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Database: UniProt
Entry: A0A1Q2M0M4_9GAMM
LinkDB: A0A1Q2M0M4_9GAMM
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ID   A0A1Q2M0M4_9GAMM        Unreviewed;       516 AA.
AC   A0A1Q2M0M4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE            EC=7.1.1.9 {ECO:0000256|RuleBase:RU363061};
GN   ORFNames=Mag101_00230 {ECO:0000313|EMBL:AQQ66250.1};
OS   Microbulbifer agarilyticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Microbulbiferaceae; Microbulbifer.
OX   NCBI_TaxID=260552 {ECO:0000313|EMBL:AQQ66250.1, ECO:0000313|Proteomes:UP000188219};
RN   [1] {ECO:0000313|EMBL:AQQ66250.1, ECO:0000313|Proteomes:UP000188219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GP101 {ECO:0000313|EMBL:AQQ66250.1,
RC   ECO:0000313|Proteomes:UP000188219};
RA   Jung J., Bae S.S., Baek K.;
RT   "Genome of Microbulbifer agarilyticus GP101.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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|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}.
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DR   EMBL; CP019650; AQQ66250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2M0M4; -.
DR   STRING; 260552.Mag101_00230; -.
DR   KEGG; maga:Mag101_00230; -.
DR   eggNOG; COG0843; Bacteria.
DR   OrthoDB; 9803294at2; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000188219; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro.
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; cd01663; Cyt_c_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; IPR033944; Cyt_c_oxase_su1_dom.
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   Reference proteome {ECO:0000313|Proteomes:UP000188219};
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        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        65..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        147..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        187..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        247..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        277..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        302..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        342..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        376..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        415..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        456..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   DOMAIN          12..516
FT                   /note="Cytochrome oxidase subunit I profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
SQ   SEQUENCE   516 AA;  57538 MW;  EE8D7F90A026B087 CRC64;
     MAHGPKPGFT RWLYTTNHKD IGSMYLWFSF AMFLLGGCMA LVIRAELFQP GLQIVQPGFF
     NQMTTMHGLI MVFGAVMPAF VGLANWMVPM MIGAPDMALP RMNNWSFWIL PFAFAMLVST
     LFMEGGAPDF GWTFYAPLST EYAPPSVTFF IFAVHIMGAS SIMGAINIVA TILNMRAPGM
     TLMKMPLFVW TWLITAYLLI AVMPVLAGVV TMMLMDIHFG TSFFSAAGGG DPVLFQHVFW
     FFGHPEVYIM ILPAFGIVSA IIPTFARKPL FGYSSMVYAT ASIAFLSFIV WAHHMFTVGM
     PIAGELFFMY ATMLIAVPTG VKVFNWVSTM FRGSMTFETP MLFSIAFVIL FTIGGFSGLM
     LAIAPADFQY HDTYFVVAHF HYVLVPGAIF SITAGVYYWL PKWTGNMYNE SMGKVHFWLA
     FVGLNVTFFP MHFVGLAGMP RRIPDYALQF ADFNQIASVG AFLFGAAQIL FLFNVIRTVR
     GGEKATDEVW ENPEGLEWSV PSPAPYHTFS TPPVVR
//
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