ID COX1_PODAN Reviewed; 541 AA. AC P20681; O21208; Q35363; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 2. DT 28-JUN-2023, entry version 141. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=7.1.1.9; DE AltName: Full=Cytochrome c oxidase polypeptide I; GN Name=COI; Synonyms=CO1; OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) OS (Pleurage anserina). OG Mitochondrion. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora; OC Podospora anserina. OX NCBI_TaxID=515849; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2558809; DOI=10.1007/bf00340719; RA Cummings D.J., Michel F., McNally K.L.; RT "DNA sequence analysis of the 24.5 kilobase pair cytochrome oxidase subunit RT I mitochondrial gene from Podospora anserina: a gene with sixteen RT introns."; RL Curr. Genet. 16:381-406(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=s; RX PubMed=2357736; DOI=10.1007/bf00334517; RA Cummings D.J., McNally K.L., Domenico J.M., Matsuura E.T.; RT "The complete DNA sequence of the mitochondrial genome of Podospora RT anserina."; RL Curr. Genet. 17:375-402(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-541. RC STRAIN=s; RX PubMed=3246349; DOI=10.1016/0378-1119(88)90172-2; RA Vierny-Jamet C.; RT "Senescence in Podospora anserina: a possible role for nucleic acid RT interacting proteins suggested by the sequence analysis of a mitochondrial RT DNA region specifically amplified in senescent cultures."; RL Gene 74:387-398(1988). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-86 AND 212-242. RX PubMed=2836091; DOI=10.1007/bf00421608; RA Kueck U., Osiewacz H.D., Schmidt U., Kappelhoff B., Schulte E., Stahl U., RA Esser K.; RT "The onset of senescence is affected by DNA rearrangements of a RT discontinuous mitochondrial gene in Podospora anserina."; RL Curr. Genet. 9:373-382(1985). 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; X55026; CAA38777.1; -; Genomic_DNA. DR EMBL; M28703; AAA32001.2; -; Genomic_DNA. DR EMBL; X07119; CAA30131.1; -; Genomic_DNA. DR EMBL; X07120; CAA30131.1; JOINED; Genomic_DNA. DR EMBL; X07121; CAA30132.1; -; Genomic_DNA. DR PIR; A48327; A48327. DR RefSeq; NP_074924.1; NC_001329.3. DR AlphaFoldDB; P20681; -. DR SMR; P20681; -. DR STRING; 515849.P20681; -. DR GeneID; 802462; -. DR KEGG; pan:PoanfMp17; -. DR InParanoid; P20681; -. DR UniPathway; UPA00705; -. DR Proteomes; UP000001197; Mitochondrion. 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; 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 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..541 FT /note="Cytochrome c oxidase subunit 1" FT /id="PRO_0000183397" FT TRANSMEM 23..43 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 70..90 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 107..127 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 152..172 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 188..208 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 241..261 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 273..293 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 311..331 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 344..364 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 383..403 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 46 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 374 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 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 382 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 384 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 CROSSLNK 247..251 FT /note="1'-histidyl-3'-tyrosine (His-Tyr)" FT /evidence="ECO:0000250|UniProtKB:P00401" FT CONFLICT 23 FT /note="N -> T (in Ref. 2; no nucleotide entry and 4; FT CAA30131)" FT /evidence="ECO:0000305" FT CONFLICT 51 FT /note="S -> G (in Ref. 2; no nucleotide entry and 4; FT CAA30131)" FT /evidence="ECO:0000305" FT CONFLICT 414 FT /note="T -> I (in Ref. 3; AAA32001)" FT /evidence="ECO:0000305" SQ SEQUENCE 541 AA; 59737 MW; 06AF3D497D03DAF2 CRC64; MSGGVSLWIE RWMLSTNAKD IGNLYLIFAL FSGLLGTAFS VLIRMELSGP SVQYIADNQL YNSIITAHAL LMIFFMVMPA LIGGFGNFLL PLLVGGPDMA FPRLNNISFW LLPPSLILLV FSACIEGGAG TGWTIYPPLS GVQSHSGPSV DLAIFALHLS GVSSLLGAMN FITTIMNMRT PSIRLHKLAL FGWAVIITAV LLLLSLPVLA GAITMLLTDR NFNTSFFETA GGGDPILFQH LFWFFGHPEV YILIIPAFGI ISTTISAYSN KSVFGYIGMV YAMMSIGILG FIVWSHHMYT VGLDVDTRAY FTAATLIIAV PTGIKIFSWL ATCYGGSIRL TPSMLFALGF VFMFTIGGLS GVVLANASLD IAFHDTYYVV AHFHYVLSMG AVFAMFSGWY FWIPKMLGLN YNMTLSKVQF WILFIGVNVT FFPQHFLGLQ GMPRRISDYP DAFAGWNLIS SFGSIISVVA AWLFLYIVYL QLVEGEYAGR FPWLNPQFYT DTLQALLNRS YPSLEWALSS PPKPHAFVSL PLQSNILRSL F //