Reviewed, UniProtKB/Swiss-Prot P22869 (MEMA_METCA)

Names and origin

Protein names

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

Gene names

Name:	mmoX
Ordered Locus Names:	MCA1194

Organism

Methylococcus capsulatus [Complete proteome] [HAMAP]

Taxonomic identifier

414 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Methylococcales › Methylococcaceae › Methylococcus

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Cofactor	Binds 2 iron ions.
Subunit structure	M.capsulatus 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	Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Complete proteome 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	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW methane monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 527

527

Methane monooxygenase component A alpha chain

PRO_0000096405

Sites

Active site

151

1

Potential

Metal binding

114

1

Iron 1

Metal binding

144

1

Iron 1

Metal binding

147

1

Iron 1

Metal binding

209

1

Iron 2

Metal binding

243

1

Iron 2

Metal binding

246

1

Iron 2

Experimental info

Sequence conflict

306

1

N → D in AAB62392. Ref.2

Sequence conflict

444

1

Q → E in AAB62392. Ref.2

Secondary structure

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527

Helix Strand Turn

Details...

Helix

25 – 29

5

Helix

30 – 35

6

Helix

64 – 83

20

Helix

85 – 88

4

Turn

89 – 93

5

Helix

97 – 127

31

Helix

131 – 161

31

Turn

166 – 170

5

Helix

171 – 174

4

Beta strand

177 – 179

3

Helix

180 – 188

9

Helix

190 – 193

4

Helix

197 – 204

8

Turn

205 – 207

3

Helix

208 – 211

4

Helix

213 – 226

14

Helix

231 – 258

28

Helix

261 – 292

32

Helix

301 – 309

9

Helix

310 – 315

6

Helix

316 – 320

5

Helix

321 – 324

4

Helix

332 – 352

21

Helix

354 – 356

3

Beta strand

357 – 360

4

Helix

366 – 375

10

Helix

379 – 392

14

Turn

393 – 396

4

Helix

404 – 410

7

Turn

419 – 421

3

Turn

427 – 429

3

Beta strand

436 – 441

6

Beta strand

444 – 450

7

Helix

451 – 459

9

Helix

461 – 463

3

Helix

469 – 473

5

Helix

478 – 484

7

Beta strand

492 – 496

5

Beta strand

498 – 500

3

Beta strand

503 – 505

3

Helix

509 – 513

5

Turn

514 – 516

3

Helix

522 – 525

4

Sequences

	Sequence		Length	Mass (Da)
	P22869-1 [UniParc]. Last modified December 7, 2004. Version 3. Checksum: 953438FDF5208374	FASTA	527	60,646
	10 20 30 40 50 60 MALSTATKAA TDALAANRAP TSVNAQEVHR WLQSFNWDFK NNRTKYATKY KMANETKEQF 70 80 90 100 110 120 KLIAKEYARM EAVKDERQFG SLQDALTRLN AGVRVHPKWN ETMKVVSNFL EVGEYNAIAA 130 140 150 160 170 180 TGMLWDSAQA AEQKNGYLAQ VLDEIRHTHQ CAYVNYYFAK NGQDPAGHND ARRTRTIGPL 190 200 210 220 230 240 WKGMKRVFSD GFISGDAVEC SLNLQLVGEA CFTNPLIVAV TEWAAANGDE ITPTVFLSIE 250 260 270 280 290 300 TDELRHMANG YQTVVSIAND PASAKYLNTD LNNAFWTQQK YFTPVLGMLF EYGSKFKVEP 310 320 330 340 350 360 WVKTWNRWVY EDWGGIWIGR LGKYGVESPR SLKDAKQDAY WAHHDLYLLA YALWPTGFFR 370 380 390 400 410 420 LALPDQEEME WFEANYPGWY DHYGKIYEEW RARGCEDPSS GFIPLMWFIE NNHPIYIDRV 430 440 450 460 470 480 SQVPFCPSLA KGASTLRVHE YNGQMHTFSD QWGERMWLAE PERYECQNIF EQYEGRELSE 490 500 510 520 VIAELHGLRS DGKTLIAQPH VRGDKLWTLD DIKRLNCVFK NPVKAFN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath)." Stainthorpe A.C., Lees V., Salmond G.P.C., Dalton H., Murrell J.C. Gene 91:27-34(1990) [PubMed: 2205538] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6. Strain: Bath / NCIMB 11132.
[2]	McDonald I., Murrell J.C. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 84; 306 AND 444.
[3]	"Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath)." Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S., Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E., Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J. , Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L., Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H., Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R., Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A. PLoS Biol. 2:1616-1628(2004) [PubMed: 15383840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bath / NCIMB 11132.
[4]	"Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane." Rosenzweig A.C., Frederick C.A., Lippard S.J., Nordlund P. Nature 366:537-543(1993) [PubMed: 8255292] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[5]	"Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states." Rosenzweig A.C., Nordlund P., Takahara P.M., Frederick C.A., Lippard S.J. Chem. Biol. 2:409-418(1995) [PubMed: 9432288] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[6]	"Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions." Rosenzweig A.C., Brandstetter H., Whittington D.A., Nordlund P., Lippard S.J., Frederick C.A. Proteins 29:141-152(1997) [PubMed: 9329079] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). Strain: Bath / NCIMB 11132.
[7]	"Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site." Whittington D.A., Lippard S.J. J. Am. Chem. Soc. 123:827-838(2001) [PubMed: 11456616] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS). Strain: Bath / NCIMB 11132.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M90050 Genomic DNA. Translation: AAB62392.3.
AE017282 Genomic DNA. Translation: AAU92736.1.

