ID COX1_CERSP Reviewed; 566 AA. AC P33517; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 17-JAN-2003, sequence version 2. DT 13-SEP-2023, entry version 146. 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; OS Cereibacter sphaeroides (Rhodobacter sphaeroides). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Cereibacter. OX NCBI_TaxID=1063; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Ga; RX PubMed=1313140; DOI=10.1111/j.1365-2958.1992.tb01511.x; RA Shapleigh J.P., Gennis R.B.; RT "Cloning, sequencing and deletion from the chromosome of the gene encoding RT subunit I of the aa3-type cytochrome c oxidase of Rhodobacter RT sphaeroides."; RL Mol. Microbiol. 6:635-642(1992). RN [2] RP SEQUENCE REVISION TO 436-439 AND 518-521. RA Shapleigh J.P., Gennis R.B.; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. 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. 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 -!- INTERACTION: CC P33517; Q03736: ctaC; NbExp=3; IntAct=EBI-1034008, EBI-1033998; CC -!- SUBCELLULAR LOCATION: Cell 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; X62645; CAA44514.2; -; Genomic_DNA. DR PIR; S20534; S20534. DR RefSeq; WP_011337048.1; NZ_WSNV01000001.1. DR PDB; 1M56; X-ray; 2.30 A; A/G=1-566. DR PDB; 1M57; X-ray; 3.00 A; A/G=1-566. DR PDB; 2GSM; X-ray; 2.00 A; A/C=1-566. DR PDB; 3DTU; X-ray; 2.15 A; A/C=1-566. DR PDB; 3FYE; X-ray; 2.15 A; A/C=1-566. DR PDB; 3FYI; X-ray; 2.20 A; A/C=1-566. DR PDB; 5WEH; X-ray; 3.45 A; A/G=1-566. DR PDB; 6CI0; X-ray; 2.40 A; A/C=17-551. DR PDBsum; 1M56; -. DR PDBsum; 1M57; -. DR PDBsum; 2GSM; -. DR PDBsum; 3DTU; -. DR PDBsum; 3FYE; -. DR PDBsum; 3FYI; -. DR PDBsum; 5WEH; -. DR PDBsum; 6CI0; -. DR AlphaFoldDB; P33517; -. DR SMR; P33517; -. DR DIP; DIP-38013N; -. DR IntAct; P33517; 3. DR DrugBank; DB03619; Deoxycholic acid. DR TCDB; 3.D.4.6.2; the proton-translocating cytochrome oxidase (cox) superfamily. DR GeneID; 67445668; -. DR OMA; WAMMSIG; -. DR BRENDA; 7.1.1.9; 5383. DR UniPathway; UPA00705; -. DR EvolutionaryTrace; P33517; -. 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 1: Evidence at protein level; KW 3D-structure; Cell membrane; Copper; Electron transport; Heme; KW Hydrogen ion transport; Ion transport; Iron; Membrane; Metal-binding; KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..566 FT /note="Cytochrome c oxidase subunit 1" FT /id="PRO_0000183459" FT TRANSMEM 29..49 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 97..117 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 141..161 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 189..209 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 227..247 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 278..298 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 310..330 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 348..368 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 381..401 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 420..440 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 455..475 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 499..519 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 543..566 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 551..566 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 102 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 284 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000305" FT BINDING 288 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000305" FT BINDING 333 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000305" FT BINDING 334 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000305" FT BINDING 419 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 421 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 284..288 FT /note="1'-histidyl-3'-tyrosine (His-Tyr)" FT /evidence="ECO:0000250" FT HELIX 16..20 FT /evidence="ECO:0007829|PDB:3DTU" FT HELIX 26..55 FT /evidence="ECO:0007829|PDB:2GSM" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:2GSM" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 65..69 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 72..78 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 92..109 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 111..115 FT /evidence="ECO:0007829|PDB:2GSM" FT TURN 116..118 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 119..128 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 136..156 FT /evidence="ECO:0007829|PDB:2GSM" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:1M56" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:2GSM" FT STRAND 165..167 FT /evidence="ECO:0007829|PDB:2GSM" FT TURN 171..174 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 178..181 FT /evidence="ECO:0007829|PDB:2GSM" FT STRAND 183..185 FT /evidence="ECO:0007829|PDB:3DTU" FT HELIX 186..214 FT /evidence="ECO:0007829|PDB:2GSM" FT TURN 222..224 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 227..258 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 266..268 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 272..306 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 313..326 FT /evidence="ECO:0007829|PDB:2GSM" FT TURN 327..330 FT /evidence="ECO:0007829|PDB:5WEH" FT HELIX 331..334 FT /evidence="ECO:0007829|PDB:2GSM" FT TURN 336..339 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 342..354 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 356..370 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 379..402 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 404..410 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 414..424 FT /evidence="ECO:0007829|PDB:2GSM" FT TURN 425..427 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 428..444 FT /evidence="ECO:0007829|PDB:2GSM" FT STRAND 445..447 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 450..476 FT /evidence="ECO:0007829|PDB:2GSM" FT STRAND 480..482 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 488..490 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 491..521 FT /evidence="ECO:0007829|PDB:2GSM" FT STRAND 528..531 FT /evidence="ECO:0007829|PDB:6CI0" FT HELIX 538..541 FT /evidence="ECO:0007829|PDB:2GSM" FT HELIX 557..559 FT /evidence="ECO:0007829|PDB:1M56" SQ SEQUENCE 566 AA; 63147 MW; 65A74DBCC5C550B0 CRC64; MADAAIHGHE HDRRGFFTRW FMSTNHKDIG VLYLFTGGLV GLISVAFTVY MRMELMAPGV QFMCAEHLES GLVKGFFQSL WPSAVENCTP NGHLWNVMIT GHGILMMFFV VIPALFGGFG NYFMPLHIGA PDMAFPRMNN LSYWLYVAGT SLAVASLFAP GGNGQLGSGI GWVLYPPLST SESGYSTDLA IFAVHLSGAS SILGAINMIT TFLNMRAPGM TMHKVPLFAW SIFVTAWLIL LALPVLAGAI TMLLTDRNFG TTFFQPSGGG DPVLYQHILW FFGHPEVYII VLPAFGIVSH VIATFAKKPI FGYLPMVYAM VAIGVLGFVV WAHHMYTAGL SLTQQSYFMM ATMVIAVPTG IKIFSWIATM WGGSIELKTP MLWALGFLFL FTVGGVTGIV LSQASVDRYY HDTYYVVAHF HYVMSLGAVF GIFAGIYFWI GKMSGRQYPE WAGKLHFWMM FVGANLTFFP QHFLGRQGMP RRYIDYPEAF ATWNFVSSLG AFLSFASFLF FLGVIFYTLT RGARVTANNY WNEHADTLEW TLTSPPPEHT FEQLPKREDW ERAPAH //