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Conserved domains on  [gi|1824660074|gb|QIQ50934|]
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methanol dehydrogenase large subunit, partial [uncultured Methyloversatilis sp.]

Protein Classification

PQQ-binding-like beta-propeller repeat protein( domain architecture ID 29103)

PQQ (pyrroloquinoline quinone)-binding-like beta-propeller repeat protein

Gene Ontology:  GO:0070968
PubMed:  16232604|11831471

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PQQ_DH_like super family cl11493
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ...
 1-156 2.09e-49

PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ.


The actual alignment was detected with superfamily member cd10277:

Pssm-ID: 472205 [Multi-domain]  Cd Length: 529  Bit Score: 166.32  E-value: 2.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824660074   1 WQTASFDVEQNMVVIGTGNPAPWNTWKRtaEGDSptkwpsLFTSGQAYVDAATGELKGFFSHTPNDAWDFSGNNSVLLFE 80
Cdd:cd10277   214 WLTGTYDPETNLLYWGVGNPAPWNGDLR--PGDN------LYTSSVLALDPDTGKIKWHYQYTPNDTWDYDGVNEPVLFD 285

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1824660074  81 YkdPKSGKQVKASAHADRNGYFFVTDREKlatgagypwkqSALIGAWPFVDGITWSKGfDSKTGLPNVVESQYPPK 156
Cdd:cd10277   286 Y--TKNGKPVKALVHADRNGFFYVLDRTN-----------GKLIWATPFVKKITWASI-DLKTGRPIYDEDKVPPK 347
 
Name Accession Description Interval E-value
PQQ_ADH_I cd10277
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ...
 1-156 2.09e-49

Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); This bacterial family of homodimeric ethanol dehydrogenases utilize pyrroloquinoline quinone (PQQ) as a cofactor. It represents proteins whose expression may be induced by ethanol, and which are similar to quinoprotein methanol dehydrogenases, but have higher specificities for ethanol and other primary and secondary alcohols. Dehydrogenases with PQQ cofactors, such as ethanol, methanol, and membrane-bound glucose dehydrogenases, form an 8-bladed beta-propeller.


Pssm-ID: 199835 [Multi-domain]  Cd Length: 529  Bit Score: 166.32  E-value: 2.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824660074   1 WQTASFDVEQNMVVIGTGNPAPWNTWKRtaEGDSptkwpsLFTSGQAYVDAATGELKGFFSHTPNDAWDFSGNNSVLLFE 80
Cdd:cd10277   214 WLTGTYDPETNLLYWGVGNPAPWNGDLR--PGDN------LYTSSVLALDPDTGKIKWHYQYTPNDTWDYDGVNEPVLFD 285

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1824660074  81 YkdPKSGKQVKASAHADRNGYFFVTDREKlatgagypwkqSALIGAWPFVDGITWSKGfDSKTGLPNVVESQYPPK 156
Cdd:cd10277   286 Y--TKNGKPVKALVHADRNGFFYVLDRTN-----------GKLIWATPFVKKITWASI-DLKTGRPIYDEDKVPPK 347
PQQ_enz_alc_DH TIGR03075
PQQ-dependent dehydrogenase, methanol/ethanol family; This protein family has a phylogenetic ...
 1-164 8.52e-47

PQQ-dependent dehydrogenase, methanol/ethanol family; This protein family has a phylogenetic distribution very similar to that coenzyme PQQ biosynthesis enzymes, as shown by partial phylogenetic profiling. Genes in this family often are found adjacent to the PQQ biosynthesis genes themselves. An unusual, strained disulfide bond between adjacent Cys residues contributes to PQQ-binding, as does a Trp residue that is part of a PQQ enzyme repeat (see pfam01011). Characterized members include the dehydrogenase subunit of a membrane-anchored, three subunit alcohol (ethanol) dehydrogenase of Gluconobacter suboxydans, a homodimeric ethanol dehydrogenase in Pseudomonas aeruginosa, and the large subunit of an alpha2/beta2 heterotetrameric methanol dehydrogenase in Methylobacterium extorquens.


