[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=OB3b; PubMed=1904125 [NCBI, ExPASy, EBI, Israel, Japan] Cardy D.L.N., Laidler V., Salmond G.P.C., Murrell J.C.; "Molecular analysis of the methane monooxygenase (MMO) gene cluster of Methylosinus trichosporium OB3b."; Mol. Microbiol. 5:335-342(1991).
[2]	PROTEIN SEQUENCE OF 2-16. PubMed=1845980 [NCBI, ExPASy, EBI, Israel, Japan] Fox B.G., Liu Y., Dege J.E., Lipscomb J.D.; "Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction."; J. Biol. Chem. 266:540-550(1991).

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: 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.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X55394; CAA39069.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S15208; S15208.

3D structure databases

PDB

1MHY; X-ray; 2.00 A; B=1-394.	[ExPASy / RCSB / EBI]
1MHZ; X-ray; 2.70 A; B=1-394.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1MHY; -.
1MHZ; -.

ModBase

P27354.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-3868; -.

Ontologies

GO:0015049;	Molecular function: methane monooxygenase activity (inferred from electronic annotation from EC).
GO:0046914;	Molecular function: transition metal ion binding (inferred from electronic annotation from InterPro).
GO:0006725;	Biological process: cellular aromatic compound metabolic process (inferred from electronic annotation from InterPro).
GO:0006730;	Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR012078; MP_mOase_hydro.
IPR003430; Phenol_Hydrox.
IPR012348; Ribncl_red_rel.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.620.20; Ribncl_red_rel; 1.

Pfam

PF02332; Phenol_Hydrox; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000040; MMOH_comp; 1.

Other

P27354; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Monooxygenase; NADP; One-carbon metabolism; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 394`	`393`	`Methane monooxygenase component A beta chain.`	`PRO_0000096408`
`TURN`	`13 15`	`3`
`HELIX`	`17 26`	`10`
`TURN`	`38 41`	`4`
`STRAND`	`45 48`	`4`
`HELIX`	`51 56`	`6`
`HELIX`	`88 90`	`3`
`HELIX`	`109 133`	`25`
`HELIX`	`135 138`	`4`
`HELIX`	`141 145`	`5`
`HELIX`	`148 172`	`25`
`HELIX`	`176 206`	`31`
`HELIX`	`215 223`	`9`
`HELIX`	`225 227`	`3`
`HELIX`	`228 239`	`12`
`HELIX`	`244 253`	`10`
`HELIX`	`255 264`	`10`
`TURN`	`265 267`	`3`
`HELIX`	`268 272`	`5`
`TURN`	`273 276`	`4`
`HELIX`	`280 302`	`23`
`HELIX`	`303 307`	`5`
`TURN`	`310 312`	`3`
`HELIX`	`313 338`	`26`
`HELIX`	`339 344`	`6`
`TURN`	`349 351`	`3`
`HELIX`	`354 375`	`22`
`HELIX`	`381 389`	`9`

Sequence information

Length: 394 AA [This is the length of the unprocessed precursor]

Molecular weight: 45020 Da [This is the MW of the unprocessed precursor]

CRC64: FA6C8F0970F28B90 [This is a checksum on the sequence]

        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

P27354 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools