ID Q7J2Z8_BRAFL Unreviewed; 515 AA.
AC Q7J2Z8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369};
DE EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949, ECO:0000256|RuleBase:RU000369};
GN Name=COI {ECO:0000313|EMBL:AAB87991.2};
GN Synonyms=COX1 {ECO:0000313|RefSeq:NP_007757.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OG Mitochondrion {ECO:0000313|EMBL:AAB87991.2,
OG ECO:0000313|RefSeq:NP_007757.1}.
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739 {ECO:0000313|EMBL:AAB87991.2};
RN [1] {ECO:0000313|EMBL:AAB87991.2, ECO:0000313|RefSeq:NP_007757.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9252184; DOI=10.1038/41460;
RA Naylor G.J., Brown W.M.;
RT "Structural biology and phylogenetic estimation.";
RL Nature 388:527-528(1997).
RN [2] {ECO:0000313|EMBL:AAB87991.2, ECO:0000313|RefSeq:NP_007757.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12064241; DOI=10.1080/106351598261030;
RA Naylor G.J., Brown W.M.;
RT "Amphioxus mitochondrial DNA, chordate phylogeny, and the limits of
RT inference based on comparisons of sequences.";
RL Syst. Biol. 47:61-76(1998).
RN [3] {ECO:0000313|EMBL:AAB87991.2, ECO:0000313|RefSeq:NP_007757.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82;
RX PubMed=10331267; DOI=10.1093/oxfordjournals.molbev.a026122;
RA Boore J.L., Daehler L.L., Brown W.M.;
RT "Complete sequence, gene arrangement, and genetic code of mitochondrial DNA
RT of the cephalochordate Branchiostoma floridae (Amphioxus).";
RL Mol. Biol. Evol. 16:410-418(1999).
RN [4] {ECO:0000313|RefSeq:NP_007757.1}
RP NUCLEOTIDE SEQUENCE.
RG NCBI Genome Project;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:BAH86342.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bf-H01 {ECO:0000313|EMBL:BAH86524.1}, Bf-H02
RC {ECO:0000313|EMBL:BAH86537.1}, Bf-H03 {ECO:0000313|EMBL:BAH86420.1},
RC Bf-H04 {ECO:0000313|EMBL:BAH86433.1}, Bf-H06
RC {ECO:0000313|EMBL:BAH86550.1}, Bf-H07 {ECO:0000313|EMBL:BAH86459.1},
RC Bf-M02 {ECO:0000313|EMBL:BAH86485.1}, Bf-M03
RC {ECO:0000313|EMBL:BAH86498.1}, Bf-M04 {ECO:0000313|EMBL:BAH86342.1},
RC Bf-M05 {ECO:0000313|EMBL:BAH86511.1}, Bf-M06
RC {ECO:0000313|EMBL:BAH86355.1}, Bf-M08 {ECO:0000313|EMBL:BAH86381.1},
RC Bf-M09 {ECO:0000313|EMBL:BAH86394.1}, and Bf-M10
RC {ECO:0000313|EMBL:BAH86407.1};
RA Takada Y., Imai T.;
RT "Branchiostoma mitochondrial DNA, complete genome.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|RefSeq:NP_007757.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC mitochondrial electron transport chain which drives oxidative
CC phosphorylation. The respiratory chain contains 3 multisubunit
CC complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC transfer electrons derived from NADH and succinate to molecular oxygen,
CC creating an electrochemical gradient over the inner membrane that
CC drives transmembrane transport and the ATP synthase. Cytochrome c
CC oxidase is the component of the respiratory chain that catalyzes the
CC reduction of oxygen to water. Electrons originating from reduced
CC cytochrome c in the intermembrane space (IMS) are transferred via the
CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC to the active site in subunit 1, a binuclear center (BNC) formed by
CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC water molecules using 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. {ECO:0000256|RuleBase:RU000369}.
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|RuleBase:RU000369};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU000369}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC inner membrane {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane
CC protein {ECO:0000256|RuleBase:RU000369}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000256|ARBA:ARBA00009578, ECO:0000256|RuleBase:RU000369}.
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DR EMBL; AF098298; AAB87991.2; -; Genomic_DNA.
DR EMBL; AB478575; BAH86342.1; -; Genomic_DNA.
DR EMBL; AB478576; BAH86355.1; -; Genomic_DNA.
DR EMBL; AB478578; BAH86381.1; -; Genomic_DNA.
DR EMBL; AB478579; BAH86394.1; -; Genomic_DNA.
DR EMBL; AB478580; BAH86407.1; -; Genomic_DNA.
DR EMBL; AB478581; BAH86420.1; -; Genomic_DNA.
DR EMBL; AB478582; BAH86433.1; -; Genomic_DNA.
DR EMBL; AB478584; BAH86459.1; -; Genomic_DNA.
DR EMBL; AB478586; BAH86485.1; -; Genomic_DNA.
DR EMBL; AB478587; BAH86498.1; -; Genomic_DNA.
DR EMBL; AB478588; BAH86511.1; -; Genomic_DNA.
DR EMBL; AB478589; BAH86524.1; -; Genomic_DNA.
DR EMBL; AB478590; BAH86537.1; -; Genomic_DNA.
DR EMBL; AB478591; BAH86550.1; -; Genomic_DNA.
DR RefSeq; NP_007757.1; NC_000834.1.
DR STRING; 7739.Q7J2Z8; -.
DR GeneID; 808726; -.
DR KEGG; bfo:808726; -.
DR CTD; 4512; -.
DR OMA; WAMMSIG; -.
DR OrthoDB; 5387269at2759; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000001554; Mitochondrion MT.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
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 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 Copper {ECO:0000256|RuleBase:RU000369};
KW Electron transport {ECO:0000256|RuleBase:RU000369};
KW Heme {ECO:0000256|RuleBase:RU000369}; Iron {ECO:0000256|RuleBase:RU000369};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369};
KW Metal-binding {ECO:0000256|RuleBase:RU000369};
KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:AAB87991.2};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW Reference proteome {ECO:0000313|Proteomes:UP000001554};
KW Respiratory chain {ECO:0000256|RuleBase:RU000369};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000369};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}.
FT TRANSMEM 16..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..512
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
SQ SEQUENCE 515 AA; 57460 MW; F915C249B0C83767 CRC64;
MYITRWLFST NHKDIGTLYF IFGAWAAMVG TAMSLLIRAE LSQPGALLGD DHLYNVIVTA
HAFVMIFFMV MPIMIGGFGN WLVPMMIGAP DMAFPRMNNM SFWMLPPSFS LLLASSAVEA
GVGTGWTVYP PLSSNIAHAG ASVDLAIFSL HLAGVSSILG AINFITTIHN MRASIEWNRV
PLFVWSIWVT AYLLLLSLPV LAGAITMLLT DRNINTTFFD PSGGGDPILY EHLFWFFGHP
EVYILILPGF GIISHIIIHY AGKLRSFGYL GMTWAMFTIG LLGFWVWAHH MFTVGMDVDT
RSYFTAATMV IAVPTGIKVF SWLATLSGSK QLKWETPLLW ALGFIFLFTV GGLTGIVLAN
SSLDIVLHDT YYVVAHFHYV LSMGAVFSIL AGLTYWFPLF TGFTLQESWT KIHFFVMFVG
VNLTFFPQHF LGLAGMPRRY SDYPDAYTIW NVISSLGSII SLGSVVFFLF ILWEAFSSQR
KAVPASHASH SAEWLMGCPP LFHTHEELPF ISKKY
//