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Database: UniProt
Entry: A0A124E0C0_9MYCO
LinkDB: A0A124E0C0_9MYCO
Original site: A0A124E0C0_9MYCO 
ID   A0A124E0C0_9MYCO        Unreviewed;       555 AA.
AC   A0A124E0C0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   13-SEP-2023, entry version 43.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE            EC=7.1.1.9 {ECO:0000256|RuleBase:RU363061};
GN   ORFNames=RMCB_4141 {ECO:0000313|EMBL:GAS90045.1};
OS   Mycolicibacterium brisbanense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=146020 {ECO:0000313|EMBL:GAS90045.1, ECO:0000313|Proteomes:UP000069620};
RN   [1] {ECO:0000313|EMBL:GAS90045.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM15654 {ECO:0000313|EMBL:GAS90045.1};
RA   Katahira K., Ogura Y., Gotoh Y., Hayashi T.;
RT   "Draft Genome Sequences of Five Rapidly Growing Mycobacterium Species, M.
RT   thermoresistibile, M. fortuitum subsp. acetamidolyticum, M. canariasense,
RT   M. brisbanense, and M. novocastrense.";
RL   Genome Announc. 4:e00322-16(2016).
CC   -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC       chain that catalyzes the reduction of oxygen to water. Subunits 1-3
CC       form the functional core of the enzyme complex. CO I is the catalytic
CC       subunit of the enzyme. Electrons originating in cytochrome c are
CC       transferred via the copper A center of subunit 2 and heme A of subunit
CC       1 to the bimetallic center formed by heme A3 and copper B.
CC       {ECO:0000256|ARBA:ARBA00025218, ECO:0000256|RuleBase:RU363061}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC         [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=7.1.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00029368,
CC         ECO:0000256|RuleBase:RU363061};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU363061}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363061};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU363061}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000256|RuleBase:RU000370}.
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:GAS90045.1}.
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DR   EMBL; BCSX01000038; GAS90045.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124E0C0; -.
DR   STRING; 146020.RMCB_4141; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000069620; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IEA:InterPro.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd01662; Ubiquinol_Oxidase_I; 1.
DR   Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 1.
DR   InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR   InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR   InterPro; IPR000883; Cyt_C_Oxase_1.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR   NCBIfam; TIGR02891; CtaD_CoxA; 1.
DR   PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|RuleBase:RU363061};
KW   Copper {ECO:0000256|RuleBase:RU363061};
KW   Electron transport {ECO:0000256|RuleBase:RU000370};
KW   Heme {ECO:0000256|RuleBase:RU000370}; Iron {ECO:0000256|RuleBase:RU363061};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363061};
KW   Metal-binding {ECO:0000256|RuleBase:RU363061};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000370};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000370};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU363061}; Transport {ECO:0000256|RuleBase:RU000370}.
FT   TRANSMEM        21..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        62..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        150..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        188..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        234..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        270..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        297..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        372..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        410..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        452..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   DOMAIN          3..517
FT                   /note="Cytochrome oxidase subunit I profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
SQ   SEQUENCE   555 AA;  61797 MW;  E158FC45DD67B0BC CRC64;
     MGPKGNLVYK LITTTDHKLI GIMYCVACFA FFFIGGLMAL LMRTELALPG LQFLSNEQFN
     QLFTMHGTVM LLFYATPIVF GFANLVLPLQ IGAPDVAFPR LNALSFWLFL FGALIAMGGF
     ITPGGAADFG WTAYSPLTDA IHSPGPGGDL WIMGLAVGGL GTILGGVNMV TTVVCMRAPG
     MTMFRMPVFT WNILVTSILV LIAFPILTAA LFGLAADRHL GAHIYDPANG GVLLWQHLFW
     FFGHPEVYII ALPFFGIVSE IFPVFSRKPI FGYTTLIYAT ISIAALSVAV WAHHMYATGA
     VLLPFFSFMT FLIAVPTGIK FFNWIGTMWK GQLTFETPML FSVGFLITFL LGGLSGVLLA
     SPPIDFHVTD SYFVIAHFHY VLFGTIVFAT YAGIYFWFPK MTGRLLDERL GKLHFWLTFI
     GFHTTFLVQH WLGDEGMPRR YADYLASDGF TTLNVISTIG SFILGISTLP FAWNVFKSWR
     YGEPVTVDDP WGYGNSLEWA TSCPPPRHNF TELPRIRSER PAFELHYPHM VERMRAEAHV
     GRSHHPELET ADQSS
//
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