ID   COX14_BRADU             Reviewed;         666 AA.
AC   P98057;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2003, sequence version 2.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Probable cytochrome c oxidase subunit 1;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
DE   AltName: Full=Fourth terminal oxidase;
GN   OrderedLocusNames=blr2715;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8200541; DOI=10.1016/0378-1119(94)90607-6;
RA   Surpin M.A., Moshiri F., Murphy A.M., Maier R.J.;
RT   "Genetic evidence for a fourth terminal oxidase in Bradyrhizobium
RT   japonicum.";
RL   Gene 143:73-77(1994).
RN   [2]
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   -!- 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 {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; L25841; AAA26210.1; -; Genomic_DNA.
DR   EMBL; BA000040; BAC47980.1; -; Genomic_DNA.
DR   RefSeq; NP_769355.1; NC_004463.1.
DR   RefSeq; WP_011085500.1; NZ_CP011360.1.
DR   AlphaFoldDB; P98057; -.
DR   SMR; P98057; -.
DR   STRING; 224911.AAV28_10585; -.
DR   EnsemblBacteria; BAC47980; BAC47980; BAC47980.
DR   GeneID; 64022471; -.
DR   KEGG; bja:blr2715; -.
DR   PATRIC; fig|224911.44.peg.2330; -.
DR   eggNOG; COG0843; Bacteria.
DR   HOGENOM; CLU_011899_7_1_5; -.
DR   InParanoid; P98057; -.
DR   OrthoDB; 9803294at2; -.
DR   PhylomeDB; P98057; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IBA:GO_Central.
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:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:InterPro.
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; cd01662; Ubiquinol_Oxidase_I; 1.
DR   Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 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; IPR014207; Cyt_c_ubiqinol_oxidase_su1.
DR   NCBIfam; TIGR02843; CyoB; 1.
DR   PANTHER; PTHR10422:SF35; CYTOCHROME BO(3) UBIQUINOL OXIDASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   3: Inferred from homology;
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..666
FT                   /note="Probable cytochrome c oxidase subunit 1"
FT                   /id="PRO_0000183471"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        346..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        456..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        591..611
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        612..632
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         105
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="1; low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         332
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         418
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="2; high-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         420
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="1; low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        283..287
FT                   /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        204
FT                   /note="G -> D (in Ref. 1; AAA26210)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   666 AA;  74469 MW;  F04F4870CD039861 CRC64;
     MLGKLDWSAI PFDQPIPLIA GAVVLVAILA VLVWVVVKGH LPYLWHEWIT SVDHKRIGVM
     YILLASIMLL RGGSDAIMMR IQQAVAYQSQ GYLPPEHYNQ IFSAHGTIMI FFVAMPFVIG
     LMNLVVPLQL GVRDVAFPTL NSVGFWLTAT GALLVNLSLV IGEFARTGWL AFPPLSGLSY
     SPGVGVDYYA WSLQISGVGT LVAGINLVTT VLKLRTKGMN YLRMPMFCWT TLASNLLIVA
     AFPILTATLA MLLLDRYLGF HFFTNEAGGN VMMFMNLIWA WGHPEVYILV LPAFGIFSEV
     VSTFSGKALF GYRSMVLATM AICVISFMVW LHHFFTMGAG PDVNAIFGIA SMIIAVPTGV
     KIYNWLFTMY GGRIRFATPM LWAVGFMVTF IIGGLTGVLV AVPPADFMLH NSMFLVAHFH
     NVIIGGVLFG AFAGFEYWFP KAFGFRLDER WGKLAFWFTF LGFYVTFMPL YIAGMLGMTR
     RLQHYDVAAW RPWMLVAAAG MAVLTIGVIC QIMQLVVSIR NREALRDRTG DPWDGRSLEW
     ATSSPPPVFN FAFSPDVRGE DAYWDMKTHA RQQSFEHDAP EYHDIEMPRN SPTGFICAFF
     ATIMGFALIW HIWWMVILGG IGAFATFVVF AWRDHDEYVI PADEVARIDR INLEERRSLV
     SMAGVV
//