COX1_BRADU
ID COX1_BRADU Reviewed; 541 AA.
AC P31833;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 154.
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; Synonyms=coxA; OrderedLocusNames=blr1171;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LO;
RX PubMed=2172930; DOI=10.1093/nar/18.20.6143;
RA Gabel C., Maier R.J.;
RT "Nucleotide sequence of the coxA gene encoding subunit I of cytochrome aa3
RT of Bradyrhizobium japonicum.";
RL Nucleic Acids Res. 18:6143-6143(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RX PubMed=1965217; DOI=10.1111/j.1365-2958.1990.tb00576.x;
RA Bott M., Bolliger M., Hennecke H.;
RT "Genetic analysis of the cytochrome c-aa3 branch of the Bradyrhizobium
RT japonicum respiratory chain.";
RL Mol. Microbiol. 4:2147-2157(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RA Rossmann R., Loferer H., Rossi P., Hennecke H.;
RT "Factors involved in biogenesis of active cytochrome aa3 encoded by the
RT coxBAEFGC gene cluster from Bradyrhizobium japonicum.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RA Mueller P.;
RT "Extended sequencing of a DNA fragment of B.japonicum adjacent to the cox
RT operon.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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.
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 -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: Free in soil (not as bacteroid).
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; X54318; CAA38216.1; -; Genomic_DNA.
DR EMBL; X54800; CAA38570.1; -; Genomic_DNA.
DR EMBL; AJ242592; CAB56819.1; -; Genomic_DNA.
DR EMBL; U33883; AAF78815.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC46436.1; -; Genomic_DNA.
DR PIR; S13076; ODZJ1.
DR RefSeq; NP_767811.1; NC_004463.1.
DR RefSeq; WP_011083990.1; NZ_CP011360.1.
DR AlphaFoldDB; P31833; -.
DR SMR; P31833; -.
DR STRING; 224911.27349422; -.
DR EnsemblBacteria; BAC46436; BAC46436; BAC46436.
DR GeneID; 64021041; -.
DR KEGG; bja:blr1171; -.
DR PATRIC; fig|224911.44.peg.574; -.
DR eggNOG; COG0843; Bacteria.
DR HOGENOM; CLU_011899_7_3_5; -.
DR InParanoid; P31833; -.
DR OMA; PVDFQYH; -.
DR PhylomeDB; P31833; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000002526; 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:0045277; C:respiratory chain complex IV; IEA:InterPro.
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:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR CDD; cd01663; Cyt_c_Oxidase_I; 1.
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; IPR033944; Cyt_c_oxase_su1_dom.
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 2: Evidence at transcript level;
KW Cell membrane; Copper; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Reference proteome; Respiratory chain; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..541
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183437"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85
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 268
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 272
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 317
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 318
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 403
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 405
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 268..272
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 541 AA; 59265 MW; 08F9A69D0C90DB85 CRC64;
MATSAAAHGD HAQDHGHDEH AHPTGWRRYV YSTNHKDIGT MYLIFAVIAG VIGAAMSIAI
RAELMYPGVQ IFHETHTYNV FVTSHGLIMI FFMVMPAMIG GFGNWFVPLM IGAPDMAFPR
MNNISFWLLP ASFGLLLMST FVEGEPGANG VGAGWTMYVP LSSSGHPGPA VDFAILSLHL
AGASSILGAI NFITTIFNMR APGMTLHKMP LFVWSILVTV FLLLLSLPVL AGAITMLLTD
RNFGTTFFAP DGGGDPVLFQ HLFWFFGHPE VYILILPGFG MISQIVSTFS RKPVFGYLGM
AYAMVAIGGI GFVVWAHHMY TVGMSSATQA YFVAATMVIA VPTGVKIFSW IATMWGGSIE
FRAPMIWAVG FIFLFTVGGV TGVVLANAGV DRVLQETYYV VAHFHYVLSL GAVFAIFAGW
YYWFPKMTGY MYNETLAKAH FWVTFIGVNL VFFPQHFLGL SGMPRRYVDY PDAFAGWNLV
SSVGSYISGF GVLIFLYCVI DAFAKKVPAG DNPWGAGATT LEWTLPSPPP FHQFEVLPRV
Q
