ID MMOC_METCA Reviewed; 348 AA. AC P22868; Q609N2; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2001, sequence version 2. DT 02-SEP-2026, entry version 178. 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; OrderedLocusNames=MCA1200; OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Methylococcales; Methylococcaceae; Methylococcus. OX NCBI_TaxID=243233; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-16. RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath; RX PubMed=2205538; DOI=10.1016/0378-1119(90)90158-n; RA Stainthorpe A.C., Lees V., Salmond G.P.C., Dalton H., Murrell J.C.; RT "The methane monooxygenase gene cluster of Methylococcus capsulatus RT (Bath)."; RL Gene 91:27-34(1990). RN [2] RP SEQUENCE REVISION TO 254. RA McDonald I., Murrell J.C.; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath; RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303; RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S., RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E., RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J., RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L., RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H., RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R., RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.; RT "Genomic insights into methanotrophy: the complete genome sequence of RT Methylococcus capsulatus (Bath)."; RL PLoS Biol. 2:1616-1628(2004). RN [4] RP STRUCTURE BY NMR. RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath; RX PubMed=11772001; DOI=10.1021/bi015668k; RA Mueller J., Lugovskoy A.A., Wagner G., Lippard S.J.; RT "NMR structure of the [2Fe-2S] ferredoxin domain from soluble methane RT monooxygenase reductase and interaction with its hydroxylase."; RL Biochemistry 41:42-51(2002). 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=methane + NADH + O2 + H(+) = methanol + NAD(+) + H2O; 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=methane + NADPH + O2 + H(+) = methanol + NADP(+) + H2O; 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). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M90050; AAB62391.2; -; Genomic_DNA. DR EMBL; AE017282; AAU92722.1; -; Genomic_DNA. DR PIR; JQ0701; JQ0701. DR RefSeq; WP_010960487.1; NC_002977.6. DR PDB; 1JQ4; NMR; -; A=1-98. DR PDB; 1TVC; NMR; -; A=99-348. DR AlphaFoldDB; P22868; -. DR BMRB; P22868; -. DR SMR; P22868; -. DR STRING; 243233.MCA1200; -. DR GeneID; 88223487; -. DR KEGG; mca:MCA1200; -. DR eggNOG; COG0543; Bacteria. DR eggNOG; COG0633; Bacteria. DR HOGENOM; CLU_003827_7_0_6; -. DR BioCyc; MetaCyc:MONOMER-3864; -. DR BRENDA; 1.14.13.25; 3305. DR BRENDA; 1.14.18.3; 3305. DR EvolutionaryTrace; P22868; -. DR Proteomes; UP000006821; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro. DR GO; GO:0015049; F:methane monooxygenase [NAD(P)H] activity; IEA:UniProtKB-EC. DR CDD; cd00207; fer2; 1. DR CDD; cd06210; MMO_FAD_NAD_binding; 1. DR DisProt; DP00379; -. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. 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; IPR054950; MethMoxCompC. DR InterPro; IPR050415; MRET. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR NCBIfam; NF045803; MethMoxFADbindMmoC; 1. DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1. DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00111; Fer2; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00371; FPNCR. DR PRINTS; PR00410; PHEHYDRXLASE. DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PDBsum; 1JQ4; -. DR PDBsum; 1TVC; -. PE 1: Evidence at protein level; KW 2Fe-2S; 3D-structure; Direct protein sequencing; Electron transport; FAD; KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; Monooxygenase; NADP; KW One-carbon metabolism; Oxidoreductase; Reference proteome; Transport. FT CHAIN 1..348 FT /note="Methane monooxygenase component C" FT /id="PRO_0000189408" FT DOMAIN 5..98 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT DOMAIN 106..211 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716" FT BINDING 42 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT BINDING 47 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT BINDING 50 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT BINDING 82 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT BINDING 221..235 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT STRAND 4..11 FT /evidence="ECO:0007829|PDB:1JQ4" FT TURN 12..14 FT /evidence="ECO:0007829|PDB:1JQ4" FT STRAND 15..23 FT /evidence="ECO:0007829|PDB:1JQ4" FT HELIX 27..34 FT /evidence="ECO:0007829|PDB:1JQ4" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:1JQ4" FT TURN 66..68 FT /evidence="ECO:0007829|PDB:1JQ4" FT HELIX 71..77 FT /evidence="ECO:0007829|PDB:1JQ4" FT TURN 81..83 FT /evidence="ECO:0007829|PDB:1JQ4" FT STRAND 90..93 FT /evidence="ECO:0007829|PDB:1JQ4" FT STRAND 106..113 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 117..120 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 123..128 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 134..138 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 147..150 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 156..161 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 167..170 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 173..177 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 183..185 FT /evidence="ECO:0007829|PDB:1TVC" FT HELIX 186..192 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 193..205 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 214..216 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 218..225 FT /evidence="ECO:0007829|PDB:1TVC" FT HELIX 228..240 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 246..251 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:1TVC" FT HELIX 261..270 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 271..273 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 275..278 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 288..295 FT /evidence="ECO:0007829|PDB:1TVC" FT HELIX 296..304 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 305..316 FT /evidence="ECO:0007829|PDB:1TVC" FT HELIX 317..330 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 335..339 FT /evidence="ECO:0007829|PDB:1TVC" FT STRAND 343..345 FT /evidence="ECO:0007829|PDB:1TVC" SQ SEQUENCE 348 AA; 38542 MW; 7577BEB408CA1C1F CRC64; MQRVHTITAV TEDGESLRFE CRSDEDVITA ALRQNIFLMS SCREGGCATC KALCSEGDYD LKGCSVQALP PEEEEEGLVL LCRTYPKTDL EIELPYTHCR ISFGEVGSFE AEVVGLNWVS SNTVQFLLQK RPDECGNRGV KFEPGQFMDL TIPGTDVSRS YSPANLPNPE GRLEFLIRVL PEGRFSDYLR NDARVGQVLS VKGPLGVFGL KERGMAPRYF VAGGTGLAPV VSMVRQMQEW TAPNETRIYF GVNTEPELFY IDELKSLERS MRNLTVKACV WHPSGDWEGE QGSPIDALRE DLESSDANPD IYLCGPPGMI DAACELVRSR GIPGEQVFFE KFLPSGAA //