MMOC_METTR
ID MMOC_METTR Reviewed; 340 AA.
AC Q53563;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Methane monooxygenase component C;
DE EC=1.14.13.25;
DE AltName: Full=Methane hydroxylase;
DE AltName: Full=Methane monooxygenase reductase;
DE Short=MMOR;
GN Name=mmoC;
OS Methylosinus trichosporium.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylocystaceae; Methylosinus.
OX NCBI_TaxID=426;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b;
RX PubMed=1785954; DOI=10.1007/bf00245395;
RA Cardy D.L.N., Laidler V., Salmond G.P.C., Murrell J.C.;
RT "The methane monooxygenase gene cluster of Methylosinus trichosporium:
RT cloning and sequencing of the mmoC gene.";
RL Arch. Microbiol. 156:477-483(1991).
RN [2]
RP PROTEIN SEQUENCE OF 1-13, CHARACTERIZATION, AND COMPLEX FORMATION.
RC STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b;
RX PubMed=1845980; DOI=10.1016/s0021-9258(18)52470-4;
RA Fox B.G., Liu Y., Dege J.E., Lipscomb J.D.;
RT "Complex formation between the protein components of methane monooxygenase
RT from Methylosinus trichosporium OB3b. Identification of sites of component
RT interaction.";
RL J. Biol. Chem. 266:540-550(1991).
CC -!- FUNCTION: Responsible for the initial oxygenation of methane to
CC methanol in methanotrophs. It also catalyzes the monohydroxylation of a
CC variety of unactivated alkenes, alicyclic, aromatic and heterocyclic
CC compounds. The component C is the iron-sulfur flavoprotein of sMMO.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + methane + NADH + O2 = H2O + methanol + NAD(+);
CC Xref=Rhea:RHEA:13637, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16183, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.25;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + methane + NADPH + O2 = H2O + methanol + NADP(+);
CC Xref=Rhea:RHEA:13641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16183, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.25;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- SUBUNIT: The soluble methane monooxygenase (sMMO) consists of four
CC components A/MMOH (composed of alpha/MmoX, beta/MmoY and gamma/MmoZ),
CC B/MMOB (MmoB), C/MMOR (MmoC) and D/MMOD (MmoD).
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DR EMBL; S81887; AAB21393.1; -; Genomic_DNA.
DR PIR; C48360; C48360.
DR AlphaFoldDB; Q53563; -.
DR SMR; Q53563; -.
DR BioCyc; MetaCyc:MON-3870; -.
DR BRENDA; 1.14.13.25; 3322.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106317; F:methane monooxygenase NADH activity; IEA:UniProtKB-EC.
DR GO; GO:0106318; F:methane monooxygenase NADPH activity; IEA:UniProtKB-EC.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Direct protein sequencing; Electron transport; FAD; Flavoprotein;
KW Iron; Iron-sulfur; Metal-binding; Monooxygenase; NADP;
KW One-carbon metabolism; Oxidoreductase; Transport.
FT CHAIN 1..340
FT /note="Methane monooxygenase component C"
FT /id="PRO_0000189409"
FT DOMAIN 1..92
FT /note="2Fe-2S ferredoxin-type"
FT DOMAIN 101..205
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 37
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 41
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 44
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 76
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 215..229
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 37991 MW; 79AE21DA8079E6D8 CRC64;
MYQIVIETED GETCRRMRPS EDWISRAEAE RNLLASCRAG CATCKADCTD GDYELIDVKV
QAVPPDEEED GKVLLCRTFP RSDLHLLVPY TYDRISFEAI QTNWLAEILA CDRVSSNVVR
LVLQRSRPMA ARISLNFVPG QFVDIEIPGT HTRRSYSMAS VAEDGQLEFI IRLLPDGAFS
KFLQTEAKVG MRVDLRGPAG SFFLHDHGGR SRVFVAGGTG LSPVLSMIRQ LGKASDPSPA
TLLFGVTNRE ELFYVDELKT LAQSMPTLGV RIAVVNDDGG NGVDKGTVID LLRAELEIDL
LLGHARRRRR RETARSCRED HRDRCPAWRS DFLEKFLASG
