ID A0A0H3ZGN3_9HYME Unreviewed; 254 AA.
AC A0A0H3ZGN3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 29-SEP-2021, entry version 22.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369};
DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369};
DE Flags: Fragment;
OS Anagyrus aurantifrons.
OG Mitochondrion {ECO:0000313|EMBL:AKN35051.1}.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Parasitoida; Chalcidoidea;
OC Encyrtidae; Tetracneminae; Anagyrus.
OX NCBI_TaxID=1672329 {ECO:0000313|EMBL:AKN35051.1};
RN [1] {ECO:0000313|EMBL:AKN35051.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26047349;
RA Beltra A., Addison P., Avalos J.A., Crochard D., Garcia-Mari F.,
RA Guerrieri E., Giliomee J.H., Malausa T., Navarro-Campos C., Palero F.,
RA Soto A.;
RT "Guiding Classical Biological Control of an Invasive Mealybug Using
RT Integrative Taxonomy.";
RL PLoS ONE 10:E0128685-E0128685(2015).
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
CC [Fe(III)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 -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU000369}.
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of a catalytic core of 3 subunits and
CC several supernumerary subunits. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC complex, complex III, CIII). {ECO:0000256|ARBA:ARBA00011164}.
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; KP771960; AKN35050.1; -; Genomic_DNA.
DR EMBL; KP771961; AKN35051.1; -; Genomic_DNA.
DR UniPathway; UPA00705; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 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:AKN35051.1};
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 17..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..254
FT /note="COX1"
FT /evidence="ECO:0000259|PROSITE:PS50855"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AKN35051.1"
FT NON_TER 254
FT /evidence="ECO:0000313|EMBL:AKN35051.1"
SQ SEQUENCE 254 AA; 28900 MW; D6FA560514D919F6 CRC64;
FGLVSHMICN ESMKKEVFGV MGMIYAMISI GLLGFIVWAH HMFTIGMDVD TRAYFTSATM
IIAVPTGIKI FSWLASMNGM KISFNVSNLW LLGFIFLFTL GGLTGIMLSN SSVDIVLHDT
YYVVAHFHYV LSMGAVFAIF GSFIYWFPVI FGLDLNKKYL KIQFFILFIG VNLTFFPQHF
LGLSGMPRRY SDYPDSYLCW NVLSSIGSFI SLLGTFMFFF IIWEALVSQR LVLFMKNLNN
SVEFLFSFPA SLHS
//