ID A0A2S1B712_9STRA Unreviewed; 249 AA.
AC A0A2S1B712;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 22-APR-2020, entry version 8.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369};
DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369};
DE Flags: Fragment;
GN Name=COI {ECO:0000313|EMBL:AWC68380.1};
OS Phytophthora himalsilva.
OG Mitochondrion {ECO:0000313|EMBL:AWC68380.1}.
OC Eukaryota; Sar; Stramenopiles; Oomycetes; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=928215 {ECO:0000313|EMBL:AWC68380.1};
RN [1] {ECO:0000313|EMBL:AWC68380.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ex-type CPHST BL 102 {ECO:0000313|EMBL:AWC68380.1}, and P19820
RC WPC {ECO:0000313|EMBL:AWC68380.1};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AWC68380.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ex-type CPHST BL 102 {ECO:0000313|EMBL:AWC68380.1}, and P19820
RC WPC {ECO:0000313|EMBL:AWC68380.1};
RA Abad Z.C., Bienapfl J.C., Burgess T.I., Coffey M.D., Redford A.J.;
RT "IDphy: Molecular and Morphological Identification of Phytophthora based on
RT the Types.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c]
CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-
CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|RuleBase:RU000369};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|RuleBase:RU000369}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU000369}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000256|RuleBase:RU000369}.
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DR EMBL; MH136901; AWC68380.1; -; 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:0009060; P:aerobic respiration; IEA:InterPro.
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:AWC68380.1};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW Oxidoreductase {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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..249
FT /note="COX1"
FT /evidence="ECO:0000259|PROSITE:PS50855"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AWC68380.1"
FT NON_TER 249
FT /evidence="ECO:0000313|EMBL:AWC68380.1"
SQ SEQUENCE 249 AA; 27130 MW; 0B1631979BD904B6 CRC64;
LFSTNHKDIG TLYLIFSAFA GVVGTTLSLL IRMELAQPGN QIFMGNHQLY NVIVTAHAFI
MVFFLVMPAL IGGFGNWFVP LMIGAPDMAF PRMNNISFWL LPPALLLLVS SAIVESGAGT
GWTVYPPLSS VQAHSGPSVD LAIFSLHLTG ISSLLGAINF ISTIYNMRAP GLSFHRLPLF
VWSVLITAFL LLLTLPVLAG AITMLLTDRN LNTSFYDPSG GGDPVLYQHL FWFFGHPEVY
ILILPGFGI
//