatlklegssgKALRQCIAAVRRGGVVS 305
Cdd:cd05285  204 KELGathTVNVRTEDTPESAEKIAELLGGK-GPDVVIECTGAE--------------------SCIQTAIYATRPGGTVV 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 306 VPGVYAGFIHgFMFGDAFDKGLTFKmgqtHVHRFM---PELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEEDCR 382
Cdd:cd05285  263 LVGMGKPEVT-LPLSAASLREIDIR----GVFRYAntyPTAIELLASGKVDVKPLITHRFPLEDAVEAFETAAKGKKGVI 337

                 ...
gi 492052054 383 KVI 385
Cdd:cd05285  338 KVV 340
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
16-371 1.06e-44

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: 158.47  E-value: 1.06e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  16 TVPDPEiqeADDIILKVTATAICGSDLHLYRGKIPT---VehgdIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVIACGS 92
Cdd:cd08279   19 ELDDPG---PGEVLVRIAAAGLCHSDLHVVTGDLPAplpA----VLGHEGAGVVEEVGPGVTGVKPGDHVVLSWIPACGT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  93 CFFCNIDLFAACEttntgRGAIINKKSIPPGAALFGFS----HLYGGIpGGQAEYVRVPKANVGpfKVPGTLADEKVLFL 168
Cdd:cd08279   92 CRYCSRGQPNLCD-----LGAGILGGQLPDGTRRFTADgepvGAMCGL-GTFAEYTVVPEASVV--KIDDDIPLDRAALL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 169 SDILPTAWQAVTN-AGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQK---TYGVIPINfdddDDP 244
Cdd:cd08279  164 GCGVTTGVGAVVNtARVRPGDTVAVIGCGGVGLNAIQGARIAGASRIIAVDPVPEKLELARRfgaTHTVNASE----DDA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 245 ADTIIRQTAGmRGVDGVVDAVGfeakgsTTETIlatlklegssgkalRQCIAAVRRGGVVSVPGVYAGF----IHGFMFG 320
Cdd:cd08279  240 VEAVRDLTDG-RGADYAFEAVG------RAATI--------------RQALAMTRKGGTAVVVGMGPPGetvsLPALELF 298
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 492052054 321 dAFDKGLT-FKMGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGY 371
Cdd:cd08279  299 -LSEKRLQgSLYGSANPRRDIPRLLDLYRAGRLKLDELVTRRYSLDEINEAF 349
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
2-369 2.54e-39

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: 144.32  E-value: 2.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   2 RALTYHGANS-VKVDTVPDPEIqEADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTA----- 75
Cdd:cd08231    2 RAAVLTGPGKpLEIREVPLPDL-EPGAVLVRVRLAGVCGSDVHTVAGRRPRVPLPIILGHEGVGRVVALGGGVTTdvage 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  76 -VQKGDRVVIPFVIACGSCFFCNIDLFAACETtntGRGAIINKKSIPPgaalfgfsHLYGGIpggqAEYVRVPkANVGPF 154
Cdd:cd08231   81 pLKVGDRVTWSVGAPCGRCYRCLVGDPTKCEN---RKKYGHEASCDDP--------HLSGGY----AEHIYLP-PGTAIV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 155 KVPGTLADEKVLFLSDILPTAWQAVTNAG-IGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKTYGV 233
Cdd:cd08231  145 RVPDNVPDEVAAPANCALATVLAALDRAGpVGAGDTVVVQGAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAREFGAD 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 234 IPINFDDDDDPADT-IIRQTAGMRGVDGVVDAVGfeakgsttetilatlklegsSGKALRQCIAAVRRGGVVSVPGVYAG 312
Cdd:cd08231  225 ATIDIDELPDPQRRaIVRDITGGRGADVVIEASG--------------------HPAAVPEGLELLRRGGTYVLVGSVAP 284
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492052054 313 ------FIHGFMFGDAFDKGLTFkmGQTHVHRFMPELLEHiEAGRLEPEAIITHRMSLEDAAK 369
Cdd:cd08231  285 agtvplDPERIVRKNLTIIGVHN--YDPSHLYRAVRFLER-TQDRFPFAELVTHRYPLEDINE 344
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
1-386 5.82e-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. 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: 143.28  E-value: 5.82e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANS-VKVDTVPDPEIQEADdIILKVTATAICGSDLHLYRGKIPtVEHGDIFGHEFMGIVEETGPAVT---AV 76
Cdd:cd08263    1 MKAAVLKGPNPpLTIEEIPVPRPKEGE-ILIRVAACGVCHSDLHVLKGELP-FPPPFVLGHEISGEVVEVGPNVEnpyGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  77 QKGDRVVIPFVIACGSCFFC---NIDLfaaCE---TTNTGRGAIINKKSIPPGAalfGFSHLYGGIPGGQAEYVRVPKAN 150
Cdd:cd08263   79 SVGDRVVGSFIMPCGKCRYCargKENL---CEdffAYNRLKGTLYDGTTRLFRL---DGGPVYMYSMGGLAEYAVVPATA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 151 VgpFKVPGTLADEKVLFLSDILPTAWQAVTNAGIGQ-GSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQK 229
Cdd:cd08263  153 L--APLPESLDYTESAVLGCAGFTAYGALKHAADVRpGETVAVIGVGGVGSSAIQLAKAFGASPIIAVDVRDEKLAKAKE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 230 TYGVIPINFDDDDDPADtiIRQTAGMRGVDgvvdaVGFEAKGStTETILATLKLEGSSGKALRQCIAA------------ 297
Cdd:cd08263  231 LGATHTVNAAKEDAVAA--IREITGGRGVD-----VVVEALGK-PETFKLALDVVRDGGRAVVVGLAPggataeipitrl 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 298 VRRGgvVSVPGVYAGfihgfmfgdafdkgltfkmgqtHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKK 377
Cdd:cd08263  303 VRRG--IKIIGSYGA----------------------RPRQDLPELVGLAASGKLDPEALVTHKYKLEEINEAYENLRKG 358

                 ....*....
gi 492052054 378 EEDCRKVIL 386
Cdd:cd08263  359 LIHGRAIVE 367
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
7-373 1.47e-37

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays a broad range of activities and are distinguished from the smaller short chain dehydrogenases(~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 138.91  E-value: 1.47e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   7 HGANSVKVDTVPDPEIQeADDIILKVTATAICGSDLHLYR-GKIPTVE--HGDIFGHEFMGIVEETGPAVTAVQKGDRVV 83
Cdd:cd08232    4 HAAGDLRVEERPAPEPG-PGEVRVRVAAGGICGSDLHYYQhGGFGTVRlrEPMVLGHEVSGVVEAVGPGVTGLAPGQRVA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  84 IPFVIACGSCFFCNIDLFAACEttnTGRGAiinkksippGAALFgFSHlyggIPGGQAEYVRVPKANVgpFKVPGTLaDE 163
Cdd:cd08232   83 VNPSRPCGTCDYCRAGRPNLCL---NMRFL---------GSAMR-FPH----VQGGFREYLVVDASQC--VPLPDGL-SL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 164 KVLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAqKTYGvipinfddddd 243
Cdd:cd08232  143 RRAALAEPLAVALHAVNRAGDLAGKRVLVTGAGPIGALVVAAARRAGAAEIVATDLADAPLAVA-RAMG----------- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 244 pADTIIR----QTAGMRGVDGVVDaVGFEAKGSTtetilatlklegssgKALRQCIAAVRRGGVVSVPGVYAGFIhGFMF 319
Cdd:cd08232  211 -ADETVNlardPLAAYAADKGDFD-VVFEASGAP---------------AALASALRVVRPGGTVVQVGMLGGPV-PLPL 272
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492052054 320 GDAFDKGLTFKmGQthvHRFMPEL---LEHIEAGRLEPEAIITHRMSLEDAAKGYKL 373
Cdd:cd08232  273 NALVAKELDLR-GS---FRFDDEFaeaVRLLAAGRIDVRPLITAVFPLEEAAEAFAL 325
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
1-388 1.47e-37

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 138.80  E-value: 1.47e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRAL--TYHGANSVKVDtVPDPEIQEaDDIILKVTATAICGSDLHLY------RGKIPTvehGDIFGHEFMGIVEETGPA 72
Cdd:PRK05396   1 MKALvkLKAEPGLWLTD-VPVPEPGP-NDVLIKVKKTAICGTDVHIYnwdewaQKTIPV---PMVVGHEFVGEVVEVGSE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  73 VTAVQKGDRVVIPFVIACGSCFFCNidlfaacettnTGRGAI-INKKSIppgaalfgfshlyG-GIPGGQAEYVRVPKAN 150
Cdd:PRK05396  76 VTGFKVGDRVSGEGHIVCGHCRNCR-----------AGRRHLcRNTKGV-------------GvNRPGAFAEYLVIPAFN 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 151 VgpFKVPGTLADEkvlfLSDILPTAWQAVTNAGIGQ--GSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQ 228
Cdd:PRK05396 132 V--WKIPDDIPDD----LAAIFDPFGNAVHTALSFDlvGEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELAR 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 229 KTYGVIPINfDDDDDPADTIirQTAGMR-GVDgvvdaVGFEAKGsttetilatlklegsSGKALRQCIAAVRRGGVVSVP 307
Cdd:PRK05396 206 KMGATRAVN-VAKEDLRDVM--AELGMTeGFD-----VGLEMSG---------------APSAFRQMLDNMNHGGRIAML 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 308 GVYAGFIhGFMFGDAFDKGLTFK------MGQThvHRFMPELLEhieaGRLEPEAIITHRMSLEDAAKGYKLFdkKEEDC 381
Cdd:PRK05396 263 GIPPGDM-AIDWNKVIFKGLTIKgiygreMFET--WYKMSALLQ----SGLDLSPIITHRFPIDDFQKGFEAM--RSGQS 333

                 ....*..
gi 492052054 382 RKVILTP 388
Cdd:PRK05396 334 GKVILDW 340
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
1-311 1.36e-36

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: 135.52  E-value: 1.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRAL--TYHGANSVKVDTVPDPEIQEaDDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQK 78
Cdd:cd08258    1 MKALvkTGPGPGNVELREVPEPEPGP-GEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEVGPDVEGWKV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  79 GDRVVI-PFVIACGSCFFCNIDLFAACETtntgRGAIINkksippgaalfgfshlygGIPGGQAEYVRVPKANVgpFKVP 157
Cdd:cd08258   80 GDRVVSeTTFSTCGRCPYCRRGDYNLCPH----RKGIGT------------------QADGGFAEYVLVPEESL--HELP 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 158 GTLADEKVLfLSDILPTAWQAV-TNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFM-VDHHPYRLTYAQKTyGVIP 235
Cdd:cd08258  136 ENLSLEAAA-LTEPLAVAVHAVaERSGIRPGDTVVVFGPGPIGLLAAQVAKLQGATVVVVgTEKDEVRLDVAKEL-GADA 213
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492052054 236 INfDDDDDPADtIIRQTAGMRGVDGVVDAVGfeakgsttetilatlklegsSGKALRQCIAAVRRGGVVSVPGVYA 311
Cdd:cd08258  214 VN-GGEEDLAE-LVNEITDGDGADVVIECSG--------------------AVPALEQALELLRKGGRIVQVGIFG 267
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
1-386 3.17e-36

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


Pssm-ID: 176218 [Multi-domain]  Cd Length: 350  Bit Score: 135.61  E-value: 3.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQeADDIILKVTATAICGSDLHLYRG---------KIPTVEHGDIFGHEFMGIVEETGP 71
Cdd:cd08256    1 MRAVVCHGPQDYRLEEVPVPRPG-PGEILVKVEACGICAGDIKCYHGapsfwgdenQPPYVKPPMIPGHEFVGRVVELGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  72 AVTA--VQKGDRVVIPFVIACGSCFFCNIDLFAACETTNtgrgaiinkksippgaaLFGFSHlygGIPGGQAEYVRVPKA 149
Cdd:cd08256   80 GAEErgVKVGDRVISEQIVPCWNCRFCNRGQYWMCQKHD-----------------LYGFQN---NVNGGMAEYMRFPKE 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 150 NVGpFKVPGTLADEKVLFLsDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQK 229
Cdd:cd08256  140 AIV-HKVPDDIPPEDAILI-EPLACALHAVDRANIKFDDVVVLAGAGPLGLGMIGAARLKNPKKLIVLDLKDERLALARK 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 230 TYGVIPINfdddddPAD----TIIRQTAGMRGVDGVVDAVGFEakgsttetilatlklegssgKALRQCIAAVRRGGVvs 305
Cdd:cd08256  218 FGADVVLN------PPEvdvvEKIKELTGGYGCDIYIEATGHP--------------------SAVEQGLNMIRKLGR-- 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 306 vpgvyagFIHGFMFGDAF---------DKGLTFkMGqTHVHRFM-PELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFD 375
Cdd:cd08256  270 -------FVEFSVFGDPVtvdwsiigdRKELDV-LG-SHLGPYCyPIAIDLIASGRLPTDGIVTHQFPLEDFEEAFELMA 340
                        410
                 ....*....|.
gi 492052054 376 KKEEDCrKVIL 386
Cdd:cd08256  341 RGDDSI-KVVL 350
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
26-151 1.18e-35

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: 126.57  E-value: 1.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   26 DDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVIACGSCFFCNIDLFAACe 105
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYNLC- 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 492052054  106 ttntgrgaiinkksipPGAALFGFshlygGIPGGQAEYVRVPKANV 151
Cdd:pfam08240  80 ----------------PNGRFLGY-----DRDGGFAEYVVVPERNL 104
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
1-388 6.74e-32

