ID A0A4Y5N1J1_9ARAC Unreviewed; 219 AA.
AC A0A4Y5N1J1;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369};
DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369};
DE Flags: Fragment;
GN Name=COI {ECO:0000313|EMBL:QCW08832.1};
OS Trite sp. 1GAB_PAK.
OG Mitochondrion {ECO:0000313|EMBL:QCW08832.1}.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Dionycha; Salticidae; Salticoida; Salticinae;
OC Trite.
OX NCBI_TaxID=2579438 {ECO:0000313|EMBL:QCW08832.1};
RN [1] {ECO:0000313|EMBL:QCW08832.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=31116764; DOI=.1371/journal.pone.0217086;
RA Ashfaq M., Blagoev G., Tahir H.M., Khan A.M., Mukhtar M.K., Akhtar S.,
RA Butt A., Mansoor S., Hebert P.D.N.;
RT "Assembling a DNA barcode reference library for the spiders (Arachnida:
RT Araneae) of Pakistan.";
RL PLoS ONE 14:e0217086-e0217086(2019).
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|ARBA:ARBA00029331};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000256|ARBA:ARBA00029331};
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: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000369}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004448,
CC 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; MK153929; QCW08428.1; -; Genomic_DNA.
DR EMBL; MK153989; QCW08488.1; -; Genomic_DNA.
DR EMBL; MK154333; QCW08832.1; -; Genomic_DNA.
DR EMBL; MK154858; QCW09357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y5N1J1; -.
DR UniPathway; UPA00705; -.
DR GO; GO:0005743; C:mitochondrial inner 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:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
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 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.
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|RuleBase:RU000369, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000369};
KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:QCW08832.1};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW Respiratory chain {ECO:0000256|RuleBase:RU000369};
KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|RuleBase:RU000369}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..219
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:QCW08832.1"
FT NON_TER 219
FT /evidence="ECO:0000313|EMBL:QCW08832.1"
SQ SEQUENCE 219 AA; 23608 MW; 059F0F1A9AED482B CRC64;
TLYLIFGAWS AMVGTAMSML IRMELGQTGS FLGNDHMYNV IVTAHAFVMI FFMVMPILIG
GFGNWLVPLM LGAPDMAFPR MNNLSFWLLP PSLFLLFVSS MAEMGVGAGW TVYPPLASIV
GHNGSSVDFA IFSLHLAGAS SIMGAINFIS TVINMRSVGM SLDSVPLFVW SVVITAVLLL
LSLPVLAGAI TMLLTDRNFN TSFFDPAGGG DPILFQHLF
//