ID   OADC_PSEU5              Reviewed;         287 AA.
AC   A4VQV5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=PST_3733;
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501;
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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; CP000304; ABP81356.1; -; Genomic_DNA.
DR   RefSeq; WP_003301755.1; NC_009434.1.
DR   AlphaFoldDB; A4VQV5; -.
DR   SMR; A4VQV5; -.
DR   STRING; 379731.PST_3733; -.
DR   EnsemblBacteria; ABP81356; ABP81356; PST_3733.
DR   GeneID; 66823004; -.
DR   KEGG; psa:PST_3733; -.
DR   eggNOG; COG2513; Bacteria.
DR   HOGENOM; CLU_027389_3_2_6; -.
DR   OMA; IAHACSY; -.
DR   Proteomes; UP000000233; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:UniProt.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
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..287
FT                   /note="Oxaloacetate decarboxylase"
FT                   /id="PRO_0000364071"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
FT   BINDING         235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
SQ   SEQUENCE   287 AA;  31396 MW;  B3CDAC710EB0DD8D CRC64;
     MPRLSHHDLR RNFRELLNAD RCFHTASVFD PMSARIAADL GFEVGILGGS VASLQVLAAP
     DFNLITLSEF VEQATRICRV AQLPVLADAD HGYGNALNVM RTVSELERAG ISALTIEDTL
     LPPKFGRRST DLIGMFEAVG KIRAALEARV DPEMAIIGRT NAGVIGFEEV IARAQAYEKA
     GADAICLVGI EDFDHLESIA SQLSKPLMLV TYGNPNLRDN ARLAALGVRI VVNGHAAYFA
     AIKATYDCLR EQRQVDALDL NASQLSVKYS TADEYVVWAE EYMQVKE