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: 123.51  E-value: 6.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANS--VKVDTVPDPEIqEADDIILKVTATAICGSDLHLYRGKIPTVeHGDIF--GHEFMGIVEETGPAVTAV 76
Cdd:cd08254    1 MKAWRFHKGSKglLVLEEVPVPEP-GPGEVLVKVKAAGVCHSDLHILDGGVPTL-TKLPLtlGHEIAGTVVEVGAGVTNF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  77 QKGDRVVIPFVIACGSCffcnidlfAACETTNTGRGAIINKKSIppgaalfgfshlygGIPGGQAEYVRVPKANVGPfkV 156
Cdd:cd08254   79 KVGDRVAVPAVIPCGAC--------ALCRRGRGNLCLNQGMPGL--------------GIDGGFAEYIVVPARALVP--V 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 157 PGTLADEKVLFLSDILPTAWQAVTNAG-IGQGSSVAIYGAGPVGLMSAACARMLGAeKIFMVDHHPYRLTYAqKTYGVIP 235
Cdd:cd08254  135 PDGVPFAQAAVATDAVLTPYHAVVRAGeVKPGETVLVIGLGGLGLNAVQIAKAMGA-AVIAVDIKEEKLELA-KELGADE 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 236 INFDDDDDPADTIIRQTAGmrGVDGVVDAVGFeakGSTTEtilatlklegssgkalrQCIAAVRRGGVVSVPGVYAG--F 313
Cdd:cd08254  213 VLNSLDDSPKDKKAAGLGG--GFDVIFDFVGT---QPTFE-----------------DAQKAVKPGGRIVVVGLGRDklT 270
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492052054 314 IHGFMFGdAFDKGLTFKMGQTHVHrfMPELLEHIEAGRLEPeaiITHRMSLEDAAKGYKLFDKKEEDCRkVILTP 388
Cdd:cd08254  271 VDLSDLI-ARELRIIGSFGGTPED--LPEVLDLIAKGKLDP---QVETRPLDEIPEVLERLHKGKVKGR-VVLVP 338
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
1-385 2.11e-31

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


Pssm-ID: 176187 [Multi-domain]  Cd Length: 340  Bit Score: 122.28  E-value: 2.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANS-VKVDTVPDPEIQeADDIILKVTATAICGSDLHLYRGKIPTVEHGD---IFGHEFMGIVEETGPAVTAV 76
Cdd:cd05284    1 MKAARLYEYGKpLRLEDVPVPEPG-PGQVLVRVGGAGVCHSDLHVIDGVWGGILPYKlpfTLGHENAGWVEEVGSGVDGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  77 QKGDRVVIPFVIACGSCFFCNIDLFAACETtntgrgaiinkkSIPPGAalfgfshlygGIPGGQAEYVRVPKANVgpFKV 156
Cdd:cd05284   80 KEGDPVVVHPPWGCGTCRYCRRGEENYCEN------------ARFPGI----------GTDGGFAEYLLVPSRRL--VKL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 157 PGTLADEKVLFLSDILPTAWQAVTNAG--IGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKTYGVI 234
Cdd:cd05284  136 PRGLDPVEAAPLADAGLTAYHAVKKALpyLDPGSTVVVIGVGGLGHIAVQILRALTPATVIAVDRSEEALKLAERLGADH 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 235 PINfdDDDDPADtIIRQTAGMRGVDGVVDAVGfeakgsttetilatlklegsSGKALRQCIAAVRRGGVVSVPGvYAGFI 314
Cdd:cd05284  216 VLN--ASDDVVE-EVRELTGGRGADAVIDFVG--------------------SDETLALAAKLLAKGGRYVIVG-YGGHG 271
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492052054 315 HgFMFGDAFDKGLTFKMGQTHVHRFMPELLEHIEAGRLEPEaiiTHRMSLEDAAKGYKLFDKKEEDCRKVI 385
Cdd:cd05284  272 R-LPTSDLVPTEISVIGSLWGTRAELVEVVALAESGKVKVE---ITKFPLEDANEALDRLREGRVTGRAVL 338
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
1-385 2.12e-31

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: 122.04  E-value: 2.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANS-VKVDTVPDPEIQEaDDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKG 79
Cdd:cd08259    1 MKAAILHKPNKpLQIEEVPDPEPGP-GEVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVGEGVERFKPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  80 DRVVIPFVIACGSCFFCNidlfaacettntgRGaiinKKSIPPGAALFGFShlyggIPGGQAEYVRVPKANVgpFKVPGT 159
Cdd:cd08259   80 DRVILYYYIPCGKCEYCL-------------SG----EENLCRNRAEYGEE-----VDGGFAEYVKVPERSL--VKLPDN 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 160 LADEKVLFLSDILPTAWQAVTNAGIGQGSSVAI-YGAGPVGLMSAACARMLGAeKIFMVDHHPYRLTYAQKTYgvipinf 238
Cdd:cd08259  136 VSDESAALAACVVGTAVHALKRAGVKKGDTVLVtGAGGGVGIHAIQLAKALGA-RVIAVTRSPEKLKILKELG------- 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 239 dddddpADTIIRQTA------GMRGVDGVVDAVGfeakgstTETILATLKlegssgkalrqciaAVRRGGVVSVPGVYAG 312
Cdd:cd08259  208 ------ADYVIDGSKfsedvkKLGGADVVIELVG-------SPTIEESLR--------------SLNKGGRLVLIGNVTP 260
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492052054 313 FIHGFMFGDAFDKGLTFKMGQTHVHRFMPELLEHIEAGRLEPeaIITHRMSLEDAAKGYKLFDKKEEDCRKVI 385
Cdd:cd08259  261 DPAPLRPGLLILKEIRIIGSISATKADVEEALKLVKEGKIKP--VIDRVVSLEDINEALEDLKSGKVVGRIVL 331
PRK10083 PRK10083
putative oxidoreductase; Provisional
1-387 3.73e-30

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 118.69  E-value: 3.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEiQEADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGD 80
Cdd:PRK10083   1 MKSIVIEKPNSLAIEERPIPQ-PAAGEVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGEGVDAARIGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCFFCNIDLFAACETTntgrgaiinkksippgaALFGFSHlyggiPGGQAEYVRVPKANVgpFKVPGTL 160
Cdd:PRK10083  80 RVAVDPVISCGHCYPCSIGKPNVCTSL-----------------VVLGVHR-----DGGFSEYAVVPAKNA--HRIPDAI 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 161 ADEKVLFLsDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSA-ACARMLGAEKIFMVDHHPYRLTYAQKTYGVIPINfd 239
Cdd:PRK10083 136 ADQYAVMV-EPFTIAANVTGRTGPTEQDVALIYGAGPVGLTIVqVLKGVYNVKAVIVADRIDERLALAKESGADWVIN-- 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 240 ddddPADTIIRQTAGMRGVDG--VVDAVGFEAkgsttetILAtlklegssgKALRQCIAAVRRG--GVVSVPG--VYAGF 313
Cdd:PRK10083 213 ----NAQEPLGEALEEKGIKPtlIIDAACHPS-------ILE---------EAVTLASPAARIVlmGFSSEPSeiVQQGI 272
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492052054 314 IhgfmfgdafDKGLTFKMGQTHVHRFmPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEEDCRKVILT 387
Cdd:PRK10083 273 T---------GKELSIFSSRLNANKF-PVVIDWLSKGLIDPEKLITHTFDFQHVADAIELFEKDQRHCCKVLLT 336
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
1-385 3.09e-29

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


Pssm-ID: 176223 [Multi-domain]  Cd Length: 341  Bit Score: 116.25  E-value: 3.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGaNSVKVDTVPDPEiQEADDIILKVTATAICGSDLHLYRGKIPTVE-----------HGDIFGHEFMGIVEET 69
Cdd:cd08262    1 MRAAVFRD-GPLVVRDVPDPE-PGPGQVLVKVLACGICGSDLHATAHPEAMVDdaggpslmdlgADIVLGHEFCGEVVDY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  70 GPAV-TAVQKGDRVV-IPFVIaCGSCFFCNIdlfaacettntgrgaiinkksippgaalfGFShlyGGIPGGQAEYVRVP 147
Cdd:cd08262   79 GPGTeRKLKVGTRVTsLPLLL-CGQGASCGI-----------------------------GLS---PEAPGGYAEYMLLS 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 148 KANVgpFKVPGTLADEKVLfLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRltya 227
Cdd:cd08262  126 EALL--LRVPDGLSMEDAA-LTEPLAVGLHAVRRARLTPGEVALVIGCGPIGLAVIAALKARGVGPIVASDFSPER---- 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 228 qktygvipinfdddddpadtiiRQTAGMRGVDGVVDA---VGFEAKGSTTETIL---ATLKLE--GSSGkALRQCIAAVR 299
Cdd:cd08262  199 ----------------------RALALAMGADIVVDPaadSPFAAWAAELARAGgpkPAVIFEcvGAPG-LIQQIIEGAP 255
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 300 RGGVVSVPGVYAGFIHgFMFGDAFDKGLTFKMGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEE 379
Cdd:cd08262  256 PGGRIVVVGVCMESDN-IEPALAIRKELTLQFSLGYTPEEFADALDALAEGKVDVAPMVTGTVGLDGVPDAFEALRDPEH 334

                 ....*.
gi 492052054 380 DCRKVI 385
Cdd:cd08262  335 HCKILV 340
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
1-389 4.58e-29

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: 115.25  E-value: 4.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYH---GANSVKVDTVPDPEIQeADDIILKVTATAICGSDLHLYRGKIP-TVEHGDIFGHEFMGIVEETGPAVTAV 76
Cdd:COG0604    1 MKAIVITefgGPEVLELEEVPVPEPG-PGEVLVRVKAAGVNPADLLIRRGLYPlPPGLPFIPGSDAAGVVVAVGEGVTGF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  77 QKGDRVVipfviacgscffcnidlfaacettntgrgaiinkksippgaalfgfshlYGGIPGGQAEYVRVPKANVGPfkV 156
Cdd:COG0604   80 KVGDRVA-------------------------------------------------GLGRGGGYAEYVVVPADQLVP--L 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 157 PGTLADEK--VLFLSdiLPTAWQA-VTNAGIGQGSSVAIYGA-GPVGLMSAACARMLGAEkIFMVDHHPYRLTYAqKTYG 232
Cdd:COG0604  109 PDGLSFEEaaALPLA--GLTAWQAlFDRGRLKPGETVLVHGAaGGVGSAAVQLAKALGAR-VIATASSPEKAELL-RALG 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 233 V-IPINFDDDDDPADtiIRQTAGMRGVDGVVDAVGfeakgsttetilatlklegssGKALRQCIAAVRRGGVVSVPGVYA 311
Cdd:COG0604  185 AdHVIDYREEDFAER--VRALTGGRGVDVVLDTVG---------------------GDTLARSLRALAPGGRLVSIGAAS 241
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 312 GFIHGFMFGDAFDKGLT------FKMGQTHVHRFMPELLEHIEAGRLEPeaIITHRMSLEDAAKGYKLFdkkeEDCR--- 382
Cdd:COG0604  242 GAPPPLDLAPLLLKGLTltgftlFARDPAERRAALAELARLLAAGKLRP--VIDRVFPLEEAAEAHRLL----ESGKhrg 315

                 ....*..
gi 492052054 383 KVILTPG 389
Cdd:COG0604  316 KVVLTVD 322
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
21-387 4.76e-29

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: 116.28  E-value: 4.76e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  21 EIQ----EADDIILKVTATAICGSDLHLYRGKIPTVeHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVIACGSCFFC 96
Cdd:cd08277   19 EIEvappKANEVRIKMLATSVCHTDILAIEGFKATL-FPVILGHEGAGIVESVGEGVTNLKPGDKVIPLFIGQCGECSNC 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  97 NIDLFAACETTNTGRGAIinkksIPPGAALFGF-----SHLYGgiPGGQAEYVRVPKANVGpfKVPGTLADEKVLFLSDI 171
Cdd:cd08277   98 RSGKTNLCQKYRANESGL-----MPDGTSRFTCkgkkiYHFLG--TSTFSQYTVVDENYVA--KIDPAAPLEHVCLLGCG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 172 LPTAWQAVTN-AGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAqKTYGVIP-INFDDDDDPADTII 249
Cdd:cd08277  169 FSTGYGAAWNtAKVEPGSTVAVFGLGAVGLSAIMGAKIAGASRIIGVDINEDKFEKA-KEFGATDfINPKDSDKPVSEVI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 250 RQTAGMrGVDGVVDAVGFEakgsttetilatlklegssgKALRQCIAAVRRG-GVVSVPGVYAG---------FIHGFMF 319
Cdd:cd08277  248 REMTGG-GVDYSFECTGNA--------------------DLMNEALESTKLGwGVSVVVGVPPGaelsirpfqLILGRTW 306
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492052054 320 GDAFdkgltfkMGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEedCRKVILT 387
Cdd:cd08277  307 KGSF-------FGGFKSRSDVPKLVSKYMNKKFDLDELITHVLPFEEINKGFDLMKSGE--CIRTVIT 365
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
1-388 3.43e-28

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: 113.51  E-value: 3.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTY--HGANSV-KVDTVPDPEIQeADDIILKVTATAICGSDLHLYRGK-IPTVEHGDIFGHEFMGIVEETGPAVTAV 76
Cdd:cd08266    1 MKAVVIrgHGGPEVlEYGDLPEPEPG-PDEVLVRVKAAALNHLDLWVRRGMpGIKLPLPHILGSDGAGVVEAVGPGVTNV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  77 QKGDRVVIPFVIACGSCFFCnidlfaacettNTGRGAIINKKSIppgaalFGFsHLyggiPGGQAEYVRVPKANVgpFKV 156
Cdd:cd08266   80 KPGQRVVIYPGISCGRCEYC-----------LAGRENLCAQYGI------LGE-HV----DGGYAEYVAVPARNL--LPI 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 157 PGTLADEKVLFLSDILPTAWQA-VTNAGIGQGSSVAIYGAGP-VGLMSAACARMLGAEKIFMVDhHPYRLTYAQKTYGVI 234
Cdd:cd08266  136 PDNLSFEEAAAAPLTFLTAWHMlVTRARLRPGETVLVHGAGSgVGSAAIQIAKLFGATVIATAG-SEDKLERAKELGADY 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 235 PINFDDDDDPAdtIIRQTAGMRGVDGVVDAVGfeakgsttetilatlklegssGKALRQCIAAVRRGGVVSVPGVYAGFI 314
Cdd:cd08266  215 VIDYRKEDFVR--EVRELTGKRGVDVVVEHVG---------------------AATWEKSLKSLARGGRLVTCGATTGYE 271
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492052054 315 HGFMFGDAFDKGLTFkMGQTHVHRF-MPELLEHIEAGRLEPeaIITHRMSLEDAAKGYKLFDKKEEdCRKVILTP 388
Cdd:cd08266  272 APIDLRHVFWRQLSI-LGSTMGTKAeLDEALRLVFRGKLKP--VIDSVFPLEEAAEAHRRLESREQ-FGKIVLTP 342
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
1-293 1.38e-27

