COX1_WICCA
ID COX1_WICCA Reviewed; 535 AA.
AC P48868;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Cytochrome c oxidase subunit 1;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide I;
GN Name=COX1;
OS Wickerhamomyces canadensis (Yeast) (Pichia canadensis).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1156965;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21;
RX PubMed=8536312; DOI=10.1007/bf00311880;
RA Sekito T., Okamoto K., Kitano H., Yoshida K.;
RT "The complete mitochondrial DNA sequence of Hansenula wingei reveals new
RT characteristics of yeast mitochondria.";
RL Curr. Genet. 28:39-53(1995).
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:0000250|UniProtKB:P00401}.
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:0000250|UniProtKB:P00401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00401};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P00401};
CC Note=Binds 2 heme A groups non-covalently per subunit.
CC {ECO:0000250|UniProtKB:P00401};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P00401};
CC Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00401};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P00401}.
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:0000250|UniProtKB:P00401}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00401}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00401}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D31785; BAA06563.2; -; Genomic_DNA.
DR PIR; S58740; S58740.
DR RefSeq; NP_038208.1; NC_001762.1.
DR AlphaFoldDB; P48868; -.
DR SMR; P48868; -.
DR GeneID; 800565; -.
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: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:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR CDD; cd01663; Cyt_c_Oxidase_I; 1.
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 InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR033944; Cyt_c_oxase_su1_dom.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 3: Inferred from homology;
KW Calcium; Copper; Electron transport; Heme; Iron; Magnesium; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..535
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183341"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 63
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_note="low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 242
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 246
FT /ligand="O2"
FT /ligand_id="ChEBI:CHEBI:15379"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 291
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 292
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 369
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with subunit 2"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 370
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with subunit 2"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 377
FT /ligand="heme a3"
FT /ligand_id="ChEBI:CHEBI:83282"
FT /ligand_note="high-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 379
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_note="low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 442
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT CROSSLNK 242..246
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:P00401"
SQ SEQUENCE 535 AA; 59025 MW; 97F7C4EFAD1AD50A CRC64;
MYIQRWLYST NAKDIAILYF IFAIFSGVIG STMSLIIRLE LAAPGNQILH GNHQLFNVLV
VGHALLMIFF LVMPGLVGGF GNYMLPLLIG ASDMSFARLN NISFWLLPPA LVCLVASTLI
ESWAGTGWTI YPPLSGIQAH SSPSVDLGIF AIHLTSISSL LGAINFIATS YNMRTNGMSY
SKMPLFVWAI IITAVMLLLS LPVLTAGVTM LLMDRNFNTS FFEVAGGGDP VLYQHLFWFF
GHPEVYILIV PGFGIISHIV STYSKKPVFG EISMVYAMAS IAFLGFLVWS HHMYIVGLDA
DTRAYFTSST MVIAVPTGIK IFSWLATLYG GSIRLAVPML YAIAFLFLFT IGGLTGVALA
NASLDVAFHD TYYVVGHFHY VLSMGAIFSL FAGYYYWSPQ ILGLYFNERL AQIQFWLIFV
GANVIFMPMH FLGLQGMPRR IPDYPDAYAG WNYVSSIGSV IAIISLALFI YIIYDQLING
LTNKIDNKSV VYSKAPDFVE SNTIFANNSI KSASIEFLLN SPPAIHSFNT PAVQS