Pssm-ID: 274419 [Multi-domain]  Cd Length: 527  Bit Score: 159.38  E-value: 8.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824660074   1 WQTASFDVEQNMVVIGTGNPAPWNTWKRtaEGDsptkwpSLFTSGQAYVDAATGELKGFFSHTPNDAWDFSGNNSVLLFE 80
Cdd:TIGR03075 236 WGTGSYDPETNLIYFGTGNPAPWNSHLR--PGD------NLYTSSIVARDPDTGKIKWHYQTTPHDEWDYDGVNEMILFD 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824660074  81 YKdpKSGKQVKASAHADRNGYFFVTDREklaTGagypwkqsALIGAWPFVDGITWSKGFDSKTGLPNVVESQYPPKPKAG 160
Cdd:TIGR03075 308 LK--KDGKPRKLLAHADRNGFFYVLDRT---NG--------KLLSAEPFVDKVNWATGVDLKTGRPIEVPEARSTDGKKG 374


                  ....
gi 1824660074 161 ADKG 164
Cdd:TIGR03075 375 KPVE 378
Gcd COG4993
Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism];
1-150 1.68e-35

Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism];


Pssm-ID: 444017 [Multi-domain]  Cd Length: 515  Bit Score: 128.74  E-value: 1.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824660074   1 WQTASFDVEQNMVVIGTGNPAP-WNTWKRtaEGDSptkwpsLFTSGQAYVDAATGELKGFFSHTPNDAWDFSGNNSVLLF 79
Cdd:COG4993   208 WGTMSYDPELGLVYLPTGNPAPdWNGGQR--PGDN------LYSSSIVALDADTGELKWHYQTVPHDLWDYDGPNEPILV 279

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1824660074  80 EYkdPKSGKQVKASAHADRNGYFFVTDREklaTGagypwkqsALIGAWPFVDGITWSKGFDSKTGLPNVVE 150
Cdd:COG4993   280 DL--PVDGKTRKALVQATKNGFIYVLDRE---TG--------EPLVTQPFVKPPNWATEIDMWGATPIQTP 337
 
Name Accession Description Interval E-value
PQQ_ADH_I cd10277
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ...
 1-156 2.09e-49

Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); This bacterial family of homodimeric ethanol dehydrogenases utilize pyrroloquinoline quinone (PQQ) as a cofactor. It represents proteins whose expression may be induced by ethanol, and which are similar to quinoprotein methanol dehydrogenases, but have higher specificities for ethanol and other primary and secondary alcohols. Dehydrogenases with PQQ cofactors, such as ethanol, methanol, and membrane-bound glucose dehydrogenases, form an 8-bladed beta-propeller.


Pssm-ID: 199835 [Multi-domain]  Cd Length: 529  Bit Score: 166.32  E-value: 2.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824660074   1 WQTASFDVEQNMVVIGTGNPAPWNTWKRtaEGDSptkwpsLFTSGQAYVDAATGELKGFFSHTPNDAWDFSGNNSVLLFE 80
Cdd:cd10277   214 WLTGTYDPETNLLYWGVGNPAPWNGDLR--PGDN------LYTSSVLALDPDTGKIKWHYQYTPNDTWDYDGVNEPVLFD 285

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1824660074  81 YkdPKSGKQVKASAHADRNGYFFVTDREKlatgagypwkqSALIGAWPFVDGITWSKGfDSKTGLPNVVESQYPPK 156
Cdd:cd10277   286 Y--TKNGKPVKALVHADRNGFFYVLDRTN-----------GKLIWATPFVKKITWASI-DLKTGRPIYDEDKVPPK 347
PQQ_enz_alc_DH TIGR03075
PQQ-dependent dehydrogenase, methanol/ethanol family; This protein family has a phylogenetic ...
 1-164 8.52e-47

