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Q53563 (MMOC_METTR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismMethylosinus trichosporium
Taxonomic identifier426 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylocystaceaeMethylosinus

Protein attributes

Sequence length340 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 – 340340Methane monooxygenase component C
PRO_0000189409

Regions

Domain1 – 92922Fe-2S ferredoxin-type
Domain101 – 205105FAD-binding FR-type
Nucleotide binding215 – 22915FAD By similarity

Sites

Metal binding371Iron-sulfur (2Fe-2S)
Metal binding411Iron-sulfur (2Fe-2S)
Metal binding441Iron-sulfur (2Fe-2S)
Metal binding761Iron-sulfur (2Fe-2S)

Sequences

Sequence LengthMass (Da)Tools
Q53563 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 79AE21DA8079E6D8

FASTA34037,991
        10         20         30         40         50         60 
MYQIVIETED GETCRRMRPS EDWISRAEAE RNLLASCRAG CATCKADCTD GDYELIDVKV 

        70         80         90        100        110        120 
QAVPPDEEED GKVLLCRTFP RSDLHLLVPY TYDRISFEAI QTNWLAEILA CDRVSSNVVR 

       130        140        150        160        170        180 
LVLQRSRPMA ARISLNFVPG QFVDIEIPGT HTRRSYSMAS VAEDGQLEFI IRLLPDGAFS 

       190        200        210        220        230        240 
KFLQTEAKVG MRVDLRGPAG SFFLHDHGGR SRVFVAGGTG LSPVLSMIRQ LGKASDPSPA 

       250        260        270        280        290        300 
TLLFGVTNRE ELFYVDELKT LAQSMPTLGV RIAVVNDDGG NGVDKGTVID LLRAELEIDL 

       310        320        330        340 
LLGHARRRRR RETARSCRED HRDRCPAWRS DFLEKFLASG 

« Hide

References

[1]"The methane monooxygenase gene cluster of Methylosinus trichosporium: cloning and sequencing of the mmoC gene."
Cardy D.L.N., Laidler V., Salmond G.P.C., Murrell J.C.
Arch. Microbiol. 156:477-483(1991) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-13, CHARACTERIZATION, COMPLEX FORMATION.
Strain: OB3b.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S81887 Genomic DNA. Translation: AAB21393.1.
PIRC48360.

3D structure databases

ProteinModelPortalQ53563.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3870.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
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. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMMOC_METTR
AccessionPrimary (citable) accession number: Q53563
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families