COX3_PARDE
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 03-AUG-2022, entry version 121.
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; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; 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] + 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 -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC {ECO:0000305}.
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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 PDBsum; 1QLE; -.
DR PDBsum; 7ATE; -.
DR PDBsum; 7ATN; -.
DR PDBsum; 7AU3; -.
DR PDBsum; 7AU6; -.
DR AlphaFoldDB; P06030; -.
DR SMR; P06030; -.
DR EvolutionaryTrace; P06030; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 1.20.120.80; -; 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; PTHR11403; 1.
DR Pfam; PF00510; COX3; 1.
DR SUPFAM; SSF81452; SSF81452; 1.
DR PROSITE; PS50253; COX3; 1.
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 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 TURN 138..140
FT /evidence="ECO:0007829|PDB:7ATN"
FT HELIX 141..164
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..268
FT /evidence="ECO:0007829|PDB:7ATE"
FT TURN 269..273
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
