COX2_PARDE
ID COX2_PARDE Reviewed; 298 AA.
AC P08306;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome aa3 subunit 2;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
DE AltName: Full=Oxidase aa(3) subunit 2;
DE Flags: Precursor;
GN Name=ctaC; Synonyms=coiI, ctaB;
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], PARTIAL PROTEIN SEQUENCE, AND
RP PYROGLUTAMATE FORMATION AT GLN-30.
RC STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
RX PubMed=2820725; DOI=10.1111/j.1432-1033.1987.tb13356.x;
RA Steinruecke P., Steffens G.C.M., Panskus G., Buse G., Ludwig B.;
RT "Subunit II of cytochrome c oxidase from Paracoccus denitrificans. DNA
RT sequence, gene expression and the protein.";
RL Eur. J. Biochem. 167:431-439(1987).
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=9380672; DOI=10.1073/pnas.94.20.10547;
RA Ostermeier C., Harrenga A., Ermler U., Michel H.;
RT "Structure at 2.7-A resolution of the Paracoccus denitrificans two-subunit
RT cytochrome c oxidase complexed with an antibody FV fragment.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:10547-10553(1997).
CC -!- FUNCTION: Subunits I and II form the functional core of the enzyme
CC complex. Electrons originating in cytochrome c are transferred via heme
CC a and Cu(A) to the binuclear center formed by heme a3 and Cu(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 -!- COFACTOR:
CC Name=binuclear copper center (CuA); Xref=ChEBI:CHEBI:47357;
CC Note=Binds a binuclear copper A center per subunit.;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; X05828; CAA29268.1; -; Genomic_DNA.
DR RefSeq; WP_011750547.1; NZ_PPGA01000006.1.
DR PDB; 1AR1; X-ray; 2.70 A; B=1-298.
DR PDB; 1QLE; X-ray; 3.00 A; B=30-281.
DR PDB; 3EHB; X-ray; 2.32 A; B=1-298.
DR PDB; 3HB3; X-ray; 2.25 A; B=1-298.
DR PDB; 7ATE; EM; 2.40 A; B=1-298.
DR PDB; 7ATN; EM; 2.66 A; B=1-298.
DR PDB; 7AU3; EM; 2.56 A; B=1-298.
DR PDB; 7AU6; EM; 2.40 A; B=1-298.
DR PDBsum; 1AR1; -.
DR PDBsum; 1QLE; -.
DR PDBsum; 3EHB; -.
DR PDBsum; 3HB3; -.
DR PDBsum; 7ATE; -.
DR PDBsum; 7ATN; -.
DR PDBsum; 7AU3; -.
DR PDBsum; 7AU6; -.
DR AlphaFoldDB; P08306; -.
DR SMR; P08306; -.
DR DIP; DIP-6089N; -.
DR IntAct; P08306; 1.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR TCDB; 3.D.4.6.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR ABCD; P08306; 1 sequenced antibody.
DR OMA; WSYEYTD; -.
DR BRENDA; 7.1.1.9; 3341.
DR EvolutionaryTrace; P08306; -.
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:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR045187; CcO_II.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR014222; Cyt_c_oxidase_su2.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR TIGRFAMs; TIGR02866; CoxB; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Copper;
KW Direct protein sequencing; Electron transport; Membrane; Metal-binding;
KW Pyrrolidone carboxylic acid; Respiratory chain; Signal; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..29
FT CHAIN 30..280
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000006059"
FT PROPEP 281..298
FT /note="C-terminal propeptide"
FT /id="PRO_0000006060"
FT TOPO_DOM 30..55
FT /note="Periplasmic"
FT TRANSMEM 56..88
FT /note="Helical"
FT TOPO_DOM 89..103
FT /note="Cytoplasmic"
FT TRANSMEM 104..134
FT /note="Helical"
FT TOPO_DOM 135..280
FT /note="Periplasmic"
FT BINDING 210
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT BINDING 245
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT BINDING 245
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT BINDING 247
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT BINDING 249
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT BINDING 249
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT BINDING 253
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT BINDING 256
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT MOD_RES 30
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2820725"
FT CONFLICT 160..161
FT /note="GV -> AF (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:3EHB"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 55..88
FT /evidence="ECO:0007829|PDB:3HB3"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 104..133
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:3HB3"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:3HB3"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 191..208
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:3HB3"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 265..278
FT /evidence="ECO:0007829|PDB:3HB3"
SQ SEQUENCE 298 AA; 32539 MW; 918A64A9E3B93366 CRC64;
MMAIATKRRG VAAVMSLGVA TMTAVPALAQ DVLGDLPVIG KPVNGGMNFQ PASSPLAHDQ
QWLDHFVLYI ITAVTIFVCL LLLICIVRFN RRANPVPARF THNTPIEVIW TLVPVLILVA
IGAFSLPILF RSQEMPNDPD LVIKAIGHQW YWSYEYPNDG VAFDALMLEK EALADAGYSE
DEYLLATDNP VVVPVGKKVL VQVTATDVIH AWTIPAFAVK QDAVPGRIAQ LWFSVDQEGV
YFGQCSELCG INHAYMPIVV KAVSQEKYEA WLAGAKEEFA ADASDYLPAS PVKLASAE