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 111.85  E-value: 1.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEIQEADDIILKVTATAICGSDlhlyrgkIPTVEHGD------IFGHEFMGIVEETGPAVT 74
Cdd:PRK10309   1 MKSVVNDTDGIVRVAESPIPEIKHQDDVLVKVASSGLCGSD-------IPRIFKNGahyypiTLGHEFSGYVEAVGSGVD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  75 AVQKGDRVVIPFVIACGSCFFCNIDLFAACETTNtgrgaIINKKSippgaalfgfshlyggiPGGQAEYVRVPKANVgpF 154
Cdd:PRK10309  74 DLHPGDAVACVPLLPCFTCPECLRGFYSLCAKYD-----FIGSRR-----------------DGGNAEYIVVKRKNL--F 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 155 KVPGTLADEKVLFLSDIlPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAqKTYGVI 234
Cdd:PRK10309 130 ALPTDMPIEDGAFIEPI-TVGLHAFHLAQGCEGKNVIIIGAGTIGLLAIQCAVALGAKSVTAIDINSEKLALA-KSLGAM 207
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492052054 235 PI-NFDDDDDPA----------DTIIRQTAGM-RGVDGVVDAVGFEAKGSTTETILATLKLEGSS-GKALRQ 293
Cdd:PRK10309 208 QTfNSREMSAPQiqsvlrelrfDQLILETAGVpQTVELAIEIAGPRAQLALVGTLHHDLHLTSATfGKILRK 279
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
25-373 1.40e-27

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: 112.15  E-value: 1.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  25 ADDIILKVTATAICGSDLHLYRGKIPTvEHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVIACGSCFFCNIDLFAAC 104
Cdd:cd05279   25 AGEVRIKVVATGVCHTDLHVIDGKLPT-PLPVILGHEGAGIVESIGPGVTTLKPGDKVIPLFGPQCGKCKQCLNPRPNLC 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 105 ETTNTGRGaiinKKSIPPGAALF-----GFSHLYGgiPGGQAEYVRVPKANVGpfKVPGTLADEKVLFLSDILPTAWQAV 179
Cdd:cd05279  104 SKSRGTNG----RGLMSDGTSRFtckgkPIHHFLG--TSTFAEYTVVSEISLA--KIDPDAPLEKVCLIGCGFSTGYGAA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 180 TN-AGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKTYGVIPINFDDDDDPADTIIRQTAGmRGV 258
Cdd:cd05279  176 VNtAKVTPGSTCAVFGLGGVGLSVIMGCKAAGASRIIAVDINKDKFEKAKQLGATECINPRDQDKPIVEVLTEMTD-GGV 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 259 DgvvdaVGFEAKGSTtetilatlklegssgKALRQCIAAVRRGG----VVSVP--GVYAGFIHGFMFGDAFDKGLTFkmG 332
Cdd:cd05279  255 D-----YAFEVIGSA---------------DTLKQALDATRLGGgtsvVVGVPpsGTEATLDPNDLLTGRTIKGTVF--G 312
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 492052054 333 QTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKL 373
Cdd:cd05279  313 GWKSKDSVPKLVALYRQKKFPLDELITHVLPFEEINDGFDL 353
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
12-377 4.84e-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: 111.07  E-value: 4.84e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  12 VKVDTVPDPEIQEaDDIILKVTATAICGSDLHLYR----GKI--PTV-EHGDIFGHEFMGIVEETGPAVTAVQKGDRVVI 84
Cdd:cd08265   39 LRVEDVPVPNLKP-DEILIRVKACGICGSDIHLYEtdkdGYIlyPGLtEFPVVIGHEFSGVVEKTGKNVKNFEKGDPVTA 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  85 PFVIACGSCFFCNIDLFAACETTNtgrgaiinkksippgaaLFGFSHlyggiPGGQAEYVRVPKANVGPFKVPGTLADEK 164
Cdd:cd08265  118 EEMMWCGMCRACRSGSPNHCKNLK-----------------ELGFSA-----DGAFAEYIAVNARYAWEINELREIYSED 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 165 VLFLSDIL--PT--AWQAV--TNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKTYG--VIPI 236
Cdd:cd08265  176 KAFEAGALvePTsvAYNGLfiRGGGFRPGAYVVVYGAGPIGLAAIALAKAAGASKVIAFEISEERRNLAKEMGAdyVFNP 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 237 NFDDDDDPADTIIRQTAGMrGVDGVVdavgfEAKGSTTETILATLKLEGSSGKalrqcIAAVRRgGVVSVPgvyagfihg 316
Cdd:cd08265  256 TKMRDCLSGEKVMEVTKGW-GADIQV-----EAAGAPPATIPQMEKSIAINGK-----IVYIGR-AATTVP--------- 314
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492052054 317 fMFGDAFDKGLTFKMG-QTHV-HRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKK 377
Cdd:cd08265  315 -LHLEVLQVRRAQIVGaQGHSgHGIFPSVIKLMASGKIDMTKIITARFPLEGIMEAIKAASER 376
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
25-359 2.94e-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: 108.36  E-value: 2.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  25 ADDIILKVTATAICGSDLHLYRGKIPTvEHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIPFViACGSCFFCNIDLFAAC 104
Cdd:cd08278   27 PDEVLVRIVATGICHTDLVVRDGGLPT-PLPAVLGHEGAGVVEAVGSAVTGLKPGDHVVLSFA-SCGECANCLSGHPAYC 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 105 ETTN---------TGRGAIinkkSIPPGAALFG--FshlyggipgGQ---AEYVRVPKANVgpFKVPGTLaDEKVL---- 166
Cdd:cd08278  105 ENFFplnfsgrrpDGSTPL----SLDDGTPVHGhfF---------GQssfATYAVVHERNV--VKVDKDV-PLELLaplg 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 167 --FLsdilpTAWQAVTNA-GIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQK---TYGVIPinfdD 240
Cdd:cd08278  169 cgIQ-----TGAGAVLNVlKPRPGSSIAVFGAGAVGLAAVMAAKIAGCTTIIAVDIVDSRLELAKElgaTHVINP----K 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 241 DDDPADTIIRQTAGmrGVDGVVDAVGfeakgsttetilatlklegsSGKALRQCIAAVRRGGVVSVPGVYA-GFIHGFMF 319
Cdd:cd08278  240 EEDLVAAIREITGG--GVDYALDTTG--------------------VPAVIEQAVDALAPRGTLALVGAPPpGAEVTLDV 297
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 492052054 320 GDAFDKGLTFK---MGQTHVHRFMPELLEHIEAGRLEPEAIIT 359
Cdd:cd08278  298 NDLLVSGKTIRgviEGDSVPQEFIPRLIELYRQGKFPFDKLVT 340
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
8-387 8.88e-25

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: 103.21  E-value: 8.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   8 GANSVKVDTVPDPEIQEADdIILKVTATAICGSDLH-LYRGKIPTV--EHGDIFGHEFMGIVEETGPAVTAVQKGDRVvi 84
Cdd:cd08269    3 GPGRFEVEEHPRPTPGPGQ-VLVRVEGCGVCGSDLPaFNQGRPWFVypAEPGGPGHEGWGRVVALGPGVRGLAVGDRV-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  85 pfviacgscffcnidlfaacettntgrgaiinkksippgAALFGfshlyggipGGQAEYVRVPKANVgpFKVPGTLADEk 164
Cdd:cd08269   80 ---------------------------------------AGLSG---------GAFAEYDLADADHA--VPLPSLLDGQ- 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 165 vLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAqKTYGVIPINFDDDDDP 244
Cdd:cd08269  109 -AFPGEPLGCALNVFRRGWIRAGKTVAVIGAGFIGLLFLQLAAAAGARRVIAIDRRPARLALA-RELGATEVVTDDSEAI 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 245 ADTIIRQTAGmRGVDGVVDAVGFEAkgsttetilatlklegssgkALRQCIAAVRRGGVVSVPGVYAGFIHGFMFGDAFD 324
Cdd:cd08269  187 VERVRELTGG-AGADVVIEAVGHQW--------------------PLDLAGELVAERGRLVIFGYHQDGPRPVPFQTWNW 245
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492052054 325 KGLTFKMGQTHVHRF----MPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKEEDCRKVILT 387
Cdd:cd08269  246 KGIDLINAVERDPRIglegMREAVKLIADGRLDLGSLLTHEFPLEELGDAFEAARRRPDGFIKGVIV 312
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
1-354 2.51e-24

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: 102.61  E-value: 2.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYH--GANSVKVDTVPDPEIQeADDIILKVTATAICGSDLHLYRGKIPTVEH-GDIFGHEFMGIVEETGPAVTAVQ 77
Cdd:cd08297    1 MKAAVVEefGEKPYEVKDVPVPEPG-PGEVLVKLEASGVCHTDLHAALGDWPVKPKlPLIGGHEGAGVVVAVGPGVSGLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  78 KGDRVVIPFVI-ACGSCFFCNIDLFAACET-TNTGRGAiinkksippgaalfgfshlyggiPGGQAEYVRVPKANVGPfk 155
Cdd:cd08297   80 VGDRVGVKWLYdACGKCEYCRTGDETLCPNqKNSGYTV-----------------------DGTFAEYAIADARYVTP-- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 156 VPGTLADEKV--LFLSDIlpTAWQAVTNAGIGQGSSVAIYGA-GPVGLMSAACARMLGAeKIFMVDHHPYRLTYAQKTYG 232
Cdd:cd08297  135 IPDGLSFEQAapLLCAGV--TVYKALKKAGLKPGDWVVISGAgGGLGHLGVQYAKAMGL-RVIAIDVGDEKLELAKELGA 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 233 VIPINFdDDDDPADTIIRQTAGMrGVDGVVdavgfeakgsttetILAtlklegSSGKALRQCIAAVRRGGVVSVPGVYAG 312
Cdd:cd08297  212 DAFVDF-KKSDDVEAVKELTGGG-GAHAVV--------------VTA------VSAAAYEQALDYLRPGGTLVCVGLPPG 269
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 492052054 313 fihGFMFGDAFD---KGLTFKMGQTHVHRFMPELLEHIEAGRLEP 354
Cdd:cd08297  270 ---GFIPLDPFDlvlRGITIVGSLVGTRQDLQEALEFAARGKVKP 311
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
57-386 2.72e-24

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: 101.19  E-value: 2.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  57 IFGHEFMGIVEETGPAVTAVQKGDRVvipfviacgscfFCnidlfaacettntgrgaiinkksippgaalfgfshlyggi 136
Cdd:cd08255   23 PPGYSSVGRVVEVGSGVTGFKPGDRV------------FC---------------------------------------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 137 PGGQAEYVRVPKANVgpFKVPGTLADEKVLFLsDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFM 216
Cdd:cd08255   51 FGPHAERVVVPANLL--VPLPDGLPPERAALT-ALAATALNGVRDAEPRLGERVAVVGLGLVGLLAAQLAKAAGAREVVG 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 217 VDHHPYRLTYAQKTYGVIPINFDDDDdpadtiirqTAGMRGVDGVVDAVGfeakgsttetilatlklegsSGKALRQCIA 296
Cdd:cd08255  128 VDPDAARRELAEALGPADPVAADTAD---------EIGGRGADVVIEASG--------------------SPSALETALR 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 297 AVRRGGVVSVPGVYAGFihGFMFGDAFD-KGLTFKMGQ-------------THVHRFMpELLEHIEAGRLEPeaIITHRM 362
Cdd:cd08255  179 LLRDRGRVVLVGWYGLK--PLLLGEEFHfKRLPIRSSQvygigrydrprrwTEARNLE-EALDLLAEGRLEA--LITHRV 253
                        330       340
                 ....*....|....*....|....
gi 492052054 363 SLEDAAKGYKLFDKKEEDCRKVIL 386
Cdd:cd08255  254 PFEDAPEAYRLLFEDPPECLKVVL 277
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
30-378 1.81e-23

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: 100.83  E-value: 1.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  30 LKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVIACGSCFFCNIDLFAACET--T 107
Cdd:cd08301   32 IKILHTSLCHTDVYFWEAKGQTPLFPRILGHEAAGIVESVGEGVTDLKPGDHVLPVFTGECKECRHCKSEKSNMCDLlrI 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 108 NTGRGAIINKKSIP------PGAALFGFSHLyggipggqAEYVRVPKANVGpfKVPGTLADEKVLFLSDILPTAWQAVTN 181
Cdd:cd08301  112 NTDRGVMINDGKSRfsingkPIYHFVGTSTF--------SEYTVVHVGCVA--KINPEAPLDKVCLLSCGVSTGLGAAWN 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 182 -AGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAqKTYGVIP-INFDDDDDPADTIIRQTAGmRGVD 259
Cdd:cd08301  182 vAKVKKGSTVAIFGLGAVGLAVAEGARIRGASRIIGVDLNPSKFEQA-KKFGVTEfVNPKDHDKPVQEVIAEMTG-GGVD 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 260 GVVDAVGfeakgsttetilatlklegsSGKALRQCIAAVRRG-GVVSVPGVYAG---------------FIHGFMFGDaf 323
Cdd:cd08301  260 YSFECTG--------------------NIDAMISAFECVHDGwGVTVLLGVPHKdavfsthpmnllngrTLKGTLFGG-- 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492052054 324 dkgltFKmGQTHVhrfmPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFDKKE 378
Cdd:cd08301  318 -----YK-PKTDL----PNLVEKYMKKELELEKFITHELPFSEINKAFDLLLKGE 362
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
1-376 1.15e-22

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: 97.25  E-value: 1.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYH---GANSVKVDTVPDPEIQEaDDIILKVTATAICGSDLHLYRG---KIPTVEHGDIFGHEFMGIVEETGPAVT 74
Cdd:cd05289    1 MKAVRIHeygGPEVLELADVPTPEPGP-GEVLVKVHAAGVNPVDLKIREGllkAAFPLTLPLIPGHDVAGVVVAVGPGVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  75 AVQKGDRVvipfviacgscffcnidlfaacettntgrgaiinkksippgaalFGFSHLYGGipGGQAEYVRVPKANVgpF 154
Cdd:cd05289   80 GFKVGDEV--------------------------------------------FGMTPFTRG--GAYAEYVVVPADEL--A 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 155 KVPGTLADEK--VLFLSDIlpTAWQAVTNAG-IGQGSSVAIYGA-GPVGLMSAACARMLGAEKIFMV--DHHPYrLtyaq 228
Cdd:cd05289  112 LKPANLSFEEaaALPLAGL--TAWQALFELGgLKAGQTVLIHGAaGGVGSFAVQLAKARGARVIATAsaANADF-L---- 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 229 KTYGvipinfdddddpADTIIRQTAGM-------RGVDGVVDAVGfeakgsttetilatlklegssGKALRQCIAAVRRG 301
Cdd:cd05289  185 RSLG------------ADEVIDYTKGDferaaapGGVDAVLDTVG---------------------GETLARSLALVKPG 231
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492052054 302 G-VVSVPgvyagfihGFMFGDAFDKGLTFKMGQTHVH---RFMPELLEHIEAGRLEPeaIITHRMSLEDAAKGYKLFDK 376
Cdd:cd05289  232 GrLVSIA--------GPPPAEQAAKRRGVRAGFVFVEpdgEQLAELAELVEAGKLRP--VVDRVFPLEDAAEAHERLES 300
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
17-370 5.80e-22

