P22869 (MEMA_METCA) Reviewed, UniProtKB/Swiss-Prot

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 (strain ATCC 33009 / NCIMB 11132 / Bath) [Complete proteome] [HAMAP]

Taxonomic identifier

243233 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Methylococcales › Methylococcaceae › Methylococcus › Methylococcus capsulatus

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
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 metabolic process 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

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

Helix

175 – 177

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 – 257

27

Beta strand

258 – 260

3

Helix

262 – 292

31

Helix

301 – 309

9

Helix

310 – 315

6

Helix

316 – 319

4

Helix

320 – 324

5

Helix

332 – 339

8

Helix

342 – 352

11

Helix

354 – 356

3

Beta strand

357 – 360

4

Helix

366 – 375

10

Helix

379 – 392

14

Turn

393 – 396

4

Helix

398 – 400

3

Helix

405 – 410

6

Turn

419 – 421

3

Turn

427 – 429

3

Beta strand

431 – 433

3

Beta strand

437 – 441

5

Beta strand

444 – 450

7

Helix

451 – 459

9

Helix

461 – 463

3

Helix

469 – 472

4

Turn

473 – 475

3

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 [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6. Strain: ATCC 33009 / NCIMB 11132 / Bath.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33009 / NCIMB 11132 / Bath.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). Strain: ATCC 33009 / NCIMB 11132 / Bath.
[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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS). Strain: ATCC 33009 / NCIMB 11132 / Bath.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

PIR

JQ0702.

RefSeq

YP_113659.1. NC_002977.6.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
4GAM	X-ray	2.90	A/F/K/P	1-527	[»]

ProteinModelPortal

P22869.

SMR

P22869. Positions 15-526.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59861N.

STRING

243233.MCA1194.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAU92736; AAU92736; MCA1194.

GeneID

3104807.

KEGG

mca:MCA1194.

PATRIC

22606220. VBIMetCap22254_1226.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

NOG29018.

HOGENOM

HOG000076230.

KO

K16157.

OMA

VSIANDP.

ProtClustDB

CLSK819184.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-3861.

Family and domain databases

Gene3D

1.10.620.20. 1 hit.

InterPro

IPR009078. Ferritin-like_SF.
IPR003430. Phenol_Hydrox.
IPR012348. RNR-rel.
[Graphical view]

Pfam

PF02332. Phenol_Hydrox. 1 hit.
[Graphical view]

SUPFAM

SSF47240. Ferritin/RR_like. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P22869.

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:	May 1, 2013
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program