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P38540 (DHM2_METME) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 87. 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 2

EC=1.1.2.7
Alternative name(s):
MDH small subunit beta
MDH-associated peptide
MEDH
Gene names
Name:moxI
OrganismMethylophilus methylotrophus (Bacterium W3A1)
Taxonomic identifier17 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylophilus

Protein attributes

Sequence length91 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of primary alcohols including methanol By similarity.

Catalytic activity

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

Subunit structure

Heterotetramer composed 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 methanol dehydrogenase subunit 2 family.

Sequence caution

The sequence AAA83766.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.2
Chain23 – 9169Methanol dehydrogenase [cytochrome c] subunit 2
PRO_0000025570

Amino acid modifications

Disulfide bond28 ↔ 34

Experimental info

Sequence conflict271N → T AA sequence Ref.2
Sequence conflict311P → A AA sequence Ref.2
Sequence conflict371N → A AA sequence Ref.2

Secondary structure

..... 91
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38540 [UniParc].

Last modified November 8, 2002. Version 2.
Checksum: 0123300087E6716A

FASTA9110,037
        10         20         30         40         50         60 
MKHVLTLLAL ASVFAVSNQA LAYDGQNCKE PGNCWENKPG YPEKIAGSKY DPKHDPVELN 

        70         80         90 
KQEESIKAMD ARNAKRIANA KSSGNFVFDV K 

« 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]"The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria."
Cox J.M., Day D.J., Anthony C.
Biochim. Biophys. Acta 1119:97-106(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-53.
Strain: ATCC 53528 / AS1 / DSM 46235 / LMG 6787 / NCIMB 10515.
[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
U41041 Genomic DNA. Translation: AAA83766.1. Different initiation.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G72X-ray1.90B/D23-91[»]
2AD6X-ray1.50B/D23-91[»]
2AD7X-ray1.50B/D23-91[»]
2AD8X-ray1.60B/D23-91[»]
4AAHX-ray2.40B/D23-91[»]
ProteinModelPortalP38540.
SMRP38540. Positions 23-91.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP38540.

Family and domain databases

Gene3D4.10.160.10. 1 hit.
InterProIPR003420. Meth_DH_bsu.
[Graphical view]
PfamPF02315. MDH. 1 hit.
[Graphical view]
PIRSFPIRSF029163. Meth_DH_beta. 1 hit.
SUPFAMSSF48666. SSF48666. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP38540.

Entry information

Entry nameDHM2_METME
AccessionPrimary (citable) accession number: P38540
Secondary accession number(s): Q59541
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 8, 2002
Last modified: October 16, 2013
This is version 87 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