COXM_BRADU
ID COXM_BRADU Reviewed; 277 AA.
AC P98053;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Alternative cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Alternative cytochrome c oxidase polypeptide II;
DE AltName: Full=Cytochrome BB3 subunit 2;
DE AltName: Full=Oxidase BB(3) subunit 2;
GN Name=coxM; OrderedLocusNames=bll3785;
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. Subunit 2 transfers the
CC electrons from cytochrome c via its binuclear copper A center to the
CC bimetallic center of the catalytic subunit 1.
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 -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: Bacteroid (nitrogen-fixing endosymbiont).
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; X68547; CAA48547.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC49050.1; -; Genomic_DNA.
DR PIR; B48364; B48364.
DR RefSeq; NP_770425.1; NC_004463.1.
DR RefSeq; WP_011086566.1; NZ_CP011360.1.
DR AlphaFoldDB; P98053; -.
DR SMR; P98053; -.
DR STRING; 224911.27352045; -.
DR EnsemblBacteria; BAC49050; BAC49050; BAC49050.
DR GeneID; 64023514; -.
DR KEGG; bja:bll3785; -.
DR PATRIC; fig|224911.44.peg.3453; -.
DR eggNOG; COG1622; Bacteria.
DR HOGENOM; CLU_036876_4_1_5; -.
DR InParanoid; P98053; -.
DR OMA; TYFWFTP; -.
DR PhylomeDB; P98053; -.
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:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR045187; CcO_II.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Copper; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..277
FT /note="Alternative cytochrome c oxidase subunit 2"
FT /id="PRO_0000183724"
FT TOPO_DOM 1..40
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..277
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT BINDING 190
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 225
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 229
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 233
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 31327 MW; D262ADE2233D36E1 CRC64;
MAVALILLLI AIGSVLFHLF SPWWWTPIAT NWGYIDDTIN ITFWITGFVF TAVILFMAYC
VFRFHHKEGR QAAYNPENKK LEWWLSVGTG VGVAAMLAPG LVVWHQFVTV PADATEVEIM
GQQWQWSFRL PGKDGRLGTS DVRNISPENP MGLNRDDPHG QDDVVIENGD LHLPIGKPVK
VLLRSVDVLH DFYVPEFRAK MDMVPGMVTY FWIRPIRTGT FDVLCAELCG AAHYQMRAKV
IVEAESDYHA WLEQQKTFAG LSGRNAVVRA KYNSGDD
