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 27-MAR-2024, entry version 168. 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 PDB; 8C8Q; EM; 3.36 A; A=1-537. DR PDB; 8Q1B; EM; 3.40 A; a=1-537. DR PDBsum; 8C8Q; -. DR PDBsum; 8Q1B; -. DR AlphaFoldDB; P07657; -. DR EMDB; EMD-18062; -. DR SMR; P07657; -. DR STRING; 284812.P07657; -. DR MaxQB; P07657; -. DR PaxDb; 4896-SPMIT-01-1; -. 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:0005751; C:mitochondrial respiratory chain complex IV; IDA:PomBase. 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:0015990; P:electron transport coupled proton transport; IBA:GO_Central. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IDA:PomBase. DR CDD; cd01663; Cyt_c_Oxidase_I; 1. 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 InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR033944; Cyt_c_oxase_su1_dom. 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. DR PROSITE; PS00077; COX1_CUB; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Copper; Electron transport; Heme; Iron; Magnesium; KW Membrane; 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 //