COX1_CORGL
ID COX1_CORGL Reviewed; 584 AA.
AC Q79VD7; Q93HZ5; Q9AEL9;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Cytochrome c oxidase subunit 1;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome aa3 subunit 1;
DE AltName: Full=Cytochrome c oxidase polypeptide I;
GN Name=ctaD; OrderedLocusNames=Cgl2523, cg2780;
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, HEME CHARACTERIZATION, AND MASS
RP 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 -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3
CC form the functional core of the enzyme complex. CO I is the catalytic
CC subunit of the enzyme. Electrons originating in cytochrome c are
CC transferred via the copper A center of subunit 2 and heme A of subunit
CC 1 to the bimetallic center formed by heme A3 and copper B (By
CC similarity). {ECO:0000250}.
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(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC Note=Binds 1 copper B ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 2 heme groups per subunit. {ECO:0000250};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBUNIT: Associates with subunits II, III 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=64955.8; Mass_error=164.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11577165};
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; AJ306417; CAC33824.1; -; Genomic_DNA.
DR EMBL; AB052748; BAB64406.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99916.1; -; Genomic_DNA.
DR EMBL; BX927155; CAF21186.1; -; Genomic_DNA.
DR RefSeq; NP_601724.2; NC_003450.3.
DR RefSeq; WP_011015188.1; NC_006958.1.
DR PDB; 7Q21; EM; 3.00 A; D/d=1-584.
DR PDBsum; 7Q21; -.
DR AlphaFoldDB; Q79VD7; -.
DR SMR; Q79VD7; -.
DR STRING; 196627.cg2780; -.
DR TCDB; 3.D.4.4.2; the proton-translocating cytochrome oxidase (cox) superfamily.
DR KEGG; cgb:cg2780; -.
DR KEGG; cgl:Cgl2523; -.
DR PATRIC; fig|196627.13.peg.2457; -.
DR eggNOG; COG0843; Bacteria.
DR HOGENOM; CLU_011899_7_3_11; -.
DR OMA; WAMMSIG; -.
DR UniPathway; UPA00705; -.
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:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015990; P:electron transport coupled proton transport; IEA:InterPro.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR TIGRFAMs; TIGR02891; CtaD_CoxA; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Copper; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Reference proteome; Respiratory chain;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..584
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183440"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 265
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 269
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 314
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 315
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 398
FT /ligand="heme a3"
FT /ligand_id="ChEBI:CHEBI:83282"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 400
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT CROSSLNK 265..269
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
FT CONFLICT 554
FT /note="R -> S (in Ref. 2; BAB64406)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 584 AA; 65102 MW; 10492DE9D173C4E6 CRC64;
MTAVAPRVDG HVAPQRPEPT GHARKGSKAW LMMTTTDHKQ LGIMYIIMSF SFFFLGGLMA
LLIRAELFTP GLQFLSNEQF NQLFTMHGTV MLLLYGTPIV WGFANYVLPL QIGAPDVAFP
RLNAFGFWIT TVGGVAMLTG FLTPGGAADF GWTMYSPLSD AIHSPGLGSD MWIVGVGATG
IGSVASAINM LTTILCLRAP GMTMFRMPIF TWNIFVVSVL ALLIFPLLLA AALGVLYDRK
LGGHLYDPAN GGSLLWQHLF WFFGHPEVYV LALPFFGIVS EIIPVFSRKP MFGYVGLIFA
TLSIGALSMA VWAHHMFVTG AVLLPFFSFM TFLISVPTGV KFFNWVGTMW KGHITWETPM
IWSVGFMATF LFGGLTGIML ASPPLDFHLA DSYFLIAHFH YTLFGTVVFA SCAGVYFWFP
KMTGRMMDER LGKIHFWLTF VGFHGTFLIQ HWVGNMGMPR RYADYLDSDG FTIYNQISTV
FSFLLGLSVI PFIWNVFKSW RYGELVTVDD PWGYGNSLEW ATSCPPPRHN FASLPRIRSE
RPAFELHYPH MIERMRAEAH TGHHDDINAP ELGTAPALAS DSSR