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: 96.15  E-value: 5.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  17 VPDPEiqeADDIILKVTATAICGSDLHLY--------RGKIPTVEHGDIF----GHEFMGIVEETGPAVTAVQKGDRVVI 84
Cdd:cd08240   20 TPKPP---GTEVLVKVTACGVCHSDLHIWdggydlggGKTMSLDDRGVKLplvlGHEIVGEVVAVGPDAADVKVGDKVLV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  85 PFVIACGSCFFCNIDLFAACEttnTGRgaiinkksippgaalfgfsHLYGGIPGGQAEYVRVPKANVgpFKVPGTLADEk 164
Cdd:cd08240   97 YPWIGCGECPVCLAGDENLCA---KGR-------------------ALGIFQDGGYAEYVIVPHSRY--LVDPGGLDPA- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 165 vlfLSDILP----TAWQAVTNAGIGQGS-SVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKTYGVIPINFD 239
Cdd:cd08240  152 ---LAATLAcsglTAYSAVKKLMPLVADePVVIIGAGGLGLMALALLKALGPANIIVVDIDEAKLEAAKAAGADVVVNGS 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 240 DDDDPADtIIRQTAGmrGVDGVVDAVGFEAkgsttetilatlklegSSGKALRqciaAVRRGGVVSVPGVYAGfihGFMF 319
Cdd:cd08240  229 DPDAAKR-IIKAAGG--GVDAVIDFVNNSA----------------TASLAFD----ILAKGGKLVLVGLFGG---EATL 282
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492052054 320 GDAFdkgLTFKMGQ---THVHRF--MPELLEHIEAGRLEPEAIITHRMS-----LEDAAKG 370
Cdd:cd08240  283 PLPL---LPLRALTiqgSYVGSLeeLRELVALAKAGKLKPIPLTERPLSdvndaLDDLKAG 340
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
1-214 4.60e-21

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: 93.18  E-value: 4.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYH--GANSVKVDTVPDPEIqEADDIILKVTATAICGSDLHLYRG-KIPTVEHgdIFGHEFMGIVEETGPAVTAVQ 77
Cdd:cd08264    1 MKALVFEksGIENLKVEDVKDPKP-GPGEVLIRVKMAGVNPVDYNVINAvKVKPMPH--IPGAEFAGVVEEVGDHVKGVK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  78 KGDRVVIPFVIACGSCFFCnidlFAACET--TNTGRGAIINKksippgaalfgfshlyggipGGQAEYVRVPKANVgpFK 155
Cdd:cd08264   78 KGDRVVVYNRVFDGTCDMC----LSGNEMlcRNGGIIGVVSN--------------------GGYAEYIVVPEKNL--FK 131
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492052054 156 VPGTLADEkvlfLSDILP----TAWQAVTNAGIGQGSSVAIYGA-GPVGLMSAACARMLGAEKI 214
Cdd:cd08264  132 IPDSISDE----LAASLPvaalTAYHALKTAGLGPGETVVVFGAsGNTGIFAVQLAKMMGAEVI 191
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
1-286 5.37e-21

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 93.18  E-value: 5.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANS-VKVDTVPDPEIQEaDDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKG 79
Cdd:PRK13771   1 MKAVILPGFKQgYRIEEVPDPKPGK-DEVVIKVNYAGLCYRDLLQLQGFYPRMKYPVILGHEVVGTVEEVGENVKGFKPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  80 DRVVIPFVIACGSCFFCNIDLFAACEttntgrgaiiNKKSippgaalfgfshlYG-GIPGGQAEYVRVPKANVgpFKVPG 158
Cdd:PRK13771  80 DRVASLLYAPDGTCEYCRSGEEAYCK----------NRLG-------------YGeELDGFFAEYAKVKVTSL--VKVPP 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 159 TLADEKVLFLSDILPTAWQAVTNAGIGQGSSVAIYGA-GPVGLMSAACARMLGAeKIFMVDHHPYRLTYAQKTygvipin 237
Cdd:PRK13771 135 NVSDEGAVIVPCVTGMVYRGLRRAGVKKGETVLVTGAgGGVGIHAIQVAKALGA-KVIAVTSSESKAKIVSKY------- 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492052054 238 fdddddpADTIIRQTA------GMRGVDGVVDAVGfeakGSTTETILATLKLEGS 286
Cdd:PRK13771 207 -------ADYVIVGSKfseevkKIGGADIVIETVG----TPTLEESLRSLNMGGK 250
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
6-386 8.02e-21

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: 93.21  E-value: 8.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   6 YHGANSVKVDTVPDPEIQEaDDIILKVTATAICGSDLHLYRG----KIPTVehgdiFGHEFMGIVEETGPAVTAVQKGDR 81
Cdd:cd08281   15 YADSRPLVIEEVELDPPGP-GEVLVKIAAAGLCHSDLSVINGdrprPLPMA-----LGHEAAGVVVEVGEGVTDLEVGDH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  82 VVIPFVIACGSCFFCNIDLFAACEttntgRGAIINKKsippGAALFGFSHLYggIPGGQ----------AEYVRVPKANV 151
Cdd:cd08281   89 VVLVFVPSCGHCRPCAEGRPALCE-----PGAAANGA----GTLLSGGRRLR--LRGGEinhhlgvsafAEYAVVSRRSV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 152 gpFKVPGTLADEK-VLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAqKT 230
Cdd:cd08281  158 --VKIDKDVPLEIaALFGCAVLTGVGAVVNTAGVRPGQSVAVVGLGGVGLSALLGAVAAGASQVVAVDLNEDKLALA-RE 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 231 YGVIPInfddDDDPADTIIRQTAGMRGvdGVVDaVGFEAKGsttetilatlklegsSGKALRQCIAAVRRGG-VVSV--P 307
Cdd:cd08281  235 LGATAT----VNAGDPNAVEQVRELTG--GGVD-YAFEMAG---------------SVPALETAYEITRRGGtTVTAglP 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 308 GVYAGFIHGFMFGDAFDKglTFK---MGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGyklFDK--KEEDCR 382
Cdd:cd08281  293 DPEARLSVPALSLVAEER--TLKgsyMGSCVPRRDIPRYLALYLSGRLPVDKLLTHRLPLDEINEG---FDRlaAGEAVR 367

                 ....
gi 492052054 383 KVIL 386
Cdd:cd08281  368 QVIL 371
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
1-323 9.65e-21

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


Pssm-ID: 176258 [Multi-domain]  Cd Length: 329  Bit Score: 92.25  E-value: 9.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGA-----NSVKVDTVPDPEIQEaDDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTA 75
Cdd:cd08298    1 MKAMVLEKPgpieeNPLRLTEVPVPEPGP-GEVLIKVEACGVCRTDLHIVEGDLPPPKLPLIPGHEIVGRVEAVGPGVTR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  76 VQKGDRV-VIPFVIACGSCFFCNidlfaacettnTGRGAIINKKSIPpgaalfGFShlyggIPGGQAEYVRVPKANVgpF 154
Cdd:cd08298   80 FSVGDRVgVPWLGSTCGECRYCR-----------SGRENLCDNARFT------GYT-----VDGGYAEYMVADERFA--Y 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 155 KVPGTLADEKV--LFLSDIlpTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEkIFMVDHHPYRLTYAQKTyg 232
Cdd:cd08298  136 PIPEDYDDEEAapLLCAGI--IGYRALKLAGLKPGQRLGLYGFGASAHLALQIARYQGAE-VFAFTRSGEHQELAREL-- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 233 vipinfdddddpadtiirqtagmrGVDGVvdavgfeakGSTTETILATLK---LEGSSGKALRQCIAAVRRGGVVSVPGV 309
Cdd:cd08298  211 ------------------------GADWA---------GDSDDLPPEPLDaaiIFAPVGALVPAALRAVKKGGRVVLAGI 257
                        330
                 ....*....|....
gi 492052054 310 YAGFIHGFMFGDAF 323
Cdd:cd08298  258 HMSDIPAFDYELLW 271
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
25-373 1.48e-20

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: 92.29  E-value: 1.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  25 ADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVIACGSCFFC---NIDLF 101
Cdd:cd08300   27 AGEVRIKILATGVCHTDAYTLSGADPEGLFPVILGHEGAGIVESVGEGVTSVKPGDHVIPLYTPECGECKFCksgKTNLC 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 102 AACETTnTGRGAIINKKS--IPPGAALFgfsHLYGgiPGGQAEYVRVPKANVGpfKVPGTLADEKVLFLSDILPTAWQAV 179
Cdd:cd08300  107 QKIRAT-QGKGLMPDGTSrfSCKGKPIY---HFMG--TSTFSEYTVVAEISVA--KINPEAPLDKVCLLGCGVTTGYGAV 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 180 TN-AGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQK---TYGVIPINFDDDDDpaDTIIRQTAGm 255
Cdd:cd08300  179 LNtAKVEPGSTVAVFGLGAVGLAVIQGAKAAGASRIIGIDINPDKFELAKKfgaTDCVNPKDHDKPIQ--QVLVEMTDG- 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 256 rGVDgvvdaVGFEAKGSTtetilatlklegssgKALRQCIAAVRRG-GVVSVPGVYAGF--IHGFMF---------GDAF 323
Cdd:cd08300  256 -GVD-----YTFECIGNV---------------KVMRAALEACHKGwGTSVIIGVAAAGqeISTRPFqlvtgrvwkGTAF 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 492052054 324 DKgltFKmGQTHVhrfmPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKL 373
Cdd:cd08300  315 GG---WK-SRSQV----PKLVEDYMKGKIKVDEFITHTMPLDEINEAFDL 356
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-388 2.12e-20

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: 91.15  E-value: 2.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVKVDTVPDPEiQEADDIILKVTATAICGSDLHLYRGKIPTvehGDIFGHEFMGIVEETGPAVTavqKGD 80
Cdd:cd08242    1 MKALVLDGGLDLRVEDLPKPE-PPPGEALVRVLLAGICNTDLEIYKGYYPF---PGVPGHEFVGIVEEGPEAEL---VGK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  81 RVVIPFVIACGSCFFCNIDLFAACEttntgrgaiiNKKSIppgaalfgfshlygGI---PGGQAEYVRVPKANvgPFKVP 157
Cdd:cd08242   74 RVVGEINIACGRCEYCRRGLYTHCP----------NRTVL--------------GIvdrDGAFAEYLTLPLEN--LHVVP 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 158 GTLADEKVLFLsDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAeKIFMVDHHPYRLTYAQKtygvipin 237
Cdd:cd08242  128 DLVPDEQAVFA-EPLAAALEILEQVPITPGDKVAVLGDGKLGLLIAQVLALTGP-DVVLVGRHSEKLALARR-------- 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 238 fdddddpADTIIRQTAGMRGVDGVVDAVgFEAKGSTTetilatlklegssgkALRQCIAAVRRGGVVSVPGVYAGFihgf 317
Cdd:cd08242  198 -------LGVETVLPDEAESEGGGFDVV-VEATGSPS---------------GLELALRLVRPRGTVVLKSTYAGP---- 250
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 318 mfgdafdkgLTFKMGQTHVHRF---------MPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLfdKKEEDCRKVILTP 388
Cdd:cd08242  251 ---------ASFDLTKAVVNEItlvgsrcgpFAPALRLLRKGLVDVDPLITAVYPLEEALEAFER--AAEPGALKVLLRP 319
PLN02702 PLN02702
L-idonate 5-dehydrogenase
8-361 8.15e-20

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 90.22  E-value: 8.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   8 GANSVKVDTVPDPEIQEaDDIILKVTATAICGSDLHLYRG-KIP--TVEHGDIFGHEFMGIVEETGPAVTAVQKGDRVVI 84
Cdd:PLN02702  25 GVNTLKIQPFKLPPLGP-HDVRVRMKAVGICGSDVHYLKTmRCAdfVVKEPMVIGHECAGIIEEVGSEVKHLVVGDRVAL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  85 PFVIACGSCFFCNIDLFAACettntgrgaiinkksipPGAALFGFSHLYGGIpggqAEYVRVPkANVGpFKVPGTLADEK 164
Cdd:PLN02702 104 EPGISCWRCNLCKEGRYNLC-----------------PEMKFFATPPVHGSL----ANQVVHP-ADLC-FKLPENVSLEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 165 VLfLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAqKTYG---VIPINFDDD 241
Cdd:PLN02702 161 GA-MCEPLSVGVHACRRANIGPETNVLVMGAGPIGLVTMLAARAFGAPRIVIVDVDDERLSVA-KQLGadeIVLVSTNIE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 242 DDPADTIIRQTAGMRGVDGVVDAVGFeakgsttetilatlklegssGKALRQCIAAVRRGGVVSVpgvyAGFIHGFM--- 318
Cdd:PLN02702 239 DVESEVEEIQKAMGGGIDVSFDCVGF--------------------NKTMSTALEATRAGGKVCL----VGMGHNEMtvp 294
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 492052054 319 ----FGDAFDKGLTFKMGQTHvhrfmPELLEHIEAGRLEPEAIITHR 361
Cdd:PLN02702 295 ltpaAAREVDVVGVFRYRNTW-----PLCLEFLRSGKIDVKPLITHR 336
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
16-306 1.03e-19

