COX3_CORGL
ID COX3_CORGL Reviewed; 205 AA.
AC Q9AEL8; Q79VE7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, 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;
GN Name=ctaE; OrderedLocusNames=Cgl2192, cg2406;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=11382224; DOI=10.1007/s002030100262;
RA Niebisch A., Bott M.;
RT "Molecular analysis of the cytochrome bc1-aa3 branch of the Corynebacterium
RT glutamicum respiratory chain containing an unusual diheme cytochrome c1.";
RL Arch. Microbiol. 175:282-294(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, AND MASS SPECTROMETRY.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=11577165; DOI=10.1099/00221287-147-10-2865;
RA Sakamoto J., Shibata T., Mine T., Miyahara R., Torigoe T., Noguchi S.,
RA Matsushita K., Sone N.;
RT "Cytochrome c oxidase contains an extra charged amino acid cluster in a new
RT type of respiratory chain in the amino acid-producing Gram-positive
RT bacterium Corynebacterium glutamicum.";
RL Microbiology 147:2865-2871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [5]
RP DETECTION IN A SUPERCOMPLEX WITH MENAQUINOL-CYTOCHROME C REDUCTASE
RP (CYTOCHROME BC1).
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12446663; DOI=10.1074/jbc.m210499200;
RA Niebisch A., Bott M.;
RT "Purification of a cytochrome bc1-aa3 supercomplex with quinol oxidase
RT activity from Corynebacterium glutamicum. Identification of a fourth
RT subunity of cytochrome aa3 oxidase and mutational analysis of diheme
RT cytochrome c1.";
RL J. Biol. Chem. 278:4339-4346(2003).
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 -!- SUBUNIT: Associates with subunits I, II and IV to form cytochrome c
CC oxidase. The 4 subunit cytochrome c oxidase forms a supercomplex with
CC the menaquinol-cytochrome c reductase complex (cytochrome bc1).
CC {ECO:0000269|PubMed:11577165}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- MASS SPECTROMETRY: Mass=22400.7; Mass_error=27.9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11577165};
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC {ECO:0000305}.
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DR EMBL; AJ306418; CAC33825.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99585.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20533.1; -; Genomic_DNA.
DR EMBL; AB052749; BAB64408.1; -; Genomic_DNA.
DR RefSeq; NP_601396.2; NC_003450.3.
DR RefSeq; WP_011014948.1; NC_006958.1.
DR PDB; 7Q21; EM; 3.00 A; E/e=1-205.
DR PDBsum; 7Q21; -.
DR AlphaFoldDB; Q9AEL8; -.
DR SMR; Q9AEL8; -.
DR STRING; 196627.cg2406; -.
DR TCDB; 3.D.4.4.2; the proton-translocating cytochrome oxidase (cox) superfamily.
DR KEGG; cgb:cg2406; -.
DR KEGG; cgl:Cgl2192; -.
DR PATRIC; fig|196627.13.peg.2129; -.
DR eggNOG; COG1845; Bacteria.
DR HOGENOM; CLU_044071_1_1_11; -.
DR OMA; SIYWWGS; -.
DR Proteomes; UP000000582; 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:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR Gene3D; 1.20.120.80; -; 1.
DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3.
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 membrane; Membrane; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..205
FT /note="Cytochrome c oxidase subunit 3"
FT /id="PRO_0000183880"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 205 AA; 22442 MW; 05EC548C01B45A63 CRC64;
MTSAVGNTGM AAPQRVAALN RPNMVSVGTI VFLSQELMFF AGLFAMYFVS RANGLANGSW
GEQTDHLNVP YALLITVILV SSSVTCQFGV FAAERGDVYG LRKWFLVTII LGSIFVIGQG
YEYITLVGHG LTIQSSVYGS AFFITTGFHA LHVIAGVMAF VVVLMRIHKS KFTPAQATAA
MVVSYYWHFV DVVWIGLFIT IYFIQ
