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P27353 (MEMA_METTR) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 82. 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 alpha chain

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

Protein attributes

Sequence length526 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.

Cofactor

Binds 2 iron ions.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 526525Methane monooxygenase component A alpha chain
PRO_0000096406

Sites

Active site1511 Potential
Metal binding1141Iron 1 By similarity
Metal binding1441Iron 1 By similarity
Metal binding1471Iron 1 By similarity
Metal binding2091Iron 2 By similarity
Metal binding2431Iron 2 By similarity
Metal binding2461Iron 2 By similarity

Secondary structure

................................................................................ 526
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27353 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: A56F4AAD0A55726B

FASTA52659,954
        10         20         30         40         50         60 
MAISLATKAA TDALKVNRAP VGVEPQEVHK WLQSFNWDFK ENRTKYPTKY HMANETKEQF 

        70         80         90        100        110        120 
KVIAKEYARM EAAKDERQFG TLLDGLTRLG AGNKVHPRWG ETMKVISNFL EVGEYNAIAA 

       130        140        150        160        170        180 
SAMLWDSATA AEQKNGYLAQ VLDEIRHTHQ CAFINHYYSK HYHDPAGHND ARRTRAIGPL 

       190        200        210        220        230        240 
WKGMKRVFAD GFISGDAVEC SVNLQLVGEA CFTNPLIVAV TEWASANGDE ITPTVFLSVE 

       250        260        270        280        290        300 
TDELRHMANG YQTVVSIAND PASAKFLNTD LNNAFWTQQK YFTPVLGYLF EYGSKFKVEP 

       310        320        330        340        350        360 
WVKTWNRWVY EDWGGIWIGR LGKYGVESPA SLRDAKRDAY WAHHDLALAA YAMWPLGFAR 

       370        380        390        400        410        420 
LALPDEEDQA WFEANYPGWA DHYGKIFNEW KKLGYEDPKS GFIPYQWLLA NGHDVYIDRV 

       430        440        450        460        470        480 
SQVPFIPSLA KGTGSLRVHE FNGKKHSLTD DWGERQWLIE PERYECHNVF EQYEGRELSE 

       490        500        510        520 
VIAEGHGVRS DGKTLIAQPH TRGDNLWTLE DIKRAGCVFP DPLAKF 

« 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]McDonald I.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"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: CAA39068.2.
PIRS15207.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MHYX-ray2.00D1-525[»]
1MHZX-ray2.70D1-525[»]
ProteinModelPortalP27353.
SMRP27353. Positions 17-526.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC38005870. VBIMetTri17036_0736.

Family and domain databases

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

Other

EvolutionaryTraceP27353.

Entry information

Entry nameMEMA_METTR
AccessionPrimary (citable) accession number: P27353
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: December 11, 2013
This is version 82 of the entry and version 4 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