PIR

JQ0702.

RefSeq

YP_113659.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FYZ	X-ray	2.15	A/B	1-527	[»]
1FZ0	X-ray	2.07	A/B	1-527	[»]
1FZ1	X-ray	1.96	A/B	1-527	[»]
1FZ2	X-ray	2.15	A/B	1-527	[»]
1FZ3	X-ray	2.03	A/B	1-527	[»]
1FZ4	X-ray	2.38	A/B	1-527	[»]
1FZ5	X-ray	2.40	A/B	1-527	[»]
1FZ6	X-ray	2.05	A/B	1-527	[»]
1FZ7	X-ray	1.96	A/B	1-527	[»]
1FZ8	X-ray	2.10	A/B	1-527	[»]
1FZ9	X-ray	2.30	A/B	1-527	[»]
1FZH	X-ray	2.60	A/B	1-527	[»]
1FZI	X-ray	3.30	A/B	1-527	[»]
1MMO	X-ray	2.20	D/E	15-526	[»]
1MTY	X-ray	1.70	D/E	15-526	[»]
1XMF	X-ray	2.32	A/B	1-527	[»]
1XMG	X-ray	2.10	A/B	1-527	[»]
1XMH	X-ray	2.32	A/B	1-527	[»]
1XU3	X-ray	2.30	A/B	1-527	[»]
1XU5	X-ray	1.96	A/B	1-527	[»]
1XVB	X-ray	1.80	A/B	1-527	[»]
1XVC	X-ray	2.00	A/B	1-527	[»]
1XVD	X-ray	2.30	A/B	1-527	[»]
1XVE	X-ray	2.40	A/B	1-527	[»]
1XVF	X-ray	2.00	A/B	1-527	[»]
1XVG	X-ray	1.96	A/B	1-527	[»]

ModBase

Search...

Genome annotation databases

GeneID

3104807.

GenomeReviews

Gene locus MCA1194 in contig AE017282_GR.

KEGG

mca:MCA1194.

NMPDR

fig|243233.4.peg.361.

TIGR

MCA1194.

Phylogenomic databases

HOGENOM

P22869.

OMA

P22869. DNRVYGA.

Enzyme and pathway databases

BioCyc

MCAP243233:MCA_1194-MON.
MetaCyc:MON-3861.

BRENDA

1.14.13.25. 2172.

Family and domain databases

InterPro

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]

ProtoNet

Search...

Entry information

Entry name

MEMA_METCA

Accession

Primary (citable) accession number: P22869
Secondary accession number(s): Q609N8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	December 7, 2004
Last modified:	June 16, 2009
This is version 77 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)