PQQ-dependent dehydrogenase, methanol/ethanol family; This protein family has a phylogenetic distribution very similar to that coenzyme PQQ biosynthesis enzymes, as shown by partial phylogenetic profiling. Genes in this family often are found adjacent to the PQQ biosynthesis genes themselves. An unusual, strained disulfide bond between adjacent Cys residues contributes to PQQ-binding, as does a Trp residue that is part of a PQQ enzyme repeat (see pfam01011). Characterized members include the dehydrogenase subunit of a membrane-anchored, three subunit alcohol (ethanol) dehydrogenase of Gluconobacter suboxydans, a homodimeric ethanol dehydrogenase in Pseudomonas aeruginosa, and the large subunit of an alpha2/beta2 heterotetrameric methanol dehydrogenase in Methylobacterium extorquens.


Pssm-ID: 274419 [Multi-domain]  Cd Length: 527  Bit Score: 159.38  E-value: 8.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824660074   1 WQTASFDVEQNMVVIGTGNPAPWNTWKRtaEGDsptkwpSLFTSGQAYVDAATGELKGFFSHTPNDAWDFSGNNSVLLFE 80
Cdd:TIGR03075 236 WGTGSYDPETNLIYFGTGNPAPWNSHLR--PGD------NLYTSSIVARDPDTGKIKWHYQTTPHDEWDYDGVNEMILFD 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824660074  81 YKdpKSGKQVKASAHADRNGYFFVTDREklaTGagypwkqsALIGAWPFVDGITWSKGFDSKTGLPNVVESQYPPKPKAG 160
Cdd:TIGR03075 308 LK--KDGKPRKLLAHADRNGFFYVLDRT---NG--------KLLSAEPFVDKVNWATGVDLKTGRPIEVPEARSTDGKKG 374


                  ....
gi 1824660074 161 ADKG 164
Cdd:TIGR03075 375 KPVE 378
Gcd COG4993
Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism];
1-150 1.68e-35

Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism];


Pssm-ID: 444017 [Multi-domain]  Cd Length: 515  Bit Score: 128.74  E-value: 1.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824660074   1 WQTASFDVEQNMVVIGTGNPAP-WNTWKRtaEGDSptkwpsLFTSGQAYVDAATGELKGFFSHTPNDAWDFSGNNSVLLF 79
Cdd:COG4993   208 WGTMSYDPELGLVYLPTGNPAPdWNGGQR--PGDN------LYSSSIVALDADTGELKWHYQTVPHDLWDYDGPNEPILV 279

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1824660074  80 EYkdPKSGKQVKASAHADRNGYFFVTDREklaTGagypwkqsALIGAWPFVDGITWSKGFDSKTGLPNVVE 150
Cdd:COG4993   280 DL--PVDGKTRKALVQATKNGFIYVLDRE---TG--------EPLVTQPFVKPPNWATEIDMWGATPIQTP 337
PQQ_DH_like cd00216
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ...
 1-107 3.73e-27

PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ.


Pssm-ID: 199833 [Multi-domain]  Cd Length: 434  Bit Score: 105.38  E-value: 3.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824660074   1 WQTASFDVEQNMVVIGTGNPAPWNTWKRTAEGDSptkwpsLFTSGQAYVDAATGELKGFFSHTPNDAWDFSGNNSVLLFE 80
Cdd:cd00216   196 WSSAAYDAELNLIYVGGGNPTPWNWGGNRTPGDN------LYTSSIVAVNADTGEMKWQYQTTPHDAWDYDGDNTPVLAD 269

                          90       100
                  ....*....|....*....|....*..
gi 1824660074  81 YKDpkSGKQVKASAHADRNGYFFVTDR 107
Cdd:cd00216   270 IKV--KGKKVKVLFAPAKNGNFYVLDR 294
PQQ_ADH_II cd10279
PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of ...
 1-158 9.49e-25

PQQ_like domain of the quinohemoprotein alcohol dehydrogenase (type II); This family of monomeric and soluble type II alcohol dehydrogenases utilizes pyrroloquinoline quinone (PQQ) as a cofactor and is related to ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller.


