[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-16. STRAIN=Bath / NCIMB 11132; DOI=10.1016/0378-1119(90)90158-N; PubMed=2205538 [NCBI, ExPASy, EBI, Israel, Japan] Stainthorpe A.C., Lees V., Salmond G.P.C., Dalton H., Murrell J.C.; "The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath)."; Gene 91:27-34(1990).
[2]	SEQUENCE REVISION TO 254. McDonald I., Murrell J.C.; Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Bath / NCIMB 11132; DOI=10.1371/journal.pbio.0020303; PubMed=15383840 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath)."; PLoS Biol. 2:1616-1628(2004).
[4]	STRUCTURE BY NMR. STRAIN=Bath / NCIMB 11132; DOI=10.1021/bi015668k; PubMed=11772001 [NCBI, ExPASy, EBI, Israel, Japan] Mueller J., Lugovskoy A.A., Wagner G., Lippard S.J.; "NMR structure of the [2Fe-2S] ferredoxin domain from soluble methane monooxygenase reductase and interaction with its hydroxylase."; Biochemistry 41:42-51(2002).

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. The component C is the iron-sulfur flavoprotein of sMMO.
CATALYTIC ACTIVITY: Methane + NAD(P)H + O₂ = methanol + NAD(P)⁺ + H₂O.
COFACTOR: Binds 1 2Fe-2S cluster.
SUBUNIT: The soluble methane monooxygenase (sMMO) consists of four components A/MMOH (composed of alpha/mmoX, beta/mmoY and gamma/mmoZ), B/MMOB (mmoB), C/MMOR (mmoC) and D/MMOD (mmoD).
SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
SIMILARITY: Contains 1 FAD-binding FR-type domain.

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

M90050; AAB62391.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017282; AAU92722.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JQ0701; JQ0701.

RefSeq

YP_113665.1; -.

3D structure databases

PDB

1JQ4; NMR; -; A=1-98.	[ExPASy / RCSB / EBI]
1TVC; NMR; -; A=99-348.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

1JQ4; -.
1TVC; -.

DP00379; -.

Enzyme and pathway databases

BioCyc

MCAP243233:MCA_1200-MON; -.
MetaCyc:MON-3864; -.

Ontologies

GO:0051537;	Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0015049;	Molecular function: methane monooxygenase activity (inferred from electronic annotation from EC).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006730;	Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006058; 2Fe2S_fd_BS.
IPR012675; b-grasp_ferredoxin-like.
IPR001041; Ferredoxin.
IPR001709; FPN_cyt_redctse.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
IPR001221; Phe_hydroxylase.
Graphical view of domain structure.

Gene3D

G3DSA:3.10.20.30; Ferredoxin_fold; 1.

Pfam

PF00970; FAD_binding_6; 1.
PF00111; Fer2; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00371; FPNCR.
PR00410; PHEHYDRXLASE.

PROSITE

PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PS51384; FAD_FR; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P22868.

Genome annotation databases

GeneID

3103263; -.

GenomeReviews

AE017282_GR; MCA1200.

KEGG

mca:MCA1200; -.

NMPDR

fig|243233.4.peg.367; -.

TIGR

MCA1200; -.

Phylogenomic databases

HOGENOM

P22868; -.

Other

UniRef

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

Keywords

2Fe-2S; 3D-structure; Complete proteome; Direct protein sequencing; Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Monooxygenase; NADP; One-carbon metabolism; Oxidoreductase; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 348`	`348`	`Methane monooxygenase component C.`	`PRO_0000189408`
`DOMAIN`	`5 98`	`94`	`2Fe-2S ferredoxin-type.`
`DOMAIN`	`106 211`	`106`	`FAD-binding FR-type.`
`NP_BIND`	`221 235`	`15`	`FAD (By similarity).`
`METAL`	`42 42`		`Iron-sulfur (2Fe-2S).`
`METAL`	`47 47`		`Iron-sulfur (2Fe-2S).`
`METAL`	`50 50`		`Iron-sulfur (2Fe-2S).`
`METAL`	`82 82`		`Iron-sulfur (2Fe-2S).`
`STRAND`	`4 11`	`8`
`TURN`	`12 14`	`3`
`STRAND`	`15 23`	`9`
`HELIX`	`27 34`	`8`
`STRAND`	`54 56`	`3`
`TURN`	`66 68`	`3`
`HELIX`	`71 77`	`7`
`TURN`	`81 83`	`3`
`STRAND`	`90 93`	`4`
`STRAND`	`106 113`	`8`
`STRAND`	`117 120`	`4`
`STRAND`	`123 128`	`6`
`STRAND`	`134 138`	`5`
`STRAND`	`147 150`	`4`
`STRAND`	`156 161`	`6`
`STRAND`	`167 170`	`4`
`STRAND`	`173 177`	`5`
`STRAND`	`183 185`	`3`
`HELIX`	`186 192`	`7`
`STRAND`	`193 205`	`13`
`STRAND`	`214 216`	`3`
`STRAND`	`218 225`	`8`
`HELIX`	`228 240`	`13`
`STRAND`	`246 251`	`6`
`STRAND`	`253 255`	`3`
`HELIX`	`261 270`	`10`
`STRAND`	`271 273`	`3`
`STRAND`	`275 278`	`4`
`STRAND`	`288 295`	`8`
`HELIX`	`296 304`	`9`
`STRAND`	`305 316`	`12`
`HELIX`	`317 330`	`14`
`STRAND`	`335 339`	`5`
`STRAND`	`343 345`	`3`

Sequence information

Length: 348 AA [This is the length of the unprocessed precursor]

Molecular weight: 38542 Da [This is the MW of the unprocessed precursor]

CRC64: 7577BEB408CA1C1F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQRVHTITAV TEDGESLRFE CRSDEDVITA ALRQNIFLMS SCREGGCATC KALCSEGDYD 

        70         80         90        100        110        120 
LKGCSVQALP PEEEEEGLVL LCRTYPKTDL EIELPYTHCR ISFGEVGSFE AEVVGLNWVS 

       130        140        150        160        170        180 
SNTVQFLLQK RPDECGNRGV KFEPGQFMDL TIPGTDVSRS YSPANLPNPE GRLEFLIRVL 

       190        200        210        220        230        240 
PEGRFSDYLR NDARVGQVLS VKGPLGVFGL KERGMAPRYF VAGGTGLAPV VSMVRQMQEW 

       250        260        270        280        290        300 
TAPNETRIYF GVNTEPELFY IDELKSLERS MRNLTVKACV WHPSGDWEGE QGSPIDALRE 

       310        320        330        340 
DLESSDANPD IYLCGPPGMI DAACELVRSR GIPGEQVFFE KFLPSGAA

P22868 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