ID   OADC_PSEE4              Reviewed;         289 AA.
AC   Q1I5P3;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=PSEEN4356;
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48;
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(2006).
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; CT573326; CAK17042.1; -; Genomic_DNA.
DR   RefSeq; WP_011535413.1; NC_008027.1.
DR   AlphaFoldDB; Q1I5P3; -.
DR   SMR; Q1I5P3; -.
DR   STRING; 384676.PSEEN4356; -.
DR   PRIDE; Q1I5P3; -.
DR   EnsemblBacteria; CAK17042; CAK17042; PSEEN4356.
DR   KEGG; pen:PSEEN4356; -.
DR   eggNOG; COG2513; Bacteria.
DR   HOGENOM; CLU_027389_3_2_6; -.
DR   OMA; IAHACSY; -.
DR   OrthoDB; 1485205at2; -.
DR   Proteomes; UP000000658; 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"
FT                   /id="PRO_0000364061"
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;  31460 MW;  8D30EAE3A6ED8603 CRC64;
     MPKASHHDLR FAFRELLASG SCYHTASVFD PMSARIAADL GFEVGILGGS VASLQVLAAP
     DFALITLSEF VEQATRIGRV AQLPVLADAD HGYGNALNVM RTVIELERAG VAGLTIEDTL
     LPAQFGRKST DLISVEEGVG KIRAALEARV DSALAIIART NAGVLTTEEI IVRTQSYQKA
     GADGICMVGV KDFDQLEQIA EHLSVPLMLV TYANPNLRDD ERLARLGVRV VVDGHAAYFA
     AIKATYDCLR LQRGLQHKSD SLNATELSHT YTQPEDYIRW AKEYMSVEE