Reviewed, UniProtKB/Swiss-Prot P27354 (MEMB_METTR)

Names and origin

Protein names

Recommended name:
    Methane monooxygenase component A beta chain
    EC=1.14.13.25
Alternative name(s):
    Methane hydroxylase

Gene names

Name:

mmoY

Organism

Methylosinus trichosporium

Taxonomic identifier

426 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylocystaceae › Methylosinus

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	One-carbon metabolism
Ligand	NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular aromatic compound metabolic process Inferred from electronic annotation. Source: InterPro one-carbon compound metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	methane monooxygenase activity Inferred from electronic annotation. Source: EC transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 394

393

Methane monooxygenase component A beta chain

PRO_0000096408

Secondary structure

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394

Helix Strand Turn

Details...

Turn

13 – 15

3

Helix

17 – 26

10

Turn

38 – 41

4

Beta 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

Sequences

	Sequence		Length	Mass (Da)
	P27354-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: FA6C8F0970F28B90	FASTA	394	45,020
	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

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: 1904125] [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: 1845980] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X55394 Genomic DNA. Translation: CAA39069.1.

PIR

S15208.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MHY	X-ray	2.00	B	1-394	[»]
1MHZ	X-ray	2.70	B	1-394	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-3868.

BRENDA

1.14.13.25. 20437.

Family and domain databases

InterPro

IPR012078. MP_mOase_hydro.
IPR003430. Phenol_Hydrox.
IPR012348. Ribncl_red_rel.
[Graphical view]

Gene3D

G3DSA:1.10.620.20. Ribncl_red_rel. 1 hit.

Pfam

PF02332. Phenol_Hydrox. 1 hit.
[Graphical view]

PIRSF

PIRSF000040. MMOH_comp. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MEMB_METTR

Accession

Primary (citable) accession number: P27354

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 56 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)