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: 89.30  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  16 TVPDPEiqeADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVI-ACGSCF 94
Cdd:cd08245   18 PVPEPG---PGEVLIKIEACGVCHTDLHAAEGDWGGSKYPLVPGHEIVGEVVEVGAGVEGRKVGDRVGVGWLVgSCGRCE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  95 FCNIDLFAACETtntgrgaiinkksippgAALFGFSHLyggipGGQAEYVRVPKANVGPFKVPGTLADEKVLFLSDIlpT 174
Cdd:cd08245   95 YCRRGLENLCQK-----------------AVNTGYTTQ-----GGYAEYMVADAEYTVLLPDGLPLAQAAPLLCAGI--T 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 175 AWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEkIFMVDHHPYRLTYAQKTYGVIPINFDDDDdpadtiiRQTAG 254
Cdd:cd08245  151 VYSALRDAGPRPGERVAVLGIGGLGHLAVQYARAMGFE-TVAITRSPDKRELARKLGADEVVDSGAEL-------DEQAA 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492052054 255 MRGVDGVVDAVgfeakgsttetilatlklegSSGKALRQCIAAVRRGG-VVSV 306
Cdd:cd08245  223 AGGADVILVTV--------------------VSGAAAEAALGGLRRGGrIVLV 255
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
7-229 2.09e-19

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 88.59  E-value: 2.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   7 HGANSVKVDTvpdPEIQ-EADDIILKVTATAICGSDLHLYR-GKIP--TVEHGDIFGHEFMGIVEETgpAVTAVQKGDRV 82
Cdd:PRK09880  11 AGKKDVAVTE---QEIEwNNNGTLVQITRGGICGSDLHYYQeGKVGnfVIKAPMVLGHEVIGKIVHS--DSSGLKEGQTV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  83 VIPFVIACGSCFFCNIDLFAACETTNTGrgaiinkksippGAALFgFSHLYGGIpggqAEYVRVPKANVGPFkvpGTLAD 162
Cdd:PRK09880  86 AINPSKPCGHCKYCLSHNENQCTTMRFF------------GSAMY-FPHVDGGF----TRYKVVDTAQCIPY---PEKAD 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492052054 163 EKVLFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQK 229
Cdd:PRK09880 146 EKVMAFAEPLAVAIHAAHQAGDLQGKRVFVSGVGPIGCLIVAAVKTLGAAEIVCADVSPRSLSLARE 212
PLN02740 PLN02740
Alcohol dehydrogenase-like
30-374 5.62e-19

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 87.93  E-value: 5.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  30 LKVTATAICGSDLHLYRG------KIPTvehgdIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVIACGSCFFCNIDLFAA 103
Cdd:PLN02740  40 IKILYTSICHTDLSAWKGeneaqrAYPR-----ILGHEAAGIVESVGEGVEDLKAGDHVIPIFNGECGDCRYCKRDKTNL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 104 CET----------TNTGRGAIINKKSIPPGAALFGFSHLyggipggqAEYVRVPKANVgpFKVPGTLADEKVLFLSDILP 173
Cdd:PLN02740 115 CETyrvdpfksvmVNDGKTRFSTKGDGQPIYHFLNTSTF--------TEYTVLDSACV--VKIDPNAPLKKMSLLSCGVS 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 174 TAWQAVTN-AGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAqKTYGVIP-INFDDDDDPADTIIRQ 251
Cdd:PLN02740 185 TGVGAAWNtANVQAGSSVAIFGLGAVGLAVAEGARARGASKIIGVDINPEKFEKG-KEMGITDfINPKDSDKPVHERIRE 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 252 TAGmRGVDgvvdaVGFEAKGSTtetilatlklegssgKALRQCIAAVRRG-GVVSVPGVYAG---------------FIH 315
Cdd:PLN02740 264 MTG-GGVD-----YSFECAGNV---------------EVLREAFLSTHDGwGLTVLLGIHPTpkmlplhpmelfdgrSIT 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492052054 316 GFMFGDafdkgltFKmGQTHvhrfMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLF 374
Cdd:PLN02740 323 GSVFGD-------FK-GKSQ----LPNLAKQCMQGVVNLDGFITHELPFEKINEAFQLL 369
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
19-212 3.70e-18

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: 84.86  E-value: 3.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  19 DPEIQEADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGDRV-VIPFVIACGSCFFCN 97
Cdd:cd05283   18 ERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDRVgVGCQVDSCGTCEQCK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  98 IDLFAACETTNTgrgaiinkksippgaalFGFSHLYGGIP--GGQAEYVRVPKANVgpFKVPGTLADEKV--LFLSDIlp 173
Cdd:cd05283   98 SGEEQYCPKGVV-----------------TYNGKYPDGTItqGGYADHIVVDERFV--FKIPEGLDSAAAapLLCAGI-- 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 492052054 174 TAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAE 212
Cdd:cd05283  157 TVYSPLKRNGVGPGKRVGVVGIGGLGHLAVKFAKALGAE 195
PLN02827 PLN02827
Alcohol dehydrogenase-like
17-389 1.41e-17

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 83.80  E-value: 1.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  17 VPDPEIQEaddIILKVTATAICGSDLHLYRGK--IPTvehgdIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVIACGSCF 94
Cdd:PLN02827  32 VSPPQPLE---IRIKVVSTSLCRSDLSAWESQalFPR-----IFGHEASGIVESIGEGVTEFEKGDHVLTVFTGECGSCR 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  95 FCNIDLFAACETTNTGRGAI----------INKKSIPPGAALFGFSHlYGGIPGGQAeyvrvpkanvgpFKVPGTLADEK 164
Cdd:PLN02827 104 HCISGKSNMCQVLGLERKGVmhsdqktrfsIKGKPVYHYCAVSSFSE-YTVVHSGCA------------VKVDPLAPLHK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 165 VLFLSDILPTAWQAVTN-AGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAqKTYGVIP-INFDDDD 242
Cdd:PLN02827 171 ICLLSCGVAAGLGAAWNvADVSKGSSVVIFGLGTVGLSVAQGAKLRGASQIIGVDINPEKAEKA-KTFGVTDfINPNDLS 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 243 DPADTIIRqtagmRGVDGVVDaVGFEAKGSTtetilatlkleGSSGKALRQCIAAVRRGGVVSVPGV-------YAGFIH 315
Cdd:PLN02827 250 EPIQQVIK-----RMTGGGAD-YSFECVGDT-----------GIATTALQSCSDGWGLTVTLGVPKAkpevsahYGLFLS 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492052054 316 GFMFgdafdKGLTFkmGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAAKGYKLFdkKEEDC-RKVILTPG 389
Cdd:PLN02827 313 GRTL-----KGSLF--GGWKPKSDLPSLVDKYMNKEIMIDEFITHNLSFDEINKAFELM--REGKClRCVIHMPK 378
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-375 5.34e-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: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 81.43  E-value: 5.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYH---GANSVKVDTVPDPEIQeADDIILKVTATAICGSDLHLYRGKIPT-VEHGDIFGHEFMGIVEETGPAVTAV 76
Cdd:cd08276    1 MKAWRLSgggGLDNLKLVEEPVPEPG-PGEVLVRVHAVSLNYRDLLILNGRYPPpVKDPLIPLSDGAGEVVAVGEGVTRF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  77 QKGDRVVipfviacgSCFFcnidlfaacetTNTGRGAIINKKsippgaalfGFSHLYGGIPGGQAEYVRVPKAnvGPFKV 156
Cdd:cd08276   80 KVGDRVV--------PTFF-----------PNWLDGPPTAED---------EASALGGPIDGVLAEYVVLPEE--GLVRA 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 157 PGTLADEKVlflsDILP----TAWQA-VTNAGIGQGSSVAIYGAGPVGLMSAACARMLGA---------EKIFMVdhhpy 222
Cdd:cd08276  130 PDHLSFEEA----ATLPcaglTAWNAlFGLGPLKPGDTVLVQGTGGVSLFALQFAKAAGArviatsssdEKLERA----- 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 223 rltyaqKTYGvipinfdddddpADTII------------RQTAGMRGVDGVVDAVGfeakgsttetilatlklegssGKA 290
Cdd:cd08276  201 ------KALG------------ADHVInyrttpdwgeevLKLTGGRGVDHVVEVGG---------------------PGT 241
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 291 LRQCIAAVRRGGVVSVPGVYAGFIHGFMFGDAFDKGLTFKmGQTHVHRFMPE-LLEHIEAGRLEPeaIITHRMSLEDAAK 369
Cdd:cd08276  242 LAQSIKAVAPGGVISLIGFLSGFEAPVLLLPLLTKGATLR-GIAVGSRAQFEaMNRAIEAHRIRP--VIDRVFPFEEAKE 318

                 ....*.
gi 492052054 370 GYKLFD 375
Cdd:cd08276  319 AYRYLE 324
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
25-218 1.98e-16

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: 80.05  E-value: 1.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  25 ADDIILKVTATAICGSDLHLYRGKIPTVeHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVIACGSCFFC-------- 96
Cdd:cd08299   32 AHEVRIKIVATGICRSDDHVVSGKLVTP-FPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFVPQCGKCRAClnpesnlc 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  97 -NIDLFAACETTNTGRGAIINK-KSIppgaalfgfsHLYGGIpGGQAEYVRVPKANVGpfKVPGTLADEKVLFLSDILPT 174
Cdd:cd08299  111 lKNDLGKPQGLMQDGTSRFTCKgKPI----------HHFLGT-STFSEYTVVDEIAVA--KIDAAAPLEKVCLIGCGFST 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 492052054 175 AWQAVTN-AGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVD 218
Cdd:cd08299  178 GYGAAVNtAKVTPGSTCAVFGLGGVGLSAIMGCKAAGASRIIAVD 222
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
1-375 6.59e-15

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: 75.17  E-value: 6.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTY---HGANSVKVDTVPDPEIqEADDIILKVTATAICGSDLHLYRGKIPTVEHG-DIFGHEFMGIVEETGPAVTAV 76
Cdd:cd05276    1 MKAIVIkepGGPEVLELGEVPKPAP-GPGEVLIRVAAAGVNRADLLQRQGLYPPPPGAsDILGLEVAGVVVAVGPGVTGW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  77 QKGDRVvipfviacgscffcnidlfaacettntgrgaiinkksippgAALfgfshLYGGipgGQAEYVRVPKANVgpFKV 156
Cdd:cd05276   80 KVGDRV-----------------------------------------CAL-----LAGG---GYAEYVVVPAGQL--LPV 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 157 PGTLADEKVLFLSDILPTAWQAV-TNAGIGQGSSVAIY-GAGPVGLMSAACARMLGAeKIFMVDHHPYRLTYAQKTYGVI 234
Cdd:cd05276  109 PEGLSLVEAAALPEVFFTAWQNLfQLGGLKAGETVLIHgGASGVGTAAIQLAKALGA-RVIATAGSEEKLEACRALGADV 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 235 PINFDDDDDpADTIIRQTAGmRGVDGVVDAVGfeakGSTTETILATLKLEGssgkalRQCIAAVRRGGVVSVPgvyagfi 314
Cdd:cd05276  188 AINYRTEDF-AEEVKEATGG-RGVDVILDMVG----GDYLARNLRALAPDG------RLVLIGLLGGAKAELD------- 248
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492052054 315 hgfmFGDAFDKGLTFkMGQTH-----------VHRFMPELLEHIEAGRLEPeaIITHRMSLEDAAKGYKLFD 375
Cdd:cd05276  249 ----LAPLLRKRLTL-TGSTLrsrsleekaalAAAFREHVWPLFASGRIRP--VIDKVFPLEEAAEAHRRME 313
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-375 1.54e-13

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 71.05  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRAL---TYHGANSVKVDTVPDPEIqEADDIILKVTATAICGSDLHLYRGKIP-TVEHGDIFGHEFMGIVEETGPAVTAV 76
Cdd:cd08272    1 MKALvleSFGGPEVFELREVPRPQP-GPGQVLVRVHASGVNPLDTKIRRGGAAaRPPLPAILGCDVAGVVEAVGEGVTRF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  77 QKGDRVvipfviacgscFFCnidlfaacettntgrgaiinkksiPPGaalfgfshlYGGIPGGQAEYVRVPKANVGPfkV 156
Cdd:cd08272   80 RVGDEV-----------YGC------------------------AGG---------LGGLQGSLAEYAVVDARLLAL--K 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 157 PGTLADEKVLFLSDILPTAWQA-VTNAGIGQGSSVAIY-GAGPVGLMSAACARMLGAEKIFMVDhhPYRLTYAQKtYGVI 234
Cdd:cd08272  114 PANLSMREAAALPLVGITAWEGlVDRAAVQAGQTVLIHgGAGGVGHVAVQLAKAAGARVYATAS--SEKAAFARS-LGAD 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 235 PINFdDDDDPADTIIRQTAGmRGVDGVVDAVGfeakgsttetilatlklegssGKALRQCIAAVRR-GGVVSVPGVYAGf 313
Cdd:cd08272  191 PIIY-YRETVVEYVAEHTGG-RGFDVVFDTVG---------------------GETLDASFEAVALyGRVVSILGGATH- 246
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492052054 314 ihgfMFGDAFDKGLTF-----------KMGQTHVHRFMPELLEHIEAGRLEPeAIITHRMSLEDAAKGYKLFD 375
Cdd:cd08272  247 ----DLAPLSFRNATYsgvftllplltGEGRAHHGEILREAARLVERGQLRP-LLDPRTFPLEEAAAAHARLE 314
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
17-214 2.21e-13

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: 70.74  E-value: 2.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  17 VPDPEIQEaddIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIP-FVIACGSCFF 95
Cdd:cd08296   20 VPLPGPGE---VLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVGEGVSRWKVGDRVGVGwHGGHCGTCDA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  96 CNIDLFAACEttntgRGAIinkksipPGAALfgfshlyggiPGGQAEYVRVPKANVGPfkVPGTLADEKV--LFLSDIlp 173
Cdd:cd08296   97 CRRGDFVHCE-----NGKV-------TGVTR----------DGGYAEYMLAPAEALAR--IPDDLDAAEAapLLCAGV-- 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 492052054 174 TAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKI 214
Cdd:cd08296  151 TTFNALRNSGAKPGDLVAVQGIGGLGHLAVQYAAKMGFRTV 191
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-376 3.28e-13

