ID COX1_RHILE Reviewed; 538 AA. AC Q08855; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 13-SEP-2023, entry version 118. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=7.1.1.9; DE AltName: Full=Cytochrome aa3 subunit 1; DE AltName: Full=Cytochrome c oxidase polypeptide I; GN Name=ctaD; Synonyms=coxA; OS Rhizobium leguminosarum. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=384; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8117073; DOI=10.1128/aem.60.1.141-148.1994; RA Gabel C., Bittinger M.A., Maier R.J.; RT "Cytochrome aa3 gene regulation in members of the family Rhizobiaceae: RT comparison of copper and oxygen effects in Bradyrhizobium japonicum and RT Rhizobium tropici."; RL Appl. Environ. Microbiol. 60:141-148(1994). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3 CC form the functional core of the enzyme complex. CO I is the catalytic CC subunit of the enzyme. Electrons originating in cytochrome c are CC transferred via the copper A center of subunit 2 and heme A of subunit CC 1 to the bimetallic center formed by heme A3 and copper B. 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 -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- DEVELOPMENTAL STAGE: Free in soil (not as bacteroid). 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; X74341; CAA52388.1; -; Genomic_DNA. DR PIR; S36424; S36424. DR AlphaFoldDB; Q08855; -. DR SMR; Q08855; -. 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:0015990; P:electron transport coupled proton transport; IEA:InterPro. 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 InterPro; IPR014241; Cyt_c_oxidase_su1_bac. DR NCBIfam; TIGR02891; CtaD_CoxA; 1. 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 2: Evidence at transcript level; KW Cell membrane; Copper; Electron transport; Heme; Iron; Membrane; KW Metal-binding; Respiratory chain; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..538 FT /note="Cytochrome c oxidase subunit 1" FT /id="PRO_0000183447" FT TRANSMEM 37..57 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 84..104 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 121..141 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 170..190 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 208..228 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 259..279 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 291..311 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 329..349 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 362..382 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 401..421 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 438..458 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 476..496 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 8..27 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 82 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:0000305" FT BINDING 265 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000305" FT BINDING 269 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000305" FT BINDING 314 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000305" FT BINDING 315 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000305" FT BINDING 400 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:0000305" FT BINDING 402 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:0000305" FT CROSSLNK 265..269 FT /note="1'-histidyl-3'-tyrosine (His-Tyr)" FT /evidence="ECO:0000250" SQ SEQUENCE 538 AA; 59133 MW; 740C8FE6C902D9BF CRC64; MATSAAAHGE HAEDHGHDEH AHPTGWRRST NHKDIGTLYL IFAIIAGVIG AAMSLAIRAE LMYPGVEYFH NTHLYNVFVT SHGVIMIFFM VMPAMIGGFG NWFLPLMIGA PDMAFPRMNN ISFWLLPASF GLLLMSTFVE GEPGANGAGA GWTMYVPLSS SGHPGPAVDL AIFSLHIAGA SSILGAINFI TTILNMRAPG MTLHKMPLFA WSVLITAFLL LLSLPVLAGA ITMLLTDRNF GTTFFAPEGG GDPLLYQHLF WFFGHPEVYI LILPGFGMIS HIISTFSRKP VFGYIGMVYA MAAIGGLGFV VWAHHMYIVG MDLDTEAYFV SATMIIAVPT GIKIFSWIAT MWGGSIEFAT PMLWALAFIF LFTVGGVTGV VLANASLDRV LHDTYYVVAH FHYVLSLGAI FAIFAGWYYW FPKMSGYMYN ETLAEAHFWL IFIGVNLIFF PEHFLGISGM PRRYIDYPDA FAGWNLVSSI GSYISGFSVL LFIYCVYDAF AKNVPVGDNP WGAGATTLEW TLPSPPPVHE FEVLPRVE //