COX2_SYNY3
ID COX2_SYNY3 Reviewed; 332 AA.
AC Q06474; P77963;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 153.
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=coxB; OrderedLocusNames=slr1136;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8383492; DOI=10.1006/bbrc.1993.1177;
RA Alge D., Peschek G.A.;
RT "Identification and characterization of the ctaC (coxB) gene as part of an
RT operon encoding subunits I, II, and III of the cytochrome c oxidase
RT (cytochrome aa3) in the cyanobacterium Synechocystis PCC 6803.";
RL Biochem. Biophys. Res. Commun. 191:9-17(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8387368;
RA Alge D., Peschek G.A.;
RT "Characterization of a cta/CDE operon-like genomic region encoding subunits
RT I-III of the cytochrome c oxidase of the cyanobacterium Synechocystis PCC
RT 6803.";
RL Biochem. Mol. Biol. Int. 29:511-525(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Note=Binds a copper A center.;
CC -!- SUBCELLULAR LOCATION: Cell 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; X53746; CAA37776.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17288.1; -; Genomic_DNA.
DR PIR; S77441; S77441.
DR AlphaFoldDB; Q06474; -.
DR SMR; Q06474; -.
DR IntAct; Q06474; 2.
DR STRING; 1148.1652366; -.
DR PaxDb; Q06474; -.
DR EnsemblBacteria; BAA17288; BAA17288; BAA17288.
DR KEGG; syn:slr1136; -.
DR eggNOG; COG1622; Bacteria.
DR InParanoid; Q06474; -.
DR OMA; HYNMQMK; -.
DR PhylomeDB; Q06474; -.
DR Proteomes; UP000001425; Chromosome.
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 GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
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; 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 PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
PE 3: Inferred from homology;
KW Cell membrane; Copper; Electron transport; Membrane; Metal-binding;
KW Reference proteome; Respiratory chain; Signal; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..332
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000006065"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 214
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 249
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 253
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 257
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT CONFLICT 240..244
FT /note="STPGQ -> RHPWA (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 320..332
FT /note="QLKDQTSPVGDLL -> N (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 35917 MW; 314F15C8F8D4AD26 CRC64;
MKIPGSVITL LIGVVITVVS LWYGQNHGLM PVAASADAEK VDGIFNYMMT IATGLFLLVE
GVLVYCLIRF RRRKDDQTDG PPIEGNVPLE ILWTAIPTVI VFTLAVYSFE VYNNLGGLDP
TISRDNAGQQ MAHNHMGHMG SMGNMVAMAG DGDVALGIGL DSEEQGVNPL MVDVKGIQYA
WIFTYPETGI ISGELHAPID RPVQLNMEAG DVIHAFWIPQ LRLKQDVIPG RGSTLVFNAS
TPGQYPVICA ELCGAYHGGM KSVFYAHTPE EYDDWVAANA PAPTESMAMT LPKATTAMTP
NEYLAPYAKE MGVQTEALAQ LKDQTSPVGD LL