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


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 69.94  E-value: 3.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSV--KVDTVPDPEIqEADDIILKVTATAICGSDLHLYRGKIP---TVEHGDIFGHEFMGIVEETGPAVTA 75
Cdd:cd08267    1 VVYTRYGSPEVLllLEVEVPIPTP-KPGEVLVKVHAASVNPVDWKLRRGPPKlllGRPFPPIPGMDFAGEVVAVGSGVTR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  76 VQKGDRVvipfviacgscffcnidlfaacettntgrgaiinkksippgaalFGFSHLYGGipGGQAEYVRVPKANVGPfK 155
Cdd:cd08267   80 FKVGDEV--------------------------------------------FGRLPPKGG--GALAEYVVAPESGLAK-K 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 156 VPG-TLADEKVLFLSDIlpTAWQAVTNAG-IGQGSSVAIYGA-GPVGlmSAAC--ARMLGAE--------KIFMVdhhpy 222
Cdd:cd08267  113 PEGvSFEEAAALPVAGL--TALQALRDAGkVKPGQRVLINGAsGGVG--TFAVqiAKALGAHvtgvcstrNAELV----- 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 223 rltyaqKTYGvipinfdddddpADTII--------RQTAGMRGVDGVVDAVGfeakgsttetilatlkleGSSGKALRQC 294
Cdd:cd08267  184 ------RSLG------------ADEVIdyttedfvALTAGGEKYDVIFDAVG------------------NSPFSLYRAS 227
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 295 IAAVRRGGVVSV----PGVYAGFIHGFMFGDAFDKGLTFKMGqTHVHRFMPELLEHIEAGRLEPeaIITHRMSLEDAAKG 370
Cdd:cd08267  228 LALKPGGRYVSVgggpSGLLLVLLLLPLTLGGGGRRLKFFLA-KPNAEDLEQLAELVEEGKLKP--VIDSVYPLEDAPEA 304

                 ....*.
gi 492052054 371 YKLFDK 376
Cdd:cd08267  305 YRRLKS 310
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
9-306 5.26e-13

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 69.68  E-value: 5.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   9 ANSVKVDTVPDPEIQ--EADDIILKVTATAICGSDLHLYRGKIPTVEhGDIFGHEFMGIVEETGPAVTAVQKGDRVVIP- 85
Cdd:PRK09422   7 NKDHTGDVVVEKTLRplKHGEALVKMEYCGVCHTDLHVANGDFGDKT-GRILGHEGIGIVKEVGPGVTSLKVGDRVSIAw 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  86 FVIACGSCFFCnidlfaacettNTGRGAIINKksippgAALFGFShlyggIPGGQAEYVRVpKANVGpFKVPGTLADEKV 165
Cdd:PRK09422  86 FFEGCGHCEYC-----------TTGRETLCRS------VKNAGYT-----VDGGMAEQCIV-TADYA-VKVPEGLDPAQA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 166 LFLSDILPTAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAEKIFMVDHHPYRLTYAQKTYGVIPINfDDDDDPA 245
Cdd:PRK09422 142 SSITCAGVTTYKAIKVSGIKPGQWIAIYGAGGLGNLALQYAKNVFNAKVIAVDINDDKLALAKEVGADLTIN-SKRVEDV 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492052054 246 DTIIRQTAGmrGVDG-VVDAVgfeakgsttetilatlklegsSGKALRQCIAAVRRGG-VVSV 306
Cdd:PRK09422 221 AKIIQEKTG--GAHAaVVTAV---------------------AKAAFNQAVDAVRAGGrVVAV 260
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
1-266 1.45e-12

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 68.13  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALT---YHGANSVKVDTVPDPEIQEaDDIILKVTATAICGSDLHLYRGKIPTVE-HGDIFGHEFMGIVEETGPAVTAV 76
Cdd:PTZ00354   2 MRAVTlkgFGGVDVLKIGESPKPAPKR-NDVLIKVSAAGVNRADTLQRQGKYPPPPgSSEILGLEVAGYVEDVGSDVKRF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  77 QKGDRVVipfviacgscffcnidlfaacettntgrgaiinkksippgaALFGfshlyggiPGGQAEYVRVPKANVgpFKV 156
Cdd:PTZ00354  81 KEGDRVM-----------------------------------------ALLP--------GGGYAEYAVAHKGHV--MHI 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 157 PGTLADEKVLFLSDILPTAWQAV-TNAGIGQGSSVAIY-GAGPVGLMSAACARMLGAEKIFMVDhHPYRLTYAQKTYGVI 234
Cdd:PTZ00354 110 PQGYTFEEAAAIPEAFLTAWQLLkKHGDVKKGQSVLIHaGASGVGTAAAQLAEKYGAATIITTS-SEEKVDFCKKLAAII 188
                        250       260       270
                 ....*....|....*....|....*....|..
gi 492052054 235 PINFDDDDDPADTIIRQTAGmRGVDGVVDAVG 266
Cdd:PTZ00354 189 LIRYPDEEGFAPKVKKLTGE-KGVNLVLDCVG 219
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
1-221 2.21e-12

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: 67.63  E-value: 2.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANS-VKVDTVPDPEIqEADDIILKVTATAICGSDLHLYRGKIPTVEHGD---IFGHEFMGIVEETGPAvTAV 76
Cdd:cd08230    1 MKAIAVKPGKPgVRVVDIPEPEP-TPGEVLVRTLEVGVCGTDREIVAGEYGTAPPGEdflVLGHEALGVVEEVGDG-SGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  77 QKGDRVViPFVI-ACGSCFFCNIDLFAACET-TNTGRGaiINkksippgaalfgfshlygGIPGGQAEYVRVPKANVgpF 154
Cdd:cd08230   79 SPGDLVV-PTVRrPPGKCLNCRIGRPDFCETgEYTERG--IK------------------GLHGFMREYFVDDPEYL--V 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492052054 155 KVPGTLADEKVLF--LSDILPTAWQAVT---NAGIGQGSSVAIYGAGPVGLMSAACARMLGAEkIFMVDHHP 221
Cdd:cd08230  136 KVPPSLADVGVLLepLSVVEKAIEQAEAvqkRLPTWNPRRALVLGAGPIGLLAALLLRLRGFE-VYVLNRRD 206
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
1-388 3.49e-12

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: 67.22  E-value: 3.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGAN--SVKVDTVPDPEIQEaDDIILKVTATAICGSD-LHLYRGKIPTveHGDIFGHEFMGIVEETGPAVTAVQ 77
Cdd:cd08249    1 QKAAVLTGPGggLLVVVDVPVPKPGP-DEVLVKVKAVALNPVDwKHQDYGFIPS--YPAILGCDFAGTVVEVGSGVTRFK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  78 KGDRVvipfviacgscffcnidlfaacettntgrgaiinkksippgaalFGFSHLYGGIP---GGQAEYVRVPKANVgpF 154
Cdd:cd08249   78 VGDRV--------------------------------------------AGFVHGGNPNDprnGAFQEYVVADADLT--A 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 155 KVPGTLADEK-------------VLFLSDILPTAWQAVTNAgiGQGSSVAIYGAG-PVGLM------------------- 201
Cdd:cd08249  112 KIPDNISFEEaatlpvglvtaalALFQKLGLPLPPPKPSPA--SKGKPVLIWGGSsSVGTLaiqlaklagykvittaspk 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 202 SAACARMLGAEKIFmvDHHpyrltyaqktygvipinfdddDDPADTIIRQTAGmRGVDGVVDAVGfeaKGSTTETILATL 281
Cdd:cd08249  190 NFDLVKSLGADAVF--DYH---------------------DPDVVEDIRAATG-GKLRYALDCIS---TPESAQLCAEAL 242
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 282 KlEGSSGKalrqcIAAVR--RGGVVSVPGVYAGFIHGFMfgdAFDKGLTFKMGQTHVHRFMPELLehiEAGRLEPEAIIT 359
Cdd:cd08249  243 G-RSGGGK-----LVSLLpvPEETEPRKGVKVKFVLGYT---VFGEIPEDREFGEVFWKYLPELL---EEGKLKPHPVRV 310
                        410       420
                 ....*....|....*....|....*....
gi 492052054 360 HRMSLEDAAKGYKLFDKKEEDCRKVILTP 388
Cdd:cd08249  311 VEGGLEGVQEGLDLLRKGKVSGEKLVVRL 339
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
1-373 1.04e-11

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: 65.60  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRAL---TYHGANSVKVDTVPdPEIQEADDIILKVTATAICGSDLHLYRGK---------IPtvehgdifGHEFMGIVEE 68
Cdd:cd08241    1 MKAVvckELGGPEDLVLEEVP-PEPGAPGEVRIRVEAAGVNFPDLLMIQGKyqvkpplpfVP--------GSEVAGVVEA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  69 TGPAVTAVQKGDRVVipfviacgscffcnidlfaacettntgrgaiinkksippgaalfGFSHLyggipGGQAEYVRVPK 148
Cdd:cd08241   72 VGEGVTGFKVGDRVV--------------------------------------------ALTGQ-----GGFAEEVVVPA 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 149 ANVgpFKVPGTLADEKVLFLSDILPTAWQA-VTNAGIGQGSSVAIYGA-GPVGLMSAACARMLGAEKIFMV--------- 217
Cdd:cd08241  103 AAV--FPLPDGLSFEEAAALPVTYGTAYHAlVRRARLQPGETVLVLGAaGGVGLAAVQLAKALGARVIAAAsseeklala 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 218 -----DHhpyRLTYAQKTYgvipinfdddddpADTIIRQTAGmRGVDGVVDAVGfeakGSTTEtilatlklegssgKALR 292
Cdd:cd08241  181 ralgaDH---VIDYRDPDL-------------RERVKALTGG-RGVDVVYDPVG----GDVFE-------------ASLR 226
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 293 qCIAavrRGGVVSVPGVYAGFI---------------HGFMFGdafdkglTFKMGQTHVHR-FMPELLEHIEAGRLEPEa 356
Cdd:cd08241  227 -SLA---WGGRLLVIGFASGEIpqipanllllknisvVGVYWG-------AYARREPELLRaNLAELFDLLAEGKIRPH- 294
                        410
                 ....*....|....*..
gi 492052054 357 iITHRMSLEDAAKGYKL 373
Cdd:cd08241  295 -VSAVFPLEQAAEALRA 310
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-388 1.27e-11

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


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 65.40  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRA--LTYHGANS--VKVDTVPDPEIQeADDIILKVTATAICGSDLHLYRGKIPTVEHGD-------------------- 56
Cdd:cd08274    1 MRAvlLTGHGGLDklVYRDDVPVPTPA-PGEVLIRVGACGVNNTDINTREGWYSTEVDGAtdstgageagwwggtlsfpr 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  57 IFGHEFMGIVEETGPAVTAVQKGDRVVIPFVIacgscffcnidlfaacettntgrgaiinkkSIPPGAALFGFSHLYGGI 136
Cdd:cd08274   80 IQGADIVGRVVAVGEGVDTARIGERVLVDPSI------------------------------RDPPEDDPADIDYIGSER 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 137 PGGQAEYVRVPKANVgpFKVPGTLADEKVLFLSDILPTAWQAVTNAGIGQGSSVAIYGA-GPVGLMSAACARMLGAEkif 215
Cdd:cd08274  130 DGGFAEYTVVPAENA--YPVNSPLSDVELATFPCSYSTAENMLERAGVGAGETVLVTGAsGGVGSALVQLAKRRGAI--- 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 216 mvdhhPYRLTYAQKTYGVIPINfdddddpADTIIR---------QTAGMRGVDGVVDAVGfeakGSTTETILATLKLEGs 286
Cdd:cd08274  205 -----VIAVAGAAKEEAVRALG-------ADTVILrdaplladaKALGGEPVDVVADVVG----GPLFPDLLRLLRPGG- 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 287 sgkalRQCIAAVRRGGVVSVPgvyagfihgfmFGDAFDKGLTFkMGQTHVHR-FMPELLEHIEAGRLEPeaIITHRMSLE 365
Cdd:cd08274  268 -----RYVTAGAIAGPVVELD-----------LRTLYLKDLTL-FGSTLGTReVFRRLVRYIEEGEIRP--VVAKTFPLS 328
                        410       420
                 ....*....|....*....|...
gi 492052054 366 DAAKGYKLFDKKEEdCRKVILTP 388
Cdd:cd08274  329 EIREAQAEFLEKRH-VGKLVLVP 350
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
26-368 1.77e-11

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: 64.51  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  26 DDIILKVTATAICGSDLHLYRGKIPTVEHGdiFGHEFMGIVEETGPAVTAVQKGDRVvipfviacgscffcnidlfaace 105
Cdd:cd05195    1 DEVEVEVKAAGLNFRDVLVALGLLPGDETP--LGLECSGIVTRVGSGVTGLKVGDRV----------------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 106 ttntgrgaiinkksippgaalFGFShlyggiPGGQAEYVRVPKANVgpFKVPGTLADEK-----VLFLsdilpTAWQAVT 180
Cdd:cd05195   56 ---------------------MGLA------PGAFATHVRVDARLV--VKIPDSLSFEEaatlpVAYL-----TAYYALV 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 181 N-AGIGQGSSVAIY-GAGPVGLMSAACARMLGAEkIFMVDHHPYRLTYAQKTYGVIP-------INFdddddpADTIIRQ 251
Cdd:cd05195  102 DlARLQKGESVLIHaAAGGVGQAAIQLAQHLGAE-VFATVGSEEKREFLRELGGPVDhifssrdLSF------ADGILRA 174
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 252 TAGmRGVDgVVdavgfeakgsttetiLATLklegsSGKALRQCIAAVRRGG-VVSVpGVYAGFIHGFMFGDAFDKGLTF- 329
Cdd:cd05195  175 TGG-RGVD-VV---------------LNSL-----SGELLRASWRCLAPFGrFVEI-GKRDILSNSKLGMRPFLRNVSFs 231
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 492052054 330 --------KMGQTHVHRFMPELLEHIEAGRLEPEAIITHRMSLEDAA 368
Cdd:cd05195  232 svdldqlaRERPELLRELLREVLELLEAGVLKPLPPTVVPSASEIDA 278
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
4-377 5.44e-11

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


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 63.44  E-value: 5.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   4 LTYHG---ANSVKVDTVPDPEiqeADDIILKVTATAICGSDLHLYRGKIPTVEHGDIF-GHEFMGIVEETGPAVTAVQKG 79
Cdd:cd08273    6 VTRRGgpeVLKVVEADLPEPA---AGEVVVKVEASGVSFADVQMRRGLYPDQPPLPFTpGYDLVGRVDALGSGVTGFEVG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  80 DRVvipfviacgscffcnidlfaacettntgrgaiinkksippgAALFgfshlyggIPGGQAEYVRVPKANVGPfkVP-G 158
Cdd:cd08273   83 DRV-----------------------------------------AALT--------RVGGNAEYINLDAKYLVP--VPeG 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 159 TLADEKVLFLSDILpTAWQAVTNAG-IGQGSSVAIYGA-GPVGLMSAACARMLGAEKIFMVD--HHPYrltyaQKTYGVI 234
Cdd:cd08273  112 VDAAEAVCLVLNYV-TAYQMLHRAAkVLTGQRVLIHGAsGGVGQALLELALLAGAEVYGTASerNHAA-----LRELGAT 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 235 PInfdddddPADT--IIRQTAGMRGVDGVVDAVGFEAKgSTTETILA---TLKLEGSSGkALRQCIAAVRRGGVVSvpgv 309
Cdd:cd08273  186 PI-------DYRTkdWLPAMLTPGGVDVVFDGVGGESY-EESYAALApggTLVCYGGNS-SLLQGRRSLAALGSLL---- 252
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492052054 310 yAGFIHGFMFGDafDKGLTF----KMGQTHVHRFMPELLEHI---EAGRLEPeaIITHRMSLEDAAKGYKLFDKK 377
Cdd:cd08273  253 -ARLAKLKLLPT--GRRATFyyvwRDRAEDPKLFRQDLTELLdllAKGKIRP--KIAKRLPLSEVAEAHRLLESG 322
adh_fam_2 TIGR02822
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
17-212 1.61e-10

