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P38539 (DHM1_METME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methanol dehydrogenase [cytochrome c] subunit 1

EC=1.1.2.7
Alternative name(s):
MDH large subunit alpha
MEDH
OrganismMethylophilus methylotrophus (Bacterium W3A1)
Taxonomic identifier17 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylophilus

Protein attributes

Sequence length573 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of primary alcohols including methanol.

Catalytic activity

A primary alcohol + 2 cytochrome c(L) = an aldehyde + 2 reduced cytochrome c(L) + 2 H+.

Cofactor

Binds 1 calcium ion per subunit.

Binds 1 PQQ per subunit. PQQ is inserted between disulfide Cys-105-Cys-106 and the indole ring of Trp-239.

Subunit structure

Heterotetramer of 2 alpha and 2 beta subunits.

Subcellular location

Cell inner membrane; Peripheral membrane protein; Periplasmic side. Note: Periplasmic, but associated with inner membrane.

Sequence similarities

Belongs to the bacterial PQQ dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 573573Methanol dehydrogenase [cytochrome c] subunit 1
PRO_0000205342

Sites

Active site2991Proton acceptor
Metal binding1731Calcium
Metal binding2571Calcium

Amino acid modifications

Disulfide bond105 ↔ 106
Disulfide bond146 ↔ 169
Disulfide bond381 ↔ 410

Secondary structure

.......................................................................................................................... 573
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38539 [UniParc].

Last modified November 8, 2002. Version 2.
Checksum: A06C9B3091BB8F0C

FASTA57362,635
        10         20         30         40         50         60 
MADADLDKQV NTAGAWPIAT GGYYSQHNSP LAQINKSNVK NVKAAWSFST GVLNGHEGAP 

        70         80         90        100        110        120 
LVIGDMMYVH SAFPNNTYAL NLNDPGKIVW QHKPKQDAST KAVMCCDVVD RGLAYGAGQI 

       130        140        150        160        170        180 
VKKQANGHLL ALDAKTGKIN WEVEVCDPKV GSTLTQAPFV AKDTVLMGCS GAELGVRGAV 

       190        200        210        220        230        240 
NAFDLKTGEL KWRAFATGSD DSVRLAKDFN SANPHYGQFG LGTKTWEGDA WKIGGGTNWG 

       250        260        270        280        290        300 
WYAYDPKLNL FYYGSGNPAP WNETMRPGDN KWTMTIWGRD LDTGMAKWGY QKTPHDEWDF 

       310        320        330        340        350        360 
AGVNQMVLTD QPVNGKMTPL LSHIDRNGIL YTLNRENGNL IVAEKVDPAV NVFKKVDLKT 

       370        380        390        400        410        420 
GTPVRDPEFA TRMDHKGTNI CPSAMGFHNQ GVDSYDPESR TLYAGLNHIC MDWEPFMLPY 

       430        440        450        460        470        480 
RAGQFFVGAT LAMYPGPNGP TKKEMGQIRA FDLTTGKAKW TKWEKFAAWG GTLYTKGGLV 

       490        500        510        520        530        540 
WYATLDGYLK ALDNKDGKEL WNFKMPSGGI GSPMTYSFKG KQYIGSMYGV GGWPGVGLVF 

       550        560        570 
DLTDPSAGLG AVGAFRELQN HTQMGGGLMV FSL 

« Hide

References

[1]"Determination of the gene sequence and the three-dimensional structure at 2.4 angstroms resolution of methanol dehydrogenase from Methylophilus W3A1."
Xia Z.-X., Dai W.-W., Zhang Y.-F., White S.A., Boyd G.D., Mathews F.S.
J. Mol. Biol. 259:480-501(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[2]"Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes."
Anthony C.
Antioxid. Redox Signal. 3:757-774(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[3]"The active site structure of the calcium-containing quinoprotein methanol dehydrogenase."
White S.A., Boyd G.D., Mathews F.S., Xia Z.-X., Dai W.-W., Zhang Y.-F., Davidson V.L.
Biochemistry 32:12955-12958(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[4]"The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-A resolution."
Xia Z.-X., Dai W.-W., Xiong J.-P., Hao Z.-P., Davidson V.L., White S.A., Mathews F.S.
J. Biol. Chem. 267:22289-22297(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U41040 Genomic DNA. Translation: AAA83765.1.
PIRS68591.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G72X-ray1.90A/C1-573[»]
2AD6X-ray1.50A/C3-573[»]
2AD7X-ray1.50A/C3-573[»]
2AD8X-ray1.60A/C3-573[»]
4AAHX-ray2.40A/C3-573[»]
ProteinModelPortalP38539.
SMRP38539. Positions 3-573.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP38539.

Family and domain databases

Gene3D2.140.10.10. 1 hit.
InterProIPR018391. PQQ_beta_propeller_repeat.
IPR017512. PQQ_MeOH/EtOH_DH.
IPR002372. PQQ_repeat.
IPR027295. Quinonprotein_ADH-like_fam.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR001479. Quinoprotein_DH_CS.
[Graphical view]
PfamPF01011. PQQ. 5 hits.
[Graphical view]
SMARTSM00564. PQQ. 4 hits.
[Graphical view]
SUPFAMSSF50998. SSF50998. 1 hit.
TIGRFAMsTIGR03075. PQQ_enz_alc_DH. 1 hit.
PROSITEPS00364. BACTERIAL_PQQ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP38539.

Entry information

Entry nameDHM1_METME
AccessionPrimary (citable) accession number: P38539
Secondary accession number(s): Q59540
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 8, 2002
Last modified: February 19, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references