OADC_PSEMY
ID OADC_PSEMY Reviewed; 290 AA.
AC A4XQ41;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Pmen_0689;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000680; ABP83457.1; -; Genomic_DNA.
DR AlphaFoldDB; A4XQ41; -.
DR SMR; A4XQ41; -.
DR STRING; 399739.Pmen_0689; -.
DR EnsemblBacteria; ABP83457; ABP83457; Pmen_0689.
DR KEGG; pmy:Pmen_0689; -.
DR PATRIC; fig|399739.8.peg.697; -.
DR eggNOG; COG2513; Bacteria.
DR HOGENOM; CLU_027389_3_2_6; -.
DR OMA; IAHACSY; -.
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..290
FT /note="Oxaloacetate decarboxylase"
FT /id="PRO_0000364065"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
SQ SEQUENCE 290 AA; 31661 MW; 84A48A1F1C787199 CRC64;
MPILQRASHH ELRSAFRALL ASERCYHTAS VFDPMSARIA ADLDFEVGIL GGSVASLQVL
GAPDFALITL SEFVEQAARI GRVARLPVIA DADHGYGNAL NVMRTVVELE RAGVAALTIE
DTLLPAQFGR KSTDLISIEE GVGKILAALE ARVDPELSII ARTHAGVLEV DEVIRRTRAY
EAAGADGICL VGVKDFAHLE QIAAGLKVPL MLVTYGNPEL RDNQRLARLG VRIVVNGHAA
YFAAIKATYD CLREQRGAQP CDLNATELTH KYTMPEDYIL WAKEFMEVRE