Pssm-ID: 199837 [Multi-domain]  Cd Length: 549  Bit Score: 99.26  E-value: 9.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824660074   1 WQTASFDVEQNMVVIGTGNPAPWNTWKRtaegdSPTKWPSLFTSGQAYVDAATGELKGFFSHTPNDAWDFSGNNSVLLFE 80
Cdd:cd10279   217 WDSITYDPELDLLYIGTGNGSPWNRKVR-----SPGGGDNLFLSSIVALDADTGRYKWHYQTTPGDTWDYTATQPIILAD 291

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1824660074  81 YkdPKSGKQVKASAHADRNGYFFVTDReklATGagypwkqsALIGAWPFVDgITWSKGFDSKTGLPNVV-ESQYPPKPK 158
Cdd:cd10279   292 L--EIDGKPRKVLMHAPKNGFFYVLDR---ATG--------KLLSAEPFVP-VNWATGIDLKTGRPIENpEARYTKGPK 356
PQQ_MDH cd10278
Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the ...
 1-162 1.43e-22

Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the utilization of C1 compounds as a source of energy and carbon by bacteria. It catalyzes the oxidation of methanol to formaldehyde, transfering two electrons per methanol to cytochrome c(L) as the acceptor. Methanol dehydrogenase belongs to a family of dehydrogenases with pyrroloquinoline quinone (PQQ) as cofactor, which also includes dehydrogenases specific to other alcohols and membrane-bound glucose dehydrogenases. This alignment model for the large subunit contains an 8-bladed beta-propeller; the functional enzyme forms a heterotetramer composed of two large and two small subunits.


Pssm-ID: 199836 [Multi-domain]  Cd Length: 553  Bit Score: 93.16  E-value: 1.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824660074   1 WQTASFDVEQNMVVIGTGNPAPWNTWKRTaeGDSptKWP-SLFTSgqayvDAATGELKGFFSHTPNDAWDFSGNNSVLLF 79
Cdd:cd10278   224 WGWYSYDPKLNLVYYGTGNPGPWNPTQRP--GDN--KWSmTIFAR-----DPDTGEAKWAYQMTPHDEWDYDGVNEMILV 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824660074  80 EYkdPKSGKQVKASAHADRNGYFFVTDREklaTGagypwkqsALIGAWPFVDgITWSKGFDSKTGLPNVVESQYPPKPKA 159
Cdd:cd10278   295 DQ--TVDGKKRKLLVHFDRNGFVYTLDRT---TG--------ELLSAEKFDP-VNNWKGVDLKTGRPVKDPEKSTHMDHN 360


                  ...
gi 1824660074 160 GAD 162
Cdd:cd10278   361 VTD 363
PQQ_mGDH cd10280
Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes ...
 1-113 3.43e-06

Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes belongs to the dehydrogenase family with pyrroloquinoline quinone (PQQ) as cofactor, and is the only subfamily that is bound to the membrane. Glucose dehydrogenase converts D-glucose to D-glucono-1,5-lactone in a reaction that is coupled with the respiratory chain in the periplasmic oxidation of sugars and alcohols in gram-negative bacteria. Ubiquinone functions as the electron acceptor. The alignment model contains an 8-bladed beta-propeller.


Pssm-ID: 199838 [Multi-domain]  Cd Length: 616  Bit Score: 45.65  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824660074   1 WQTASFDVEQNMVVIGTGNPAPwNTW--KRTAEGdsptkwpsLFTSGQAYVDAATGELKGFFSHTPNDAWDFSGNNSVLL 78
Cdd:cd10280   231 WAGMSADEKLGLVYLPTGSATP-DFYggDRPGDN--------LFANSLVALDAATGKRRWHFQTVHHDLWDYDLPAQPTL 301

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1824660074  79 FEYkdPKSGKQVKASAHADRNGYFFVTDREklaTG 113
Cdd:cd10280   302 VDV--PRDGKTVPAVAQPTKQGFVFVLDRR---TG 331
 
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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