ID   OADC1_PSEPF             Reviewed;         289 AA.
AC   Q3KEL1;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Oxaloacetate decarboxylase 1 {ECO:0000255|HAMAP-Rule:MF_01299};
DE            EC=4.1.1.112 {ECO:0000255|HAMAP-Rule:MF_01299};
GN   OrderedLocusNames=Pfl01_2052;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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; CP000094; ABA73795.1; -; Genomic_DNA.
DR   RefSeq; WP_007956238.1; NC_007492.2.
DR   AlphaFoldDB; Q3KEL1; -.
DR   SMR; Q3KEL1; -.
DR   STRING; 205922.Pfl01_2052; -.
DR   PRIDE; Q3KEL1; -.
DR   EnsemblBacteria; ABA73795; ABA73795; Pfl01_2052.
DR   KEGG; pfo:Pfl01_2052; -.
DR   eggNOG; COG2513; Bacteria.
DR   HOGENOM; CLU_027389_3_2_6; -.
DR   OMA; IAHACSY; -.
DR   Proteomes; UP000002704; 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.
FT   CHAIN           1..289
FT                   /note="Oxaloacetate decarboxylase 1"
FT                   /id="PRO_0000364063"
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   289 AA;  31586 MW;  DE8E1B7264B7DF4A CRC64;
     MTRLSHQDLR RNFRQLLASD TCYHTASVFD PMSARIAADL GFEVGILGGS VASLQVLGAP
     DFALITLSEF AEQATRIGRV AQLPVIADAD HGYGNALNVM RTIVELERAG VAALTIEDTL
     LPAQFGRKST DLITVAEGVG KIRAALEARV DSEMAIIART NAGILPNQEI ISRTKQYQAA
     GADGICMVGI QDFDQLEQIA EHLTVPLMLV TYGNPALRDD KRLAELGVRV TIDGHGAYFA
     AIKATYDSLR EQRQIFTQAS DLSATELTHT YTQPEEYILW AKEYMSVKE