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: 61.86  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   17 VPDPEIQEaddIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIPFV-IACGSCFF 95
Cdd:TIGR02822  22 VPRPGPGE---LLVRVRACGVCRTDLHVSEGDLPVHRPRVTPGHEVVGEVAGRGADAGGFAVGDRVGIAWLrRTCGVCRY 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   96 CNidlfaacettntgRGAiinkKSIPPGAALFGFSHlyggiPGGQAEYVRVPKANVgpFKVPGTLADEKV--LFLSDILp 173
Cdd:TIGR02822  99 CR-------------RGA----ENLCPASRYTGWDT-----DGGYAEYTTVPAAFA--YRLPTGYDDVELapLLCAGII- 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 492052054  174 tAWQAVTNAGIGQGSSVAIYGAGPVGLMSAACARMLGAE 212
Cdd:TIGR02822 154 -GYRALLRASLPPGGRLGLYGFGGSAHLTAQVALAQGAT 191
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
1-312 3.63e-10

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


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 60.70  E-value: 3.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYH---GANSVKVDTVPDPEIQeADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPavTAVQ 77
Cdd:cd08243    1 MKAIVIEqpgGPEVLKLREIPIPEPK-PGWVLIRVKAFGLNRSEIFTRQGHSPSVKFPRVLGIEAVGEVEEAPG--GTFT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  78 KGDRVVipfviacgscffcnidlfaaceTTNTGrgaiinkksippgaalFGFShlyggIPGGQAEYVRVPKANVgpFKVP 157
Cdd:cd08243   78 PGQRVA----------------------TAMGG----------------MGRT-----FDGSYAEYTLVPNEQV--YAID 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 158 GTLADEKVLFLSDILPTAWQAVTNA-GIGQGSSVAIYGA-GPVGLMSAACARMLGAEKIFMVdHHPYRltyaQKTYGVIP 235
Cdd:cd08243  113 SDLSWAELAALPETYYTAWGSLFRSlGLQPGDTLLIRGGtSSVGLAALKLAKALGATVTATT-RSPER----AALLKELG 187
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492052054 236 INFDDDDDPADTIIRQTAGmRGVDGVVDAVGfeakgstTETILATLKlegssgkalrqciaAVRRGGVVSVPGVYAG 312
Cdd:cd08243  188 ADEVVIDDGAIAEQLRAAP-GGFDKVLELVG-------TATLKDSLR--------------HLRPGGIVCMTGLLGG 242
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
25-210 6.18e-10

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 60.20  E-value: 6.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  25 ADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVI-ACGSCFFCNIDLFAA 103
Cdd:PLN02514  34 PEDVVIKVIYCGICHTDLHQIKNDLGMSNYPMVPGHEVVGEVVEVGSDVSKFTVGDIVGVGVIVgCCGECSPCKSDLEQY 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 104 CettntgrgaiiNKKsippgaaLFGFSHLY-GGIP--GGQAEYVRVPKANVgpFKVPGTLADEKVLFLSDILPTAWQAVT 180
Cdd:PLN02514 114 C-----------NKR-------IWSYNDVYtDGKPtqGGFASAMVVDQKFV--VKIPEGMAPEQAAPLLCAGVTVYSPLS 173
                        170       180       190
                 ....*....|....*....|....*....|.
gi 492052054 181 NAGIGQ-GSSVAIYGAGPVGLMSAACARMLG 210
Cdd:PLN02514 174 HFGLKQsGLRGGILGLGGVGHMGVKIAKAMG 204
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-388 1.23e-09

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: 59.15  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYH---GANSVKVDTVPDPEIQeADDIILKVTATAICGSDLHLYRGK-IPTVEHGDIFGHEFMGIVEETGPAVTAV 76
Cdd:cd08268    1 MRAVRFHqfgGPEVLRIEELPVPAPG-AGEVLIRVEAIGLNRADAMFRRGAyIEPPPLPARLGYEAAGVVEAVGAGVTGF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  77 QKGDRVvipfviacgscffcnidlfaacettntgrgaiinkkSIPPGAalfgFSHLYGGIpggqAEYVRVPKANVgpFKV 156
Cdd:cd08268   80 AVGDRV------------------------------------SVIPAA----DLGQYGTY----AEYALVPAAAV--VKL 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 157 PGTLADEK--VLFLSdiLPTAWQA-VTNAGIGQGSSVAIYGA-GPVGLMSAACARMLGAEKIFMVDHHPYRltYAQKTYG 232
Cdd:cd08268  114 PDGLSFVEaaALWMQ--YLTAYGAlVELAGLRPGDSVLITAAsSSVGLAAIQIANAAGATVIATTRTSEKR--DALLALG 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 233 VIPINFDDDDDPADTIIRQTAGmRGVDGVVDAVGfeakgsttetilatlklegssGKALRQCIAAVRRGGVVSVPGVYAG 312
Cdd:cd08268  190 AAHVIVTDEEDLVAEVLRITGG-KGVDVVFDPVG---------------------GPQFAKLADALAPGGTLVVYGALSG 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 313 FIHGFMFGDAFDKGLTFK--------MGQTHVHRFMPELLEHIEAGRLEPeaIITHRMSLEDAAKGYKLFDKKEEdCRKV 384
Cdd:cd08268  248 EPTPFPLKAALKKSLTFRgysldeitLDPEARRRAIAFILDGLASGALKP--VVDRVFPFDDIVEAHRYLESGQQ-IGKI 324

                 ....
gi 492052054 385 ILTP 388
Cdd:cd08268  325 VVTP 328
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
26-378 8.65e-09

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


Pssm-ID: 176213 [Multi-domain]  Cd Length: 303  Bit Score: 56.28  E-value: 8.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  26 DDIILKVTATAICGSDLHLYRGKIPTV-EHGDIFGHEFMGIVEETGPAVTAVQKGDRVVipfviacgscffcnidlfaac 104
Cdd:cd08251    8 GEVRIQVRAFSLNFGDLLCVRGLYPTMpPYPFTPGFEASGVVRAVGPHVTRLAVGDEVI--------------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 105 ettntgrgAIInkksippGAALfgfshlyggipGGQAEYVRVPKANVgpFKVPGTLADEKVLFLSDILPTAWQAVTNAGI 184
Cdd:cd08251   67 --------AGT-------GESM-----------GGHATLVTVPEDQV--VRKPASLSFEEACALPVVFLTVIDAFARAGL 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 185 GQGSSVAIYGA-GPVGLMSAACARMLGAEkIFMVDHHPYRLTYAqKTYGV-IPINFDDDDDPADtIIRQTAGmRGVDGVV 262
Cdd:cd08251  119 AKGEHILIQTAtGGTGLMAVQLARLKGAE-IYATASSDDKLEYL-KQLGVpHVINYVEEDFEEE-IMRLTGG-RGVDVVI 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 263 DAVGFEAkgsttetILATLKLEGSSGKALRQCIAAVRRGGVVSVPG------VYAGFIHGFMFGDAfdkgltfkmgqTHV 336
Cdd:cd08251  195 NTLSGEA-------IQKGLNCLAPGGRYVEIAMTALKSAPSVDLSVlsnnqsFHSVDLRKLLLLDP-----------EFI 256
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 492052054 337 HRFMPELLEHIEAGRLEPeaIITHRMSLEDAAKGYKLFDKKE 378
Cdd:cd08251  257 ADYQAEMVSLVEEGELRP--TVSRIFPFDDIGEAYRYLSDRE 296
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
197-349 1.15e-08

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 52.99  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  197 PVGLMSAACARMLGAeKIFMVDHHPYRLTYAqKTYGVIPINFDDDDDPADTIIRQTAGmRGVDGVVDAVGfeakgsttet 276
Cdd:pfam00107   1 GVGLAAIQLAKAAGA-KVIAVDGSEEKLELA-KELGADHVINPKETDLVEEIKELTGG-KGVDVVFDCVG---------- 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492052054  277 ilatlklegsSGKALRQCIAAVRRGGVVsvpgVYAGFIHG---FMFGDAFDKGLTFK---MGQTHVhrfMPELLEHIEA 349
Cdd:pfam00107  68 ----------SPATLEQALKLLRPGGRV----VVVGLPGGplpLPLAPLLLKELTILgsfLGSPEE---FPEALDLLAS 129
ADH_N_assoc pfam13823
Alcohol dehydrogenase GroES-associated; This short domain is frequently found at the ...
1-23 3.38e-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: 48.94  E-value: 3.38e-08
                          10        20
                  ....*....|....*....|...
gi 492052054    1 MRALTYHGANSVKVDTVPDPEIQ 23
Cdd:pfam13823   1 MKAVTYQGPKDVRVEEVPDPRIE 23
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
11-387 7.38e-08

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: 53.82  E-value: 7.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  11 SVKVDTVPDPEiQEADDIILKVTATAICGSDLHL----YRGKI--PTVEhgdifGHEFMGIVEETGPAVTAVQKGDRVvi 84
Cdd:cd05282   13 VLELVSLPIPP-PGPGEVLVRMLAAPINPSDLITisgaYGSRPplPAVP-----GNEGVGVVVEVGSGVSGLLVGQRV-- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  85 pfviacgscffcnidlfaacettntgrgaiinkksIPPGAAlfgfshlyggipGGQAEYVRVPKANVgpFKVPGTLADEK 164
Cdd:cd05282   85 -----------------------------------LPLGGE------------GTWQEYVVAPADDL--IPVPDSISDEQ 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 165 VLFLSdILP-TAWQAVTNAGIGQ-GSSVAIYGAGP-VGLMSAACARMLGAEKIFMV--DHHPYRLtyaqKTYGVIP-INF 238
Cdd:cd05282  116 AAMLY-INPlTAWLMLTEYLKLPpGDWVIQNAANSaVGRMLIQLAKLLGFKTINVVrrDEQVEEL----KALGADEvIDS 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 239 DDDDDPADtiIRQTAGMRGVDGVVDAVGfeakGSTTETILATLK------LEGSSGKALRQCIAAVRRGGVVSVpgvyAG 312
Cdd:cd05282  191 SPEDLAQR--VKEATGGAGARLALDAVG----GESATRLARSLRpggtlvNYGLLSGEPVPFPRSVFIFKDITV----RG 260
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492052054 313 FIHGFMFGDAFDKGLTFKMGqthvhrfmpELLEHIEAGRLEPEaiITHRMSLEDAAKGYKlfdKKEEDCR--KVILT 387
Cdd:cd05282  261 FWLRQWLHSATKEAKQETFA---------EVIKLVEAGVLTTP--VGAKFPLEDFEEAVA---AAEQPGRggKVLLT 323
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
31-373 2.01e-07

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 52.01  E-value: 2.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054    31 KVTATAICGSDLHLYRGKIPtveHGDIFGHEFMGIVEETGPAVTAVQKGDRVvipfviacgscffcnidlfaacettntg 110
Cdd:smart00829   2 EVRAAGLNFRDVLIALGLYP---GEAVLGGECAGVVTRVGPGVTGLAVGDRV---------------------------- 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   111 rgaiinkksippgaalFGFShlyggiPGGQAEYVRVPKANVgpFKVPGTLADEK-----VLFLsdilpTAWQA-VTNAGI 184
Cdd:smart00829  51 ----------------MGLA------PGAFATRVVTDARLV--VPIPDGWSFEEaatvpVVFL-----TAYYAlVDLARL 101
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   185 GQGSSVAIY-GAGPVGLMSAACARMLGAEkIFMVDHHPYRLTYAqKTYGVIP--------INFdddddpADTIIRQTAGm 255
Cdd:smart00829 102 RPGESVLIHaAAGGVGQAAIQLARHLGAE-VFATAGSPEKRDFL-RALGIPDdhifssrdLSF------ADEILRATGG- 172
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   256 RGVDgVVdavgfeakgsttetiLATLklegsSGKALRQCIAAVRRGGVvsvpgvyagFI---------HGFMFGDAFDKG 326
Cdd:smart00829 173 RGVD-VV---------------LNSL-----SGEFLDASLRCLAPGGR---------FVeigkrdirdNSQLAMAPFRPN 222
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 492052054   327 LTF------KM--GQTHVHRFMPELLEHIEAGRLEPeaIITHRMSLEDAAKGYKL 373
Cdd:smart00829 223 VSYhavdldALeeGPDRIRELLAEVLELFAEGVLRP--LPVTVFPISDAEDAFRY 275
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
26-104 3.56e-07

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 51.95  E-value: 3.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  26 DDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVI-ACGSCFFCNIDLFAAC 104
Cdd:PLN02178  32 NDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVGKNVTKFKEGDRVGVGVIIgSCQSCESCNQDLENYC 111
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
26-104 4.17e-07

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 51.42  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  26 DDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQKGDRVVIPFVI-ACGSCFFCNIDLFAAC 104
Cdd:PLN02586  38 EDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGKNVKKFKEGDRVGVGVIVgSCKSCESCDQDLENYC 117
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
1-214 4.87e-07

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: 51.05  E-value: 4.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYH--GANSV-KVDTVPDPEIqEADDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGH-EFMGIVEETGPAVTAV 76
Cdd:cd08253    1 MRAIRYHefGAPDVlRLGDLPVPTP-GPGEVLVRVHASGVNPVDTYIRAGAYPGLPPLPYVPGsDGAGVVEAVGEGVDGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  77 QKGDRVvipfviacgscffcnidlfaacettntgrgaiinkksippgaalFGFSHLYGGIPGGQAEYVRVPKANVgpFKV 156
Cdd:cd08253   80 KVGDRV--------------------------------------------WLTNLGWGRRQGTAAEYVVVPADQL--VPL 113
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492052054 157 PGTLADEK-----VLFLsdilpTAWQAVT-NAGIGQGSSVAIYG-AGPVGLMSAACARMLGAEKI 214
Cdd:cd08253  114 PDGVSFEQgaalgIPAL-----TAYRALFhRAGAKAGETVLVHGgSGAVGHAAVQLARWAGARVI 173
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
12-199 1.33e-06

