COX4_PARDE
ID COX4_PARDE Reviewed; 50 AA.
AC P77921;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cytochrome c oxidase subunit 4;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome aa3 subunit 4;
DE AltName: Full=Cytochrome c oxidase polypeptide IV;
GN Name=ctaH;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Pd 1222;
RX PubMed=9038156; DOI=10.1074/jbc.272.9.5514;
RA Witt H., Ludwig B.;
RT "Isolation, analysis, and deletion of the gene coding for subunit IV of
RT cytochrome c oxidase in Paracoccus denitrificans.";
RL J. Biol. Chem. 272:5514-5517(1997).
RN [2]
RP PROTEIN SEQUENCE OF 2-32.
RX PubMed=8068652; DOI=10.1021/bi00198a044;
RA Haltia T., Semo N., Arrondo J.L., Goni F.M., Freire E.;
RT "Thermodynamic and structural stability of cytochrome c oxidase from
RT Paracoccus denitrificans.";
RL Biochemistry 33:9731-9740(1994).
RN [3]
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 -!- FUNCTION: Not required for enzymatic activity or proton pumping of the
CC cytochrome c oxidase complex. {ECO:0000269|PubMed:9038156}.
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; Single-pass membrane
CC protein.
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DR EMBL; Y08372; CAA69659.1; -; Genomic_DNA.
DR RefSeq; WP_041529744.1; NZ_PPGA01000010.1.
DR PDB; 1QLE; X-ray; 3.00 A; D=8-50.
DR PDB; 7ATE; EM; 2.40 A; D=1-50.
DR PDB; 7ATN; EM; 2.66 A; D=1-50.
DR PDB; 7AU3; EM; 2.56 A; D=1-50.
DR PDB; 7AU6; EM; 2.40 A; D=1-50.
DR PDBsum; 1QLE; -.
DR PDBsum; 7ATE; -.
DR PDBsum; 7ATN; -.
DR PDBsum; 7AU3; -.
DR PDBsum; 7AU6; -.
DR AlphaFoldDB; P77921; -.
DR SMR; P77921; -.
DR EvolutionaryTrace; P77921; -.
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 Gene3D; 1.20.5.160; -; 1.
DR InterPro; IPR036596; Cyt-C_aa3_sf.
DR InterPro; IPR012422; Cyt_c_oxidase_su4_bac-aa3.
DR Pfam; PF07835; COX4_pro_2; 1.
DR SUPFAM; SSF81469; SSF81469; 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:8068652"
FT CHAIN 2..50
FT /note="Cytochrome c oxidase subunit 4"
FT /id="PRO_0000183904"
FT TOPO_DOM 2..17
FT /note="Cytoplasmic"
FT TRANSMEM 18..49
FT /note="Helical"
FT TOPO_DOM 50
FT /note="Periplasmic"
FT HELIX 18..49
FT /evidence="ECO:0007829|PDB:7ATE"
SQ SEQUENCE 50 AA; 5501 MW; 1D6B6674CAF5EC88 CRC64;
MASHHEITDH KHGEMDIRHQ QATFAGFIKG ATWVSILSIA VLVFLALANS