ID E6QDE9_9ZZZZ Unreviewed; 342 AA.
AC E6QDE9;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Methane monooxygenase component C (Methane hydroxylase) (Methane monooxygenase reductase) (MMOR) {ECO:0000313|EMBL:CBI05225.1};
DE EC=1.14.13.25 {ECO:0000313|EMBL:CBI05225.1};
GN Name=mmoC {ECO:0000313|EMBL:CBI05225.1};
GN ORFNames=CARN5_1254 {ECO:0000313|EMBL:CBI05225.1};
OS mine drainage metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=410659 {ECO:0000313|EMBL:CBI05225.1};
RN [1] {ECO:0000313|EMBL:CBI05225.1}
RP NUCLEOTIDE SEQUENCE.
RA Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F.,
RA Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C.,
RA Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O.,
RA Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N.,
RA Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P.,
RA Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., Medigue C.,
RA Le Paslier D.;
RT "Diversity of trophic interactions inside an arsenic-rich microbial
RT ecosystem.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CBI05225.1}.
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DR EMBL; CABP01000105; CBI05225.1; -; Genomic_DNA.
DR AlphaFoldDB; E6QDE9; -.
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 CDD; cd00207; fer2; 1.
DR CDD; cd06210; MMO_FAD_NAD_binding; 1.
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; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
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; 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.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Monooxygenase {ECO:0000313|EMBL:CBI05225.1};
KW Oxidoreductase {ECO:0000313|EMBL:CBI05225.1}.
FT DOMAIN 4..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 105..208
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 342 AA; 38376 MW; 8D0C701D34B4BBCA CRC64;
MSNYDITIHT RDRQQVSFVC SEAEDLLSTA DRENILLPSQ CRKGTCGACV ATVTAGSYHL
GEVSMEALPE QVQARGEVLL CRTYPREDLI LEAPYDYNYI RFERIPEREA EVIDVTMVAT
GTRRLLLRLQ PDEQGGAAEF EAGQFMEIQV PGSDARRAYS LANNTNWNGD LEFFITLRPG
GAFSTYLESA LVGDRLNIRG PLGTFTLREN GLRPRWFIGG GTGLVPLLSM LRRMADWGEM
LPARLYFGAR YEDELFCQEE IRQIQEKLPQ LQVKICLSRP GNHWMDYRGS VVDALRDDLG
SLAALPDLYV CGSTRLVQGV TELALNQGLP DSCLQFERFL SA
//
