ID COX3_PARDE Reviewed; 274 AA. AC P06030; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 10-JUN-2026, entry version 128. DE RecName: Full=Cytochrome c oxidase subunit 3; DE EC=7.1.1.9; DE AltName: Full=Cytochrome aa3 subunit 3; DE AltName: Full=Cytochrome c oxidase polypeptide III; DE AltName: Full=Oxidase aa(3) subunit 3; GN Name=ctaE; Synonyms=coiII; OS Paracoccus denitrificans. OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rhodobacterales; 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). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-144. RC STRAIN=S1657; RX PubMed=3019767; DOI=10.1016/0014-5793(86)81359-x; RA Saraste M., Raitio M., Jalli T., Peraemaa A.; RT "A gene in Paracoccus for subunit III of cytochrome oxidase."; RL FEBS Lett. 206:154-156(1986). RN [3] RP PROTEIN SEQUENCE OF 2-16. RX PubMed=2832167; DOI=10.1111/j.1432-1033.1988.tb13923.x; RA Haltia T., Puustinen A., Finel M.; RT "The Paracoccus denitrificans cytochrome aa3 has a third subunit."; RL Eur. J. Biochem. 172:543-546(1988). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=7651515; DOI=10.1038/376660a0; RA Iwata S., Ostermeier C., Ludwig B., Michel H.; RT "Structure at 2.8-A resolution of cytochrome c oxidase from Paracoccus RT denitrificans."; RL Nature 376:660-669(1995). CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(II)-[cytochrome c] + O2 + 8 H(+)(in) = 4 Fe(III)- CC [cytochrome c] + 2 H2O + 4 H(+)(out); 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 -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 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; X04406; CAA27995.1; -; Genomic_DNA. DR EMBL; X05828; CAA29272.1; -; Genomic_DNA. DR PIR; S03807; S03807. DR PDB; 1QLE; X-ray; 3.00 A; C=2-274. DR PDB; 7ATE; EM; 2.40 A; C=1-274. DR PDB; 7ATN; EM; 2.66 A; C=1-274. DR PDB; 7AU3; EM; 2.56 A; C=1-274. DR PDB; 7AU6; EM; 2.40 A; C=1-274. DR AlphaFoldDB; P06030; -. DR EMDB; EMD-11921; -. DR EMDB; EMD-11922; -. DR EMDB; EMD-11924; -. DR EMDB; EMD-11925; -. DR SMR; P06030; -. DR EvolutionaryTrace; P06030; -. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro. DR CDD; cd01665; Cyt_c_Oxidase_III; 1. DR FunFam; 1.20.120.80:FF:000002; Cytochrome c oxidase subunit 3; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 1.20.120.80; Cytochrome c oxidase, subunit III, four-helix bundle; 1. DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3. DR InterPro; IPR033945; Cyt_c_oxase_su3_dom. DR InterPro; IPR000298; Cyt_c_oxidase-like_su3. DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf. DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx. DR PANTHER; PTHR11403:SF7; CYTOCHROME C OXIDASE SUBUNIT 3; 1. DR PANTHER; PTHR11403; CYTOCHROME C OXIDASE SUBUNIT III; 1. DR Pfam; PF00510; COX3; 1. DR SUPFAM; SSF81452; Cytochrome c oxidase subunit III-like; 1. DR PROSITE; PS50253; COX3; 1. DR PDBsum; 1QLE; -. DR PDBsum; 7ATE; -. DR PDBsum; 7ATN; -. DR PDBsum; 7AU3; -. DR PDBsum; 7AU6; -. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; KW Direct protein sequencing; Membrane; Translocase; Transmembrane; KW Transmembrane helix. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2832167" FT CHAIN 2..274 FT /note="Cytochrome c oxidase subunit 3" FT /id="PRO_0000183886" FT TOPO_DOM 2..15 FT /note="Cytoplasmic" FT TRANSMEM 16..36 FT /note="Helical" FT TOPO_DOM 37..48 FT /note="Periplasmic" FT TRANSMEM 49..77 FT /note="Helical" FT TOPO_DOM 78..79 FT /note="Cytoplasmic" FT TRANSMEM 80..115 FT /note="Helical" FT TOPO_DOM 116..139 FT /note="Periplasmic" FT TRANSMEM 140..166 FT /note="Helical" FT TOPO_DOM 167..168 FT /note="Cytoplasmic" FT TRANSMEM 169..197 FT /note="Helical" FT TOPO_DOM 198..203 FT /note="Periplasmic" FT TRANSMEM 204..237 FT /note="Helical" FT TOPO_DOM 238..244 FT /note="Cytoplasmic" FT TRANSMEM 245..274 FT /note="Helical" FT HELIX 12..14 FT /evidence="ECO:0007829|PDB:7ATE" FT HELIX 17..36 FT /evidence="ECO:0007829|PDB:7ATE" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:7ATN" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:7ATE" FT HELIX 50..75 FT /evidence="ECO:0007829|PDB:7ATE" FT HELIX 81..114 FT /evidence="ECO:0007829|PDB:7ATE" FT TURN 119..123 FT /evidence="ECO:0007829|PDB:7ATE" FT HELIX 134..137 FT /evidence="ECO:0007829|PDB:7ATE" FT TURN 138..140 FT /evidence="ECO:0007829|PDB:7ATN" FT HELIX 141..161 FT /evidence="ECO:0007829|PDB:7ATE" FT HELIX 162..166 FT /evidence="ECO:0007829|PDB:7ATE" FT HELIX 169..195 FT /evidence="ECO:0007829|PDB:7ATE" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:1QLE" FT HELIX 205..237 FT /evidence="ECO:0007829|PDB:7ATE" FT HELIX 246..265 FT /evidence="ECO:0007829|PDB:7ATE" FT HELIX 266..272 FT /evidence="ECO:0007829|PDB:7ATE" SQ SEQUENCE 274 AA; 30786 MW; 082F95AF9AD4A27B CRC64; MAHVKNHDYQ ILPPSIWPFF GAIGAFVMLT GAVAWMKGIT FFGLPVEGPW MFLIGLVGVL YVMFGWWADV VNEGETGEHT PVVRIGLQYG FILFIMSEVM FFVAWFWAFI KNALYPMGPD SPIKDGVWPP EGIVTFDPWH LPLINTLILL LSGVAVTWAH HAFVLEGDRK TTINGLIVAV ILGVCFTGLQ AYEYSHAAFG LADTVYAGAF YMATGFHGAH VIIGTIFLFV CLIRLLKGQM TQKQHVGFEA AAWYWHFVDV VWLFLFVVIY IWGR //