ID   OADC_BRADU              Reviewed;         288 AA.
AC   Q89JL7;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Oxaloacetate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01299};
DE            EC=4.1.1.112 {ECO:0000255|HAMAP-Rule:MF_01299};
GN   OrderedLocusNames=bll5266;
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 [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: Catalyzes the decarboxylation of oxaloacetate into pyruvate.
CC       Seems to play a role in maintaining cellular concentrations of
CC       bicarbonate and pyruvate. {ECO:0000255|HAMAP-Rule:MF_01299}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:16526; EC=4.1.1.112; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01299};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01299};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01299};
CC   -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_01299}.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Oxaloacetate decarboxylase family. {ECO:0000305}.
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DR   EMBL; BA000040; BAC50531.1; -; Genomic_DNA.
DR   RefSeq; NP_771906.1; NC_004463.1.
DR   RefSeq; WP_011088022.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89JL7; -.
DR   SMR; Q89JL7; -.
DR   STRING; 224911.27353541; -.
DR   EnsemblBacteria; BAC50531; BAC50531; BAC50531.
DR   GeneID; 64025025; -.
DR   KEGG; bja:bll5266; -.
DR   PATRIC; fig|224911.44.peg.5155; -.
DR   eggNOG; COG2513; Bacteria.
DR   HOGENOM; CLU_027389_3_2_5; -.
DR   InParanoid; Q89JL7; -.
DR   OMA; IAHACSY; -.
DR   PhylomeDB; Q89JL7; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046421; F:methylisocitrate lyase activity; IBA:GO_Central.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IBA:GO_Central.
DR   GO; GO:0042866; P:pyruvate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; -; 1.
DR   HAMAP; MF_01299; OadC; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR023687; Oxaloacetate_deCOase_bac.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   SUPFAM; SSF51621; SSF51621; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..288
FT                   /note="Oxaloacetate decarboxylase"
FT                   /id="PRO_0000364052"
FT   BINDING         47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
FT   BINDING         85
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
SQ   SEQUENCE   288 AA;  30161 MW;  C2E0C907B93D8239 CRC64;
     MAFRSRREKL RSILSGPGCI HPGSVYDAIS IRIAEDLGFP LGMFGGSVAS LAVLGDPDIT
     LITLTELAEQ MRRMSRASAL PVLVDADHGY GNALNVRRTV QELETAGAAG LTIEDTLLPA
     AFGEAKTQLI SLEEGVGKMK AALSGRSDPT LVIMGRTGAA AITSLDDTIR RAQAYEATGV
     DALFFTGIKS RAELEAVAAA THLPIVLGGA PEELNAPDYL AGQRVRIALQ GHAPIAAATQ
     AVHDTLKALR EGAPPKALKG LASAELTSRV MREAETKARG ADVLGFKK