COXN_BRADU
ID COXN_BRADU Reviewed; 591 AA.
AC P98000;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Alternative cytochrome c oxidase subunit 1;
DE EC=7.1.1.9;
DE AltName: Full=Alternative cytochrome c oxidase polypeptide I;
DE AltName: Full=Cytochrome BB3 subunit 1;
DE AltName: Full=Oxidase BB(3) subunit 1;
GN Name=coxN; OrderedLocusNames=bll3784;
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=1444719; DOI=10.1007/bf00245362;
RA Bott M., Preisig O., Hennecke H.;
RT "Genes for a second terminal oxidase in Bradyrhizobium japonicum.";
RL Arch. Microbiol. 158:335-343(1992).
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 are
CC transferred via the copper A center of subunit 2 and a low-spin heme of
CC subunit 1 to the bimetallic center formed by a high-spin heme and
CC 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 -!- SUBUNIT: This alternate cytochrome c oxidase consists of a subunit I
CC and two cytochromes c. Equivalents to subunit 2 and 3 are not present
CC in this complex.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: Bacteroid (nitrogen-fixing endosymbiont).
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; X68547; CAA48548.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC49049.1; -; Genomic_DNA.
DR PIR; C48364; C48364.
DR RefSeq; NP_770424.1; NC_004463.1.
DR RefSeq; WP_011086565.1; NZ_CP011360.1.
DR AlphaFoldDB; P98000; -.
DR SMR; P98000; -.
DR STRING; 224911.27352044; -.
DR EnsemblBacteria; BAC49049; BAC49049; BAC49049.
DR GeneID; 64023513; -.
DR KEGG; bja:bll3784; -.
DR PATRIC; fig|224911.44.peg.3452; -.
DR eggNOG; COG0843; Bacteria.
DR HOGENOM; CLU_011899_7_3_5; -.
DR InParanoid; P98000; -.
DR OMA; PPAHGNW; -.
DR PhylomeDB; P98000; -.
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: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:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
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 PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 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..591
FT /note="Alternative cytochrome c oxidase subunit 1"
FT /id="PRO_0000183454"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 88
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:0000305"
FT BINDING 280
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 284
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 329
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 330
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 415
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:0000305"
FT BINDING 417
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:0000305"
FT CROSSLNK 280..284
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 591 AA; 65654 MW; F58B0B43EE21903E CRC64;
MVDVPYDRIA DIPPAEVPDV ELYHPRSWWT RYVFSQDAKV IAIQYSLTAS AIGLVALVLS
WLMRLQLGFP GTFSFIDANQ YLQFITMHGM IMVIYLLTAL FLGGFGNYLI PLMVGARDMV
FPYVNMLSYW VYLLAVLVLA SAFFVPGGPT GAGWTLYPPQ AILSGTPGQD WGIVLMLSSL
ILFIIGFTMG GLNYVVTVLQ ARTRGMTLMR LPLTVWGIFT ATVMALLAFP ALFVGSVMLL
LDRLLGTSFF MPTLVEMGQL SKYGGGSPLL FQHLFWFFGH PEVYIVALPA FGIVSDLIST
HARKNIFGYR MMVWAIVAIG ALSFVVWAHH MYVSGMYPYF GFFFATTTLI IAIPTAIKVY
NWVLTLWHGD IHLTVPMLFA LGFIITFVNG GLTGLFLGNV VVDVPLSDTM FVVAHFHMVM
GVAPIMVVLG AIYHWYPKVT GRMLNDVLGK FHFWVTFLGA YLIFFPMHYL GLLGVPRRYF
ELGDAAFIPP SAHSLNAFIT VVALTVGFAQ MVFLFNLVWS LFEGEPSGGN PWRATTLEWQ
TPETPPGHGN WGKQLPIVYR WAYDYSVPGA AQDFIPQNQP PPTGAVQGVA P
