COX1_SCHPO
ID COX1_SCHPO Reviewed; 537 AA.
AC P07657;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 4.
DT 03-AUG-2022, entry version 159.
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; ORFNames=SPMIT.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD7-50;
RA Lang B.F.;
RT "The mitochondrial genome of Schizosaccharomyces pombe.";
RL (In) O'Brien S.J. (eds.);
RL Genetic Maps (6th edition), pp.3118-3119, Cold Spring Harbor Laboratory
RL Press, New York (1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 201-537.
RC STRAIN=AD7-50;
RX PubMed=6092057; DOI=10.1002/j.1460-2075.1984.tb02102.x;
RA Lang B.F.;
RT "The mitochondrial genome of the fission yeast Schizosaccharomyces pombe:
RT highly homologous introns are inserted at the same position of the
RT otherwise less conserved cox1 genes in Schizosaccharomyces pombe and
RT Aspergillus nidulans.";
RL EMBO J. 3:2129-2136(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 136-409.
RC STRAIN=EF1;
RX PubMed=3026914; DOI=10.1016/0378-1119(86)90027-2;
RA Trinkl H., Wolf K.;
RT "The mosaic cox1 gene in the mitochondrial genome of Schizosaccharomyces
RT pombe: minimal structural requirements and evolution of group I introns.";
RL Gene 45:289-297(1986).
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; X54421; CAA38284.1; -; Genomic_DNA.
DR EMBL; X00886; CAA25421.1; -; Genomic_DNA.
DR EMBL; M15671; AAB00165.1; -; Genomic_DNA.
DR EMBL; M15670; AAB00164.1; -; Genomic_DNA.
DR EMBL; M15669; AAB00164.1; JOINED; Genomic_DNA.
DR PIR; S78195; S78195.
DR RefSeq; NP_039499.1; NC_001326.1.
DR AlphaFoldDB; P07657; -.
DR SMR; P07657; -.
DR STRING; 4896.SPMIT.01.1; -.
DR MaxQB; P07657; -.
DR PaxDb; P07657; -.
DR EnsemblFungi; SPMIT.01.1; SPMIT.01.1:pep; SPMIT.01.
DR GeneID; 1669524; -.
DR KEGG; spo:ScpofMp01; -.
DR PomBase; SPMIT.01; cox1.
DR VEuPathDB; FungiDB:SPMIT.01; -.
DR eggNOG; KOG4769; Eukaryota.
DR HOGENOM; CLU_011899_7_3_1; -.
DR InParanoid; P07657; -.
DR OMA; WAMMSIG; -.
DR PhylomeDB; P07657; -.
DR UniPathway; UPA00705; -.
DR PRO; PR:P07657; -.
DR Proteomes; UP000002485; Mitochondrion.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:PomBase.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; ISO:PomBase.
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; IBA:GO_Central.
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; ISO:PomBase.
DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
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 Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..537
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183414"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 68
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 247
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 251
FT /ligand="O2"
FT /ligand_id="ChEBI:CHEBI:15379"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 296
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 297
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 375
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 376
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 383
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 385
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 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT CROSSLNK 247..251
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT CONFLICT 401
FT /note="Y -> YY (in Ref. 3; AAB00165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 59412 MW; FF4BFD284B27BBBA CRC64;
MNSWWTYVNR WIFSTNAKDI AILYLLFGLV SGIIGSVFSF IIRMELSAPG SQFLSGNGQL
YNVAISAHGI LMIFFFIIPA LFGAFGNYLV PLMIGAPDVA YPRVNNFTFW LLPPALMLLL
ISALTEEGPG GGWTVYPPLS SITSHSGPAI DLAILSLQLT GISSTLGSVN LIATMINMRA
PGLSLYQMPL FAWAIMITSI LLLLTLPVLA GGLFMLFSDR NLNTSFYAPE GGGDPVLYQH
LFWFFGHPEV YILIMPAFGV VSHIIPSLAH KPIFGKEGML WAMLSIALLG LMVWSHHLFT
VGLDVDTRAY FSAATMVIAI PTGIKIFSWL ATLTGGAIQW SRVPMLYAIG FLILFTIGGL
TGVILSNSVL DIAFHDTYFV VAHFHYVLSM GALFGLCGAY YWSPKMFGLM YNETLASIQF
WILFIGVNIV FGPQHFLGLN GMPRRIPDYP EAFVGWNFVS SIGSVISILS LFLFMYVMYD
QFTSNRVVKT NPYLIPSYFD DNVIFVNEKL GVAQSIEWLL HSPVHEHAFN TLPTKSI
