MMOC_METCA
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 03-AUG-2022, entry version 164.
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; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC 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=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).
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 PDBsum; 1JQ4; -.
DR PDBsum; 1TVC; -.
DR AlphaFoldDB; P22868; -.
DR BMRB; P22868; -.
DR SMR; P22868; -.
DR STRING; 243233.MCA1200; -.
DR EnsemblBacteria; AAU92722; AAU92722; MCA1200.
DR KEGG; mca:MCA1200; -.
DR eggNOG; COG0543; Bacteria.
DR eggNOG; COG0633; Bacteria.
DR HOGENOM; CLU_003827_7_0_6; -.
DR OMA; TCMGRCE; -.
DR OrthoDB; 1834577at2; -.
DR BioCyc; MetaCyc:MON-3864; -.
DR BRENDA; 1.14.13.25; 3305.
DR EvolutionaryTrace; P22868; -.
DR Proteomes; UP000006821; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
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 DisProt; DP00379; -.
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; 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; 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; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
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
