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P27354 (MEMB_METTR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Methane monooxygenase component A beta chain

EC=1.14.13.25
Alternative name(s):
Methane hydroxylase
Gene names
Name:mmoY
OrganismMethylosinus trichosporium
Taxonomic identifier426 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylocystaceaeMethylosinus

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds.

Catalytic activity

Methane + NAD(P)H + O2 = methanol + NAD(P)+ + H2O.

Subunit structure

M.trichosporium has two forms of methane monooxygenase, a soluble and a membrane-bound type. The soluble type consists of four components (A to D): protein A, comprising three chains, in an alpha-2, beta-2, gamma-2 configuration, is a nonheme iron protein containing an unusual mu-hydroxo bridge structure at its active site and interacts with both oxygen and methane.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   LigandNADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcellular aromatic compound metabolic process

Inferred from electronic annotation. Source: InterPro

one-carbon metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmethane monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 394393Methane monooxygenase component A beta chain
PRO_0000096408

Secondary structure

.................................................. 394
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27354 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: FA6C8F0970F28B90

FASTA39445,020
        10         20         30         40         50         60 
MSQPQSSQVT KRGLTDPERA AIIAAAVPDH ALDTQRKYHY FIQPRWKPLS EYEQLSCYAQ 

        70         80         90        100        110        120 
PNPDWIAGGL DWGDWTQKFH GGRPSWGNES TELRTTDWYR HRDPARRWHH PYVKDKSEEA 

       130        140        150        160        170        180 
RYTQRFLAAY SSEGSIRTID PYWRDEILNK YFGALLYSEY GLFNAHSSVG RDCLSDTIRQ 

       190        200        210        220        230        240 
TAVFAALDKV DNAQMIQMER LFIAKLVPGF DASTDVPKKI WTTDPIYSGA RATVQEIWQG 

       250        260        270        280        290        300 
VQDWNEILWA GHAVMIATFG QFARREFFQR LATVYGDTLT PFFTAQSQTY FQTTRGAIDD 

       310        320        330        340        350        360 
LFVYCLANDS EFGAHNRTFL NAWTEHYLAS SVAALKDFVG LYAKVEKSRA DRSRRRLRGA 

       370        380        390 
AASSAIGRSI TPDKIGFRVD VDQKVDAVLA GYKN 

« Hide

References

[1]"Molecular analysis of the methane monooxygenase (MMO) gene cluster of Methylosinus trichosporium OB3b."
Cardy D.L.N., Laidler V., Salmond G.P.C., Murrell J.C.
Mol. Microbiol. 5:335-342(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: OB3b.
[2]"Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction."
Fox B.G., Liu Y., Dege J.E., Lipscomb J.D.
J. Biol. Chem. 266:540-550(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55394 Genomic DNA. Translation: CAA39069.1.
PIRS15208.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MHYX-ray2.00B1-394[»]
1MHZX-ray2.70B1-394[»]
ProteinModelPortalP27354.
SMRP27354. Positions 11-392.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3868.

Family and domain databases

Gene3D1.10.620.20. 1 hit.
InterProIPR009078. Ferritin-like_SF.
IPR012078. MP_mOase_hydro.
IPR003430. Phenol_Hydrox.
IPR012348. RNR-rel.
[Graphical view]
PfamPF02332. Phenol_Hydrox. 1 hit.
[Graphical view]
PIRSFPIRSF000040. MMOH_comp. 1 hit.
SUPFAMSSF47240. SSF47240. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP27354.

Entry information

Entry nameMEMB_METTR
AccessionPrimary (citable) accession number: P27354
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: January 22, 2014
This is version 76 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references