FIXN_BRADU
ID FIXN_BRADU Reviewed; 549 AA.
AC Q03073;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cytochrome c oxidase subunit 1 homolog, bacteroid;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome CBB3 subunit 1;
DE AltName: Full=Cytochrome c oxidase polypeptide I homolog;
DE AltName: Full=Heme B/copper cytochrome c oxidase subunit;
GN Name=fixN; OrderedLocusNames=blr2763;
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=USDA 110spc4;
RX PubMed=8386371; DOI=10.1073/pnas.90.8.3309;
RA Preisig O., Anthamatten D., Hennecke H.;
RT "Genes for a microaerobically induced oxidase complex in Bradyrhizobium
RT japonicum are essential for a nitrogen-fixing endosymbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3309-3313(1993).
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 -!- 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 or a
CC quinol are transferred to the bimetallic center formed by a high-spin
CC heme 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 -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:D9IA43};
CC Note=Binds 1 copper ion per subunit, denoted as copper B.
CC {ECO:0000250|UniProtKB:D9IA43};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:D9IA43};
CC Note=Binds 2 heme b groups per subunit, denoted as high- and low-spin.
CC {ECO:0000250|UniProtKB:D9IA43};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: Bacteroid (nitrogen-fixing endosymbiont).
CC -!- INDUCTION: By low oxygen levels.
CC -!- MISCELLANEOUS: This cytochrome oxidase is probably a cbb3-type.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; L07487; AAA26203.1; -; Genomic_DNA.
DR EMBL; AJ005001; CAA06279.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC48028.1; -; Genomic_DNA.
DR PIR; A47468; A47468.
DR RefSeq; NP_769403.1; NC_004463.1.
DR RefSeq; WP_011085548.1; NZ_CP011360.1.
DR AlphaFoldDB; Q03073; -.
DR SMR; Q03073; -.
DR STRING; 224911.27351020; -.
DR EnsemblBacteria; BAC48028; BAC48028; BAC48028.
DR GeneID; 64022520; -.
DR KEGG; bja:blr2763; -.
DR PATRIC; fig|224911.44.peg.2384; -.
DR eggNOG; COG3278; Bacteria.
DR HOGENOM; CLU_017702_3_4_5; -.
DR InParanoid; Q03073; -.
DR OMA; WGWQLII; -.
DR PhylomeDB; Q03073; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045278; C:plasma membrane 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; cd01661; cbb3_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; IPR004677; Cyt_c_oxidase_cbb3_su1.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR PANTHER; PTHR10422:SF29; PTHR10422:SF29; 1.
DR Pfam; PF00115; COX1; 1.
DR SUPFAM; SSF81442; SSF81442; 1.
DR TIGRFAMs; TIGR00780; ccoN; 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..549
FT /note="Cytochrome c oxidase subunit 1 homolog, bacteroid"
FT /id="PRO_0000183469"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 131
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|UniProtKB:D9IA43"
FT BINDING 280
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
FT BINDING 330
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
FT BINDING 331
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:D9IA43"
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|UniProtKB:D9IA43"
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|UniProtKB:D9IA43"
SQ SEQUENCE 549 AA; 61273 MW; EEFBB48F18C364E3 CRC64;
MSQPSISKSM TIGESGLAVV FAATAFLCVI AAAKALDAPF AFHAALSAAA SVAAVFCIVN
RYFERPAALP PAEINGRPNY NMGPIKFSSF MAMFWGIAGF LVGLIIASQL AWPALNFDLP
WISFGRLRPL HTSAVIFAFG GNVLIATSFY VVQKSCRVRL AGDLAPWFVV VGYNFFILVA
GTGYLLGVTQ SKEYAEPEWY ADLWLTIVWV VYLLVFLATI IKRKEPHIFV ANWFYLAFIV
TIAVLHLGNN PALPVSAFGS KSYVAWGGIQ DAMFQWWYGH NAVGFFLTAG FLAIMYYFIP
KRAERPIYSY RLSIIHFWAL IFLYIWAGPH HLHYTALPDW TQTLGMTFSI MLWMPSWGGM
INGLMTLSGA WDKLRTDPVL RMLVVSVAFY GMSTFEGPMM SIKVVNSLSH YTDWTIGHVH
SGALGWVGFV SFGALYCLVP WAWNRKGLYS LKLVNWHFWV ATLGIVLYIS AMWVSGILQG
LMWRAYTSLG FLEYSFIETV EAMHPFYIIR AAGGGLFLIG ALIMAYNLWM TVRVGEAEVQ
MPVALQPAE