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: 49.91  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  12 VKVDTVPDPEIQEADDIILKVTATAI--------CG---SDLHLYRGKIPTVEHGDIF----GHEFMGIVEETGPAVTAV 76
Cdd:cd08248   16 LLLENARIPVIRKPNQVLIKVHAASVnpidvlmrSGygrTLLNKKRKPQSCKYSGIEFpltlGRDCSGVVVDIGSGVKSF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  77 QKGDRVvipfviacgscffcnidlfaacettntgrgaiinkksippgaalFGFSHLYGgiPGGQAEYVRVPKANVGpfKV 156
Cdd:cd08248   96 EIGDEV--------------------------------------------WGAVPPWS--QGTHAEYVVVPENEVS--KK 127
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492052054 157 PGTLADEKvlflSDILP----TAWQAVTNAGI-----GQGSSVAIYGA-GPVG 199
Cdd:cd08248  128 PKNLSHEE----AASLPyaglTAWSALVNVGGlnpknAAGKRVLILGGsGGVG 176
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
8-369 1.75e-06

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: 49.36  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   8 GANSVKVDTVPDPEIQeADDIILKVTATAICGSDLH----LYRGKIPTvehgdIFGHEFMGIVEETGPAVTAVQKGDRVV 83
Cdd:cd05286   10 GPEVLEYEDVPVPEPG-PGEVLVRNTAIGVNFIDTYfrsgLYPLPLPF-----VLGVEGAGVVEAVGPGVTGFKVGDRVA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  84 ipfviacgscffcnidlfaacettntgrgaiinkksippgaalfgfshlYGGIPGGQAEYVRVPKANVgpFKVPGTLADE 163
Cdd:cd05286   84 -------------------------------------------------YAGPPGAYAEYRVVPASRL--VKLPDGISDE 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 164 KV--LFLSDIlpTAWQAVTNAG-IGQGSSVAIYG-AGPVGLMSAACARMLGAEKIFMVDhHPYRLTYAqKTYG---VIP- 235
Cdd:cd05286  113 TAaaLLLQGL--TAHYLLRETYpVKPGDTVLVHAaAGGVGLLLTQWAKALGATVIGTVS-SEEKAELA-RAAGadhVINy 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 236 --INFdddddpADTIIRQTAGmRGVDGVVDAVGfeakGSTTETILATLKlegssgkalrqciaavRRGGVVS-------V 306
Cdd:cd05286  189 rdEDF------VERVREITGG-RGVDVVYDGVG----KDTFEGSLDSLR----------------PRGTLVSfgnasgpV 241
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 307 PGVyagFIHGFMFGDAFdkgLTFKMGQTHV-------HRFMpELLEHIEAGRLEPEaiITHRMSLEDAAK 369
Cdd:cd05286  242 PPF---DLLRLSKGSLF---LTRPSLFHYIatreellARAA-ELFDAVASGKLKVE--IGKRYPLADAAQ 302
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
1-368 4.38e-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: 48.13  E-value: 4.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYH---GANSVKVDTVPDPEIQeADDIILKVTATAICGSDLHLYRGK---IPTVEHGDIFGHEFMGIVEETGPAVT 74
Cdd:cd08244    1 MRAIRLHefgPPEVLVPEDVPDPVPG-PGQVRIAVAAAGVHFVDTQLRSGWgpgPFPPELPYVPGGEVAGVVDAVGPGVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  75 AVQKGDRVVipfviacgscffcnidlfaacetTNTGRGaiinkksippgaalfgfshlyggiPGGQAEYVRVPKANVGPf 154
Cdd:cd08244   80 PAWLGRRVV-----------------------AHTGRA------------------------GGGYAELAVADVDSLHP- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 155 kVPGTLADEKVLFLSDILPTAWQAVTNAGIGQGSSVAIYGA-GPVGLMSAACARMLGAeKIFMVDHHPYRLTYAQKTYGV 233
Cdd:cd08244  112 -VPDGLDLEAAVAVVHDGRTALGLLDLATLTPGDVVLVTAAaGGLGSLLVQLAKAAGA-TVVGAAGGPAKTALVRALGAD 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 234 IPINFDDDDDPAdtIIRQTAGMRGVDGVVDAVGfeakgsttetilatlklegssGKALRQCIAAVRRGGVVSVPGVYAGF 313
Cdd:cd08244  190 VAVDYTRPDWPD--QVREALGGGGVTVVLDGVG---------------------GAIGRAALALLAPGGRFLTYGWASGE 246
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492052054 314 IHGFMFGDAFDKGLTF------KMGQTHVHRFMPELLEHIEAGRLEPeaIITHRMSLEDAA 368
Cdd:cd08244  247 WTALDEDDARRRGVTVvgllgvQAERGGLRALEARALAEAAAGRLVP--VVGQTFPLERAA 305
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
1-83 1.72e-05

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


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 46.44  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTY--HG--ANSVKVDTVPDPEIQEADDIILKVTATAICGSDLHL----YRGKIPTVEHGD-IFGHEFMGIVEETGP 71
Cdd:cd08290    1 AKALVYteHGepKEVLQLESYEIPPPGPPNEVLVKMLAAPINPADINQiqgvYPIKPPTTPEPPaVGGNEGVGEVVKVGS 80
                         90
                 ....*....|..
gi 492052054  72 AVTAVQKGDRVV 83
Cdd:cd08290   81 GVKSLKPGDWVI 92
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-357 3.13e-05

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 45.73  E-value: 3.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGAN---SVKVDTVPDPEIQEaDDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVTAVQ 77
Cdd:cd08271    1 MKAWVLPKPGaalQLTLEEIEIPGPGA-GEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTGWK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  78 KGDRVVIpfviacgscffcnidlfaacettntgrgaiinkksippgaalfgfsHLYGGIPGGQAEYVRVPKAnvGPFKVP 157
Cdd:cd08271   80 VGDRVAY----------------------------------------------HASLARGGSFAEYTVVDAR--AVLPLP 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 158 GTLADEKVLFLSDILPTAWQAVTN-AGIGQGSSVAIYGA-GPVGLMSAACARMLGAEKIFMVD--HHPyrltYAQKTYGV 233
Cdd:cd08271  112 DSLSFEEAAALPCAGLTAYQALFKkLRIEAGRTILITGGaGGVGSFAVQLAKRAGLRVITTCSkrNFE----YVKSLGAD 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 234 IPINFDDDDDPADtiIRQTAGMRGVDGVVDAVGfeakGSTTETILATLKLEG-----------SSGKALRQciaavrrgg 302
Cdd:cd08271  188 HVIDYNDEDVCER--IKEITGGRGVDAVLDTVG----GETAAALAPTLAFNGhlvciqgrpdaSPDPPFTR--------- 252
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492052054 303 VVSVPGVYAGFIHGfmFGDAFDKGLTFKMGQthvhrfmpELLEHIEAGRLEPEAI 357
Cdd:cd08271  253 ALSVHEVALGAAHD--HGDPAAWQDLRYAGE--------ELLELLAAGKLEPLVI 297
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
9-217 6.07e-05

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


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 44.71  E-value: 6.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   9 ANSVKVDTVPDPEIQEaDDIILKVTATAICGSDLHLYRGKIPTV----------EHGDIFGHEFMGIVEETGPAVTAVQK 78
Cdd:cd08246   27 AQAIQLEDVPVPELGP-GEVLVAVMAAGVNYNNVWAALGEPVSTfaarqrrgrdEPYHIGGSDASGIVWAVGEGVKNWKV 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  79 GDRVVIpfviacgscfFCNIDlfaacETTNTGRGAiiNKKSIPPGAALFGFSHLYGGIpggqAEYVRVPKANVGPfkVPG 158
Cdd:cd08246  106 GDEVVV----------HCSVW-----DGNDPERAG--GDPMFDPSQRIWGYETNYGSF----AQFALVQATQLMP--KPK 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492052054 159 TLADEKVLFLSDILPTAWQAVTN---AGIGQGSSVAIYGA-GPVGLMSAACARMLGAEKIFMV 217
Cdd:cd08246  163 HLSWEEAAAYMLVGATAYRMLFGwnpNTVKPGDNVLIWGAsGGLGSMAIQLARAAGANPVAVV 225
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
1-84 4.93e-04

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


Pssm-ID: 176252 [Multi-domain]  Cd Length: 324  Bit Score: 41.94  E-value: 4.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTY--HG--ANSVKVDTVPDPEIQeADDIILKVTATAICGSDLHLYRGKIPTV-EHGDIFGHEFMGIVEETGPAVTA 75
Cdd:cd08292    1 MRAAVHtqFGdpADVLEIGEVPKPTPG-AGEVLVRTTLSPIHNHDLWTIRGTYGYKpELPAIGGSEAVGVVDAVGEGVKG 79

                 ....*....
gi 492052054  76 VQKGDRVVI 84
Cdd:cd08292   80 LQVGQRVAV 88
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
1-82 8.04e-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: 41.36  E-value: 8.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGANSVK-----VD-TVPDPEIQEaDDIILKVTATAICGSDLHLYRGKIPTVEHGDIFGHEFMGIVEETGPAVT 74
Cdd:cd08252    1 MKAIGFTQPLPITdpdslIDiELPKPVPGG-RDLLVRVEAVSVNPVDTKVRAGGAPVPGQPKILGWDASGVVEAVGSEVT 79

                 ....*...
gi 492052054  75 AVQKGDRV 82
Cdd:cd08252   80 LFKVGDEV 87
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-355 1.39e-03

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: 40.43  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   1 MRALTYHGAN--SVKVDTVPDPEIQeADDIILKVTATAICGSDLHLyrgkIPTVEHGDIFGHEFMGIVEE-----TGPAv 73
Cdd:cd08270    1 MRALVVDPDAplRLRLGEVPDPQPA-PHEALVRVAAISLNRGELKF----AAERPDGAVPGWDAAGVVERaaadgSGPA- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  74 tavqKGDRVVIpfviacgscffcnidlfaacettntgrgaiinkksippgaalfgfshlyGGIPGGQAEYVRVPKANVGP 153
Cdd:cd08270   75 ----VGARVVG-------------------------------------------------LGAMGAWAELVAVPTGWLAV 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 154 fkVPGTLADEKVLFLSDILPTAWQAVTNAGIGQGSSVAIYGA-GPVGLMSAACARMLGAEKIFMVDHHPY-----RLTYA 227
Cdd:cd08270  102 --LPDGVSFAQAATLPVAGVTALRALRRGGPLLGRRVLVTGAsGGVGRFAVQLAALAGAHVVAVVGSPARaeglrELGAA 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 228 QKTYGVIPInfddDDDPadtiirqtagmrgVDGVVDAVGfeakgsttetilatlklegssGKALRQCIAAVRRGGVVSVP 307
Cdd:cd08270  180 EVVVGGSEL----SGAP-------------VDLVVDSVG---------------------GPQLARALELLAPGGTVVSV 221
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492052054 308 GVYAGFIHGFMFGDAFDKGL-----TFKMGQ-THVHRFMPELLEHIEAGRLEPE 355
Cdd:cd08270  222 GSSSGEPAVFNPAAFVGGGGgrrlyTFFLYDgEPLAADLARLLGLVAAGRLDPR 275
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
245-369 1.93e-03

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 38.08  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  245 ADTII-------RQTAGMRGVDGVVDAVGfeakgsttetilatlklegssGKALRQCIAAVRRGG-VVSVPGVYAGFIHG 316
Cdd:pfam13602   3 ADEVIdyrttdfVQATGGEGVDVVLDTVG---------------------GEAFEASLRVLPGGGrLVTIGGPPLSAGLL 61
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 492052054  317 FMFGDAFDKGLTFKMGQT---HVHRFMPELLEHIEAGRLEPeaIITHRMSLEDAAK 369
Cdd:pfam13602  62 LPARKRGGRGVKYLFLFVrpnLGADILQELADLIEEGKLRP--VIDRVFPLEEAAE 115
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
2-388 1.96e-03

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: 39.88  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054   2 RALTYHGA---NSVKVDTVPDPEIQEaDDIILKVTAtaiCG---SDLH----LYRG--KIPTVehgdiFGHEFMGIVEET 69
Cdd:cd08275    1 RAVVLTGFgglDKLKVEKEALPEPSS-GEVRVRVEA---CGlnfADLMarqgLYDSapKPPFV-----PGFECAGTVEAV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054  70 GPAVTAVQKGDRVVipfviaCGSCFfcnidlfaacettntgrgaiinkksippgaalfgfshlyggipGGQAEYVRVPKA 149
Cdd:cd08275   72 GEGVKDFKVGDRVM------GLTRF-------------------------------------------GGYAEVVNVPAD 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 150 NVgpFKVP-GTLADEKVLFLSDILpTAWQAVTN-AGIGQGSSVAIYGA-GPVGLMSAACARMLgaEKIFMV-DHHPYRLT 225
Cdd:cd08275  103 QV--FPLPdGMSFEEAAAFPVNYL-TAYYALFElGNLRPGQSVLVHSAaGGVGLAAGQLCKTV--PNVTVVgTASASKHE 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 226 YAQKTYGVIPINFDDDDDPADtiIRQTAGmRGVDGVVDAVGfeakGSTTETILATLKlegSSGKALRQCIAAVRRGGVVS 305
Cdd:cd08275  178 ALKENGVTHVIDYRTQDYVEE--VKKISP-EGVDIVLDALG----GEDTRKSYDLLK---PMGRLVVYGAANLVTGEKRS 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492052054 306 VPGVYAGFIHGF------MFGD-----AFDKGLTFKMGQTHVHRfMPELLEHIEAGRLEPeaIITHRMSLEDAAKGYKLF 374
Cdd:cd08275  248 WFKLAKKWWNRPkvdpmkLISEnksvlGFNLGWLFEERELLTEV-MDKLLKLYEEGKIKP--KIDSVFPFEEVGEAMRRL 324
                        410
                 ....*....|....*
gi 492052054 375 -DKKEEDcrKVILTP 388
Cdd:cd08275  325 qSRKNIG--KVVLTP 337
 
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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