ID COX1A_PARDE Reviewed; 554 AA. AC P08305; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 03-MAY-2023, entry version 127. DE RecName: Full=Cytochrome c oxidase subunit 1-alpha; DE EC=7.1.1.9; DE AltName: Full=Cytochrome aa3 subunit 1-alpha; DE AltName: Full=Cytochrome c oxidase polypeptide I-alpha; GN Name=ctaDI; Synonyms=coi; OS Paracoccus denitrificans. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Paracoccus. OX NCBI_TaxID=266; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=S1657; RX PubMed=16453796; DOI=10.1002/j.1460-2075.1987.tb02579.x; RA Raitio M., Jalli T., Saraste M.; RT "Isolation and analysis of the genes for cytochrome c oxidase in Paracoccus RT denitrificans."; RL EMBO J. 6:2825-2833(1987). CC -!- FUNCTION: Subunit I and II form the functional core of the enzyme CC complex. Electrons originating in cytochrome c are transferred via heme CC a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). This CC cytochrome c oxidase shows proton pump activity across the membrane in CC addition to the electron transfer. 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 -!- COFACTOR: CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; CC Note=Binds 1 copper B ion per subunit.; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Note=Binds 2 heme groups per subunit.; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. 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; X05829; CAA29274.1; -; Genomic_DNA. DR PIR; S03809; S03809. DR AlphaFoldDB; P08305; -. DR SMR; P08305; -. DR UniPathway; UPA00705; -. DR GO; GO:0005886; C:plasma 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 Cell inner membrane; Cell membrane; Copper; Disulfide bond; KW Electron transport; Heme; Hydrogen ion transport; Ion transport; Iron; KW Membrane; Metal-binding; Respiratory chain; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..554 FT /note="Cytochrome c oxidase subunit 1-alpha" FT /id="PRO_0000183455" FT TRANSMEM 26..56 FT /note="Helical" FT /evidence="ECO:0000250" FT TRANSMEM 81..118 FT /note="Helical" FT /evidence="ECO:0000250" FT TRANSMEM 127..148 FT /note="Helical" FT /evidence="ECO:0000250" FT TRANSMEM 175..203 FT /note="Helical" FT /evidence="ECO:0000250" FT TRANSMEM 215..248 FT /note="Helical" FT /evidence="ECO:0000250" FT TRANSMEM 260..295 FT /note="Helical" FT /evidence="ECO:0000250" FT TRANSMEM 301..319 FT /note="Helical" FT /evidence="ECO:0000250" FT TRANSMEM 331..359 FT /note="Helical" FT /evidence="ECO:0000250" FT TRANSMEM 367..390 FT /note="Helical" FT /evidence="ECO:0000250" FT TRANSMEM 399..425 FT /note="Helical" FT /evidence="ECO:0000250" FT TRANSMEM 436..463 FT /note="Helical" FT /evidence="ECO:0000250" FT TRANSMEM 478..508 FT /note="Helical" FT /evidence="ECO:0000250" FT BINDING 91 FT /ligand="Fe(II)-heme a" FT /ligand_id="ChEBI:CHEBI:61715" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250" FT BINDING 273 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250" FT BINDING 277 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250" FT BINDING 322 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250" FT BINDING 323 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250" FT BINDING 406 FT /ligand="heme a3" FT /ligand_id="ChEBI:CHEBI:83282" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250" FT BINDING 408 FT /ligand="Fe(II)-heme a" FT /ligand_id="ChEBI:CHEBI:61715" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250" FT DISULFID 63..77 FT /evidence="ECO:0000250" FT CROSSLNK 273..277 FT /note="1'-histidyl-3'-tyrosine (His-Tyr)" FT /evidence="ECO:0000250" SQ SEQUENCE 554 AA; 62013 MW; 58AD591FBBDCE794 CRC64; MSAQISDSIE EKRGFFTRWF MSTNHKDIGV LYLFTAGLAG LISVTLTVYM RMELQHPGVQ YMCLEGMRLV ADAAAECTPN AHLWNVVVTY HGILMMFFVV IPALFGGFGN YFMPLHIGAP DMAFPRLNNL SYWLYVCGVS LAIASLLSPG GSDQPGAGVG WVLYPPLSTT EAGYAMDLAI FAVHVSGATS ILGAINIITT FLNMRAPGMT LFKVPLFAWA VFITAWMILL SLPVLAGGIT MLLMDRNFGT QFFDPAGGGD PVLYQHILWF FGHPEVYMLI LPGFGIISHV ISTFARKPIF GYLPMVLAMA AIAFLGFIVW AHHMYTAGMS LTQQTYFQMA TMTIAVPTGI KVFSWIATMW GGSIEFKTPM LWALAFLFTV GGVTGVVIAQ GSLDRVYHDT YYIVAHFHYV MSLGALFAIF AGTYYWIGKM SGRQYPEWAG QLHFWMMFIG SNLIFFPQHF LGRQGMPRRY IDYPVEFSYW NNISSIGAYI SFASFLFFIG IVFYTLFAGK PVNVPNYWNE HADTLEWTLP SPPPEHTFET LPKPEDWDRA QAHR //