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P22868 (MMOC_METCA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methane monooxygenase component C
EC=1.14.13.25
Alternative name(s):
Methane hydroxylase
Methane monooxygenase reductase
Short name=MMOR
Gene names
Name:mmoC
Ordered Locus Names:MCA1200
OrganismMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) [Complete proteome] [HAMAP]
Taxonomic identifier243233 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Methylococcales › Methylococcaceae › Methylococcus ›

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existenceEvidence 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. 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 structure

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).

Sequence similarities

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 FAD-binding FR-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 348348Methane monooxygenase component C
PRO_0000189408

Regions

Domain5 – 98942Fe-2S ferredoxin-type
Domain106 – 211106FAD-binding FR-type
Nucleotide binding221 – 23515FAD By similarity

Sites

Metal binding421Iron-sulfur (2Fe-2S)
Metal binding471Iron-sulfur (2Fe-2S)
Metal binding501Iron-sulfur (2Fe-2S)
Metal binding821Iron-sulfur (2Fe-2S)

Secondary structure

1 ............................................................. 348
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22868 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: 7577BEB408CA1C1F

FASTA34838,542
        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

« Hide

References

« Hide '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 1-16.
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 254.
[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. expand/collapse author list , 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]"NMR structure of the [2Fe-2S] ferredoxin domain from soluble methane monooxygenase reductase and interaction with its hydroxylase."
Mueller J., Lugovskoy A.A., Wagner G., Lippard S.J.
Biochemistry 41:42-51(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
Strain: ATCC 33009 / NCIMB 11132 / Bath.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M90050 Genomic DNA. Translation: AAB62391.2.
AE017282 Genomic DNA. Translation: AAU92722.1.
PIRJQ0701.
RefSeqYP_113665.1. NC_002977.6.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JQ4NMR-A1-98[»]
1TVCNMR-A99-348[»]
DisProtDP00379.
ProteinModelPortalP22868.
SMRP22868. Positions 1-348.
ModBaseSearch...

Protein-protein interaction databases

STRING243233.MCA1200.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU92722; AAU92722; MCA1200.
GeneID3103263.
KEGGmca:MCA1200.
PATRIC22606232. VBIMetCap22254_1232.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0543.
HOGENOMHOG000263663.
KOK16161.
OMASMLRRMA.
ProtClustDBCLSK2765706.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3864.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001221. Phe_hydroxylase.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMSSF54292. Ferredoxin. 1 hit.
SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP22868.

Entry information

Entry nameMMOC_METCA
AccessionPrimary (citable) accession number: P22868
Secondary accession number(s): Q609N2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: September 26, 2001
Last modified: May 1, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents