OADC_PSESM
ID OADC_PSESM Reviewed; 289 AA.
AC Q886Y2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=PSPTO_1443;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO54964.1; -; Genomic_DNA.
DR RefSeq; NP_791269.1; NC_004578.1.
DR RefSeq; WP_011103551.1; NC_004578.1.
DR AlphaFoldDB; Q886Y2; -.
DR SMR; Q886Y2; -.
DR STRING; 223283.PSPTO_1443; -.
DR EnsemblBacteria; AAO54964; AAO54964; PSPTO_1443.
DR GeneID; 1183080; -.
DR KEGG; pst:PSPTO_1443; -.
DR PATRIC; fig|223283.9.peg.1463; -.
DR eggNOG; COG2513; Bacteria.
DR HOGENOM; CLU_027389_3_2_6; -.
DR OMA; IAHACSY; -.
DR OrthoDB; 1485205at2; -.
DR PhylomeDB; Q886Y2; -.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0008807; F:carboxyvinyl-carboxyphosphonate phosphorylmutase activity; ISS:JCVI.
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:0017000; P:antibiotic biosynthetic process; ISS:JCVI.
DR GO; GO:0006113; P:fermentation; ISS:JCVI.
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..289
FT /note="Oxaloacetate decarboxylase"
FT /id="PRO_0000364074"
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; 31294 MW; 471050D7C4C45EDD CRC64;
MPKASHQDLR RSFRALTSSN SCFHTASVFD PMSAQIAADL GFEVGILGGS VASLQVLAAP
DFALITLSEF VEQATRIGRV AQLPVIADAD HGYGNALNVM RTVVELERAG ISALTIEDTL
LPAQFGRKST DLISTAEGVG KIRAALEARV DPEMSIFART NAAIIPVQEA ISRVQQYQAA
GADGITIVGI RDFDHLAQVS EGITVPLMLV TYGNPELHDN ARLAEMGVRV CVHGHAAYFA
AIKATYDCLR EQRQILGSES NMSATELTHT YTQPEDYVEW AKKFMNVNE
