Q53563 (MMOC_METTR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Methylosinus trichosporium

Taxonomic identifier

426 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylocystaceae › Methylosinus

Protein attributes

Sequence length	340 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. 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.

Ontologies

Keywords
Biological process	Electron transport One-carbon metabolism Transport
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro metal 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 – 340	340	Methane monooxygenase component C		PRO_0000189409
Regions
	Domain	1 – 92	92	2Fe-2S ferredoxin-type
	Domain	101 – 205	105	FAD-binding FR-type
	Nucleotide binding	215 – 229	15	FAD By similarity
Sites
	Metal binding	37	1	Iron-sulfur (2Fe-2S)
	Metal binding	41	1	Iron-sulfur (2Fe-2S)
	Metal binding	44	1	Iron-sulfur (2Fe-2S)
	Metal binding	76	1	Iron-sulfur (2Fe-2S)

Sequences

	Sequence		Length	Mass (Da)
	Q53563 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 79AE21DA8079E6D8	FASTA	340	37,991
	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

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.
PIR	C48360.
3D structure databases
ProteinModelPortal	Q53563.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-3870.
Family and domain databases
Gene3D	3.10.20.30. 1 hit.
InterPro	IPR001041. 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]
Pfam	PF00970. FAD_binding_6. 1 hit. PF00111. Fer2. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00371. FPNCR. PR00410. PHEHYDRXLASE.
SUPFAM	SSF54292. Ferredoxin. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. False negative. PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MMOC_METTR

Accession

Primary (citable) accession number: Q